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Volumn 58, Issue 1-2, 2011, Pages 62-87

Interpreting protein chemical shift data

Author keywords

Chemical shift; NMR; Prediction; Protein; Structure

Indexed keywords

CHEMICAL ANALYSIS; FORECASTING; NUCLEAR MAGNETIC RESONANCE; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PROTEINS; STRUCTURE (COMPOSITION);

EID: 79451469120     PISSN: 00796565     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pnmrs.2010.07.004     Document Type: Review
Times cited : (202)

References (230)
  • 1
    • 36149012226 scopus 로고
    • The dependence of a nuclear magnetic resonance frequency upon chemical compound
    • W.G. Proctor, and F.C. Yu The dependence of a nuclear magnetic resonance frequency upon chemical compound Phys. Rev. 77 1950 717
    • (1950) Phys. Rev. , vol.77 , pp. 717
    • Proctor, W.G.1    Yu, F.C.2
  • 2
    • 0000397743 scopus 로고
    • Chemical effects on nuclear-induction signals from organic compounds
    • J.T. Arnold, S.S. Dharmatti, and M.E. Packard Chemical effects on nuclear-induction signals from organic compounds J. Chem. Phys. 19 1951 507
    • (1951) J. Chem. Phys. , vol.19 , pp. 507
    • Arnold, J.T.1    Dharmatti, S.S.2    Packard, M.E.3
  • 6
    • 4444369986 scopus 로고    scopus 로고
    • Recent developments in automated structure elucidation of natural products
    • C. Steinbeck Recent developments in automated structure elucidation of natural products Nat. Prod. Rep. 21 2004 512 518
    • (2004) Nat. Prod. Rep. , vol.21 , pp. 512-518
    • Steinbeck, C.1
  • 7
    • 0014123731 scopus 로고
    • Magnetic resonance studies of macromolecules. I. Aromatic-methyl interactions and helical structure effects in lysozyme
    • H. Sternlicht, and D. Wilson Magnetic resonance studies of macromolecules. I. Aromatic-methyl interactions and helical structure effects in lysozyme Biochemistry 6 1967 2881 2892
    • (1967) Biochemistry , vol.6 , pp. 2881-2892
    • Sternlicht, H.1    Wilson, D.2
  • 8
    • 0015524293 scopus 로고
    • Molecular Zeeman effect in formamide and the proton chemical shift in poly(l-alanine)
    • H.L. Tigelaar, and W.H. Flygare Molecular Zeeman effect in formamide and the proton chemical shift in poly(l-alanine) J. Am. Chem. Soc. 94 1972 343 346
    • (1972) J. Am. Chem. Soc. , vol.94 , pp. 343-346
    • Tigelaar, H.L.1    Flygare, W.H.2
  • 11
    • 0020475314 scopus 로고
    • Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance
    • K. Wüthrich, G. Wider, G. Wagner, and W. Braun Sequential resonance assignments as a basis for determination of spatial protein structures by high resolution proton nuclear magnetic resonance J. Mol. Biol. 155 1982 311 319
    • (1982) J. Mol. Biol. , vol.155 , pp. 311-319
    • Wüthrich, K.1    Wider, G.2    Wagner, G.3    Braun, W.4
  • 12
    • 0021755426 scopus 로고
    • Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance
    • M.P. Williamson, D. Marion, and K. Wüthrich Secondary structure in the solution conformation of the proteinase inhibitor IIA from bull seminal plasma by nuclear magnetic resonance J. Mol. Biol. 173 1984 341 359
    • (1984) J. Mol. Biol. , vol.173 , pp. 341-359
    • Williamson, M.P.1    Marion, D.2    Wüthrich, K.3
  • 14
    • 0001202015 scopus 로고
    • The relationship between chemical shift and secondary structure in proteins
    • A. Pastore, and V. Saudek The relationship between chemical shift and secondary structure in proteins J. Magn. Reson. 90 1990 165 176
    • (1990) J. Magn. Reson. , vol.90 , pp. 165-176
    • Pastore, A.1    Saudek, V.2
  • 15
    • 0025328818 scopus 로고
    • Secondary-structure dependent chemical shifts in proteins
    • M.P. Williamson Secondary-structure dependent chemical shifts in proteins Biopolymers 29 1990 1428 1431
    • (1990) Biopolymers , vol.29 , pp. 1428-1431
    • Williamson, M.P.1
  • 16
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • D.S. Wishart, B.D. Sykes, and F.M. Richards Relationship between nuclear magnetic resonance chemical shift and protein secondary structure J. Mol. Biol. 222 1991 311 333
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 17
    • 0347610773 scopus 로고
    • 13C nuclear magnetic resonance chemical shifts
    • 13C nuclear magnetic resonance chemical shifts J. Am. Chem. Soc. 113 1991 5490 5492
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 5490-5492
    • Spera, S.1    Bax, A.2
  • 18
    • 0019330572 scopus 로고
    • Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution
    • S.J. Perkins, and R.A. Dwek Comparisons of ring-current shifts calculated from the crystal structure of egg white lysozyme of hen with the proton nuclear magnetic resonance spectrum of lysozyme in solution Biochemistry 19 1980 245 258
    • (1980) Biochemistry , vol.19 , pp. 245-258
    • Perkins, S.J.1    Dwek, R.A.2
  • 19
    • 0000865993 scopus 로고
    • A new analysis of proton chemical shifts in proteins
    • K. Osapay, and D.A. Case A new analysis of proton chemical shifts in proteins J. Am. Chem. Soc. 113 1991 9436 9444
    • (1991) J. Am. Chem. Soc. , vol.113 , pp. 9436-9444
    • Osapay, K.1    Case, D.A.2
  • 20
    • 0033626528 scopus 로고    scopus 로고
    • C-13 NMR chemical shifts can predict disulfide bond formation
    • D. Sharma, and K. Rajarathnam C-13 NMR chemical shifts can predict disulfide bond formation J. Biomol. NMR 18 2000 165 171
    • (2000) J. Biomol. NMR , vol.18 , pp. 165-171
    • Sharma, D.1    Rajarathnam, K.2
  • 21
    • 33645037915 scopus 로고    scopus 로고
    • Predicting the redox state and secondary structure of cysteine residues in proteins using NMR chemical shifts
    • C.C. Wang, J.H. Chen, S.H. Yin, and W.J. Chuang Predicting the redox state and secondary structure of cysteine residues in proteins using NMR chemical shifts Proteins 63 2006 219 226
    • (2006) Proteins , vol.63 , pp. 219-226
    • Wang, C.C.1    Chen, J.H.2    Yin, S.H.3    Chuang, W.J.4
  • 22
    • 66149144387 scopus 로고    scopus 로고
    • Relationship between chemical shift value and accessible surface area for all amino acid atoms
    • W.F. Vranken, and W. Rieping Relationship between chemical shift value and accessible surface area for all amino acid atoms BMC Struct. Biol. 9 2009 20
    • (2009) BMC Struct. Biol. , vol.9 , pp. 20
    • Vranken, W.F.1    Rieping, W.2
  • 23
    • 10644250720 scopus 로고    scopus 로고
    • Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure
    • F. Avbelj, D. Kocjan, and R.L. Baldwin Protein chemical shifts arising from alpha-helices and beta-sheets depend on solvent exposure Proc. Natl. Acad. Sci. USA 101 2004 17394 17397
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 17394-17397
    • Avbelj, F.1    Kocjan, D.2    Baldwin, R.L.3
  • 24
    • 27544456339 scopus 로고    scopus 로고
    • A simple method to predict protein flexibility using secondary chemical shifts
    • M.V. Berjanskii, and D.S. Wishart A simple method to predict protein flexibility using secondary chemical shifts J. Am. Chem. Soc. 127 2005 14970 14971
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 14970-14971
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 25
    • 0025943469 scopus 로고
    • Simple techniques for the quantification of protein secondary structure by H-1 NMR spectroscopy
    • D.S. Wishart, B.D. Sykes, and F.M. Richards Simple techniques for the quantification of protein secondary structure by H-1 NMR spectroscopy FEBS Lett. 293 1991 72 80
    • (1991) FEBS Lett. , vol.293 , pp. 72-80
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 26
    • 0028673594 scopus 로고
    • Chemical shifts as a tool for structure determination
    • D.S. Wishart, and B.D. Sykes Chemical shifts as a tool for structure determination Meth. Enzym. 239 1994 363 392
    • (1994) Meth. Enzym. , vol.239 , pp. 363-392
    • Wishart, D.S.1    Sykes, B.D.2
  • 27
    • 0032454094 scopus 로고    scopus 로고
    • Protein chemical shift analysis: A practical guide
    • D.S. Wishart, and A.M. Nip Protein chemical shift analysis: a practical guide Biochem. Cell Biol. 76 1998 153 163
    • (1998) Biochem. Cell Biol. , vol.76 , pp. 153-163
    • Wishart, D.S.1    Nip, A.M.2
  • 28
    • 0033003335 scopus 로고    scopus 로고
    • Protein backbone angle restraints from searching a database for chemical shift and sequence homology
    • G. Cornilescu, F. Delaglio, and A. Bax Protein backbone angle restraints from searching a database for chemical shift and sequence homology J. Biomol. NMR 13 1999 289 302
    • (1999) J. Biomol. NMR , vol.13 , pp. 289-302
    • Cornilescu, G.1    Delaglio, F.2    Bax, A.3
  • 29
    • 0034031647 scopus 로고    scopus 로고
    • Interpretation of chemical shifts and coupling constants in macromolecules
    • D.A. Case Interpretation of chemical shifts and coupling constants in macromolecules Curr. Opin. Struct. Biol. 10 2000 197 203
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , pp. 197-203
    • Case, D.A.1
  • 30
    • 0034923356 scopus 로고    scopus 로고
    • Use of chemical shifts in macromolecular structure determination
    • D.S. Wishart, and D.A. Case Use of chemical shifts in macromolecular structure determination Meth. Enzym. 338 2001 3 34
    • (2001) Meth. Enzym. , vol.338 , pp. 3-34
    • Wishart, D.S.1    Case, D.A.2
  • 35
    • 41149110741 scopus 로고    scopus 로고
    • 13C(alpha) chemical shifts to determine, refine, and validate protein structures
    • 13C(alpha) chemical shifts to determine, refine, and validate protein structures Proteins 71 2008 641 654
    • (2008) Proteins , vol.71 , pp. 641-654
    • Vila, J.A.1    Scheraga, H.A.2
  • 37
    • 63049100192 scopus 로고    scopus 로고
    • Characterization of protein secondary structure from NMR chemical shifts
    • S.P. Mielke, and V.V. Krishnan Characterization of protein secondary structure from NMR chemical shifts Prog. Nucl. Magn. Reson. Spectrosc. 54 2009 141 165
    • (2009) Prog. Nucl. Magn. Reson. Spectrosc. , vol.54 , pp. 141-165
    • Mielke, S.P.1    Krishnan, V.V.2
  • 38
    • 75749113781 scopus 로고    scopus 로고
    • NMR chemical shift data and ab initio shielding calculations: Emerging tools for protein structure determination
    • F.A. Mulder, and M. Filatov NMR chemical shift data and ab initio shielding calculations: emerging tools for protein structure determination Chem. Soc. Rev. 39 2010 578 590
    • (2010) Chem. Soc. Rev. , vol.39 , pp. 578-590
    • Mulder, F.A.1    Filatov, M.2
  • 39
    • 0024239356 scopus 로고
    • Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry
    • A.D. Kline, W. Braun, and K. Wüthrich Determination of the complete three-dimensional structure of the alpha-amylase inhibitor tendamistat in aqueous solution by nuclear magnetic resonance and distance geometry J. Mol. Biol. 204 1988 675 724
    • (1988) J. Mol. Biol. , vol.204 , pp. 675-724
    • Kline, A.D.1    Braun, W.2    Wüthrich, K.3
  • 40
    • 0026597879 scopus 로고
    • The chemical shift index - A fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • D.S. Wishart, B.D. Sykes, and F.M. Richards The chemical shift index - a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy Biochemistry 31 1992 1647 1651
    • (1992) Biochemistry , vol.31 , pp. 1647-1651
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3
  • 41
    • 0028393784 scopus 로고
    • The C-13 chemical-shift index - A simple method for the identification of protein secondary structure using C-13 chemical-shift data
    • D.S. Wishart, and B.D. Sykes The C-13 chemical-shift index - a simple method for the identification of protein secondary structure using C-13 chemical-shift data J. Biomol. NMR 4 1994 171 180
    • (1994) J. Biomol. NMR , vol.4 , pp. 171-180
    • Wishart, D.S.1    Sykes, B.D.2
  • 42
    • 0028394633 scopus 로고
    • Analysis of proton chemical shifts in regular secondary structure of proteins
    • K. Osapay, and D.A. Case Analysis of proton chemical shifts in regular secondary structure of proteins J. Biomol. NMR 4 1994 215 230
    • (1994) J. Biomol. NMR , vol.4 , pp. 215-230
    • Osapay, K.1    Case, D.A.2
  • 44
    • 0031063339 scopus 로고    scopus 로고
    • Automated probabilistic method for assigning backbone resonances of (C-13, N-15)-labeled proteins
    • J.A. Lukin, A.P. Gove, S.N. Talukdar, and C. Ho Automated probabilistic method for assigning backbone resonances of (C-13, N-15)-labeled proteins J. Biomol. NMR 9 1997 151 166
    • (1997) J. Biomol. NMR , vol.9 , pp. 151-166
    • Lukin, J.A.1    Gove, A.P.2    Talukdar, S.N.3    Ho, C.4
  • 45
  • 47
    • 0032866939 scopus 로고    scopus 로고
    • RESCUE: An artificial neural network tool for the NMR spectral assignment of proteins
    • J.L. Pons, and M.A. Delsuc RESCUE: an artificial neural network tool for the NMR spectral assignment of proteins J. Biomol. NMR 15 1999 15 26
    • (1999) J. Biomol. NMR , vol.15 , pp. 15-26
    • Pons, J.L.1    Delsuc, M.A.2
  • 48
    • 33746587501 scopus 로고    scopus 로고
    • Probabilistic approach to determining unbiased random-coil carbon-13 chemical shift values from the protein chemical shift database
    • L. Wang, H.R. Eghbalnia, and J.L. Markley Probabilistic approach to determining unbiased random-coil carbon-13 chemical shift values from the protein chemical shift database J. Biomol. NMR 35 2006 155 165
    • (2006) J. Biomol. NMR , vol.35 , pp. 155-165
    • Wang, L.1    Eghbalnia, H.R.2    Markley, J.L.3
  • 49
    • 35449003970 scopus 로고    scopus 로고
    • Nearest-neighbor effects on backbone alpha and beta carbon chemical shifts in proteins
    • L. Wang, H.R. Eghbalnia, and J.L. Markley Nearest-neighbor effects on backbone alpha and beta carbon chemical shifts in proteins J. Biomol. NMR 39 2007 247 257
    • (2007) J. Biomol. NMR , vol.39 , pp. 247-257
    • Wang, L.1    Eghbalnia, H.R.2    Markley, J.L.3
  • 50
    • 0037184476 scopus 로고    scopus 로고
    • Investigation of the neighboring residue effects on protein chemical shifts
    • Y.J. Wang, and O. Jardetzky Investigation of the neighboring residue effects on protein chemical shifts J. Am. Chem. Soc. 124 2002 14075 14084
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 14075-14084
    • Wang, Y.J.1    Jardetzky, O.2
  • 51
    • 1442306656 scopus 로고    scopus 로고
    • Assignment validation software suite for the evaluation and presentation of protein resonance assignment data
    • H.N. Moseley, G. Sahota, and G.T. Montelione Assignment validation software suite for the evaluation and presentation of protein resonance assignment data J. Biomol. NMR 28 2004 341 355
    • (2004) J. Biomol. NMR , vol.28 , pp. 341-355
    • Moseley, H.N.1    Sahota, G.2    Montelione, G.T.3
  • 52
    • 68349093958 scopus 로고    scopus 로고
    • TALOS+: A hybrid method for predicting protein backbone torsion angles from NMR chemical shifts
    • Y. Shen, F. Delaglio, G. Cornilescu, and A. Bax TALOS+: a hybrid method for predicting protein backbone torsion angles from NMR chemical shifts J. Biomol. NMR 44 2009 213 223
    • (2009) J. Biomol. NMR , vol.44 , pp. 213-223
    • Shen, Y.1    Delaglio, F.2    Cornilescu, G.3    Bax, A.4
  • 53
    • 32544456608 scopus 로고    scopus 로고
    • SimShift: Identifying structural similarities from NMR chemical shifts
    • S.W. Ginzinger, and J. Fischer SimShift: identifying structural similarities from NMR chemical shifts Bioinformatics 22 2006 460 465
    • (2006) Bioinformatics , vol.22 , pp. 460-465
    • Ginzinger, S.W.1    Fischer, J.2
  • 54
    • 61549095002 scopus 로고    scopus 로고
    • SimShiftDB; Local conformational restraints derived from chemical shift similarity searches on a large synthetic database
    • S.W. Ginzinger, and M. Coles SimShiftDB; local conformational restraints derived from chemical shift similarity searches on a large synthetic database J. Biomol. NMR 43 2009 179 185
    • (2009) J. Biomol. NMR , vol.43 , pp. 179-185
    • Ginzinger, S.W.1    Coles, M.2
  • 55
    • 0032110340 scopus 로고    scopus 로고
    • Recommendations for the presentation of NMR structures of proteins and nucleic acids: IUPAC-IUBMB-IUPAB Inter-Union Task Group on the Standardization of Data Bases of Protein and Nucleic Acid Structures Determined by NMR Spectroscopy
    • J.L. Markley, A. Bax, Y. Arata, C.W. Hilbers, R. Kaptein, B.D. Sykes, P.E. Wright, and K. Wüthrich Recommendations for the presentation of NMR structures of proteins and nucleic acids. IUPAC-IUBMB-IUPAB Inter-union task group on the standardization of data bases of protein and nucleic acid structures determined by NMR spectroscopy J. Biomol. NMR 12 1998 1 23 (Pubitemid 128512831)
    • (1998) Journal of Biomolecular NMR , vol.12 , Issue.1 , pp. 1-23
    • Markley, J.L.1    Bax, A.2    Arata, Y.3    Hilbers, C.W.4    Kaptein, R.5    Sykes, B.D.6    Wright, P.E.7    Wuthrich, K.8
  • 58
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • C. Bartels, T.H. Xia, M. Billeter, P. Güntert, and K. Wüthrich The program XEASY for computer-supported NMR spectral analysis of biological macromolecules J. Biomol. NMR 5 1995 1 10
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 60
    • 0031302286 scopus 로고    scopus 로고
    • Automated H-1 and C-13 chemical shift prediction using the BioMagResBank
    • D.S. Wishart, M.S. Watson, R.F. Boyko, and B.D. Sykes Automated H-1 and C-13 chemical shift prediction using the BioMagResBank J. Biomol. NMR 10 1997 329 336
    • (1997) J. Biomol. NMR , vol.10 , pp. 329-336
    • Wishart, D.S.1    Watson, M.S.2    Boyko, R.F.3    Sykes, B.D.4
  • 61
    • 34249765651 scopus 로고
    • NMRView: A computer program for the visualization and analysis of NMR data
    • B.A. Johnson, and R.A. Blevins NMRView: a computer program for the visualization and analysis of NMR data J. Biomol. NMR 4 1994 605 614
    • (1994) J. Biomol. NMR , vol.4 , pp. 605-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 62
    • 4644259437 scopus 로고    scopus 로고
    • Using NMRView to visualize and analyze the NMR spectra of macromolecules
    • B.A. Johnson Using NMRView to visualize and analyze the NMR spectra of macromolecules Methods Mol. Biol. 278 2004 313 352
    • (2004) Methods Mol. Biol. , vol.278 , pp. 313-352
    • Johnson, B.A.1
  • 64
    • 23144462958 scopus 로고    scopus 로고
    • Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications
    • L. Wang, H.R. Eghbalnia, A. Bahrami, and J.L. Markley Linear analysis of carbon-13 chemical shift differences and its application to the detection and correction of errors in referencing and spin system identifications J. Biomol. NMR 32 2005 13 22
    • (2005) J. Biomol. NMR , vol.32 , pp. 13-22
    • Wang, L.1    Eghbalnia, H.R.2    Bahrami, A.3    Markley, J.L.4
  • 65
    • 0037354231 scopus 로고    scopus 로고
    • RefDB: A database of uniformly referenced protein chemical shifts
    • H. Zhang, S. Neal, and D.S. Wishart RefDB: a database of uniformly referenced protein chemical shifts J. Biomol. NMR 25 2003 173 195
    • (2003) J. Biomol. NMR , vol.25 , pp. 173-195
    • Zhang, H.1    Neal, S.2    Wishart, D.S.3
  • 66
    • 34547179849 scopus 로고    scopus 로고
    • Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology
    • Y. Shen, and A. Bax Protein backbone chemical shifts predicted from searching a database for torsion angle and sequence homology J. Biomol. NMR 38 2007 289 302
    • (2007) J. Biomol. NMR , vol.38 , pp. 289-302
    • Shen, Y.1    Bax, A.2
  • 68
    • 67349267665 scopus 로고    scopus 로고
    • 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing
    • 13C secondary chemical shifts and its application to nitrogen chemical shift re-referencing J. Biomol. NMR 44 2009 95 99
    • (2009) J. Biomol. NMR , vol.44 , pp. 95-99
    • Wang, L.1    Markley, J.L.2
  • 69
    • 0000824485 scopus 로고
    • Recommendations for the presentation of NMR data for publication in chemical journals
    • IUPAC
    • IUPAC Recommendations for the presentation of NMR data for publication in chemical journals Pure Appl. Chem. 29 1972 627 628
    • (1972) Pure Appl. Chem. , vol.29 , pp. 627-628
  • 70
    • 0035742515 scopus 로고    scopus 로고
    • NMR nomenclature: Nuclear spin properties and conventions for chemical shifts. IUPAC recommendations 2001
    • R.J. Harris, E.D. Becker, S.M. Cabral de Menezes, R. Goodfellow, and P. Granger NMR nomenclature: nuclear spin properties and conventions for chemical shifts. IUPAC recommendations 2001 Pure Appl. Chem. 73 2001 1795 1818
    • (2001) Pure Appl. Chem. , vol.73 , pp. 1795-1818
    • Harris, R.J.1    Becker, E.D.2    Cabral De Menezes, S.M.3    Goodfellow, R.4    Granger, P.5
  • 71
    • 44449127248 scopus 로고    scopus 로고
    • International union of pure and applied chemistry physical and biophysical chemistry division. Further conventions for NMR shielding and chemical shifts (IUPAC recommendations 2008)
    • R.K. Harris, E.D. Becker, S.M. De Menezes, P. Granger, R.E. Hoffman, and K.W. Zilm International union of pure and applied chemistry physical and biophysical chemistry division. Further conventions for NMR shielding and chemical shifts (IUPAC recommendations 2008) Magn. Reson. Chem. 46 2008 582 598
    • (2008) Magn. Reson. Chem. , vol.46 , pp. 582-598
    • Harris, R.K.1    Becker, E.D.2    De Menezes, S.M.3    Granger, P.4    Hoffman, R.E.5    Zilm, K.W.6
  • 73
    • 15844395840 scopus 로고    scopus 로고
    • 15N chemical shift assignments of proteins
    • 15N chemical shift assignments of proteins J. Biomol. NMR 31 2005 143 148
    • (2005) J. Biomol. NMR , vol.31 , pp. 143-148
    • Wang, Y.1    Wishart, D.S.2
  • 74
    • 35448950267 scopus 로고    scopus 로고
    • CheckShift: Automatic correction of inconsistent chemical shift referencing
    • S.W. Ginzinger, F. Gerick, M. Coles, and V. Heun CheckShift: automatic correction of inconsistent chemical shift referencing J. Biomol. NMR 39 2007 223 227
    • (2007) J. Biomol. NMR , vol.39 , pp. 223-227
    • Ginzinger, S.W.1    Gerick, F.2    Coles, M.3    Heun, V.4
  • 75
    • 68349101323 scopus 로고    scopus 로고
    • CheckShift improved: Fast chemical shift reference correction with high accuracy
    • S.W. Ginzinger, M. Skocibusić, and V. Heun CheckShift improved: fast chemical shift reference correction with high accuracy J. Biomol. NMR 44 2009 207 211
    • (2009) J. Biomol. NMR , vol.44 , pp. 207-211
    • Ginzinger, S.W.1    Skocibusić, M.2    Heun, V.3
  • 76
    • 77954688894 scopus 로고    scopus 로고
    • A probabilistic approach for validating protein NMR chemical shift assignments
    • B. Wang, Y. Wang, and D.S. Wishart A probabilistic approach for validating protein NMR chemical shift assignments J. Biomol. NMR 47 2010 85 99
    • (2010) J. Biomol. NMR , vol.47 , pp. 85-99
    • Wang, B.1    Wang, Y.2    Wishart, D.S.3
  • 77
    • 0034044314 scopus 로고    scopus 로고
    • The PSIPRED protein structure prediction server
    • L.J. McGuffin, K. Bryson, and D.T. Jones The PSIPRED protein structure prediction server Bioinformatics 16 2000 404 405
    • (2000) Bioinformatics , vol.16 , pp. 404-405
    • McGuffin, L.J.1    Bryson, K.2    Jones, D.T.3
  • 78
    • 0020758436 scopus 로고
    • Structural information from NMR secondary chemical shifts of peptide alpha C-H protons in proteins
    • D.C. Dalgarno, B.A. Levine, and R.J. Williams Structural information from NMR secondary chemical shifts of peptide alpha C-H protons in proteins Biosci. Rep. 3 1983 443 452
    • (1983) Biosci. Rep. , vol.3 , pp. 443-452
    • Dalgarno, D.C.1    Levine, B.A.2    Williams, R.J.3
  • 79
    • 0018118592 scopus 로고
    • Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-LAla-OH
    • R. Richarz, and K. Wüthrich Carbon-13 NMR chemical shifts of the common amino acid residues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-LAla-OH Biopolymers 17 1978 2133 2141
    • (1978) Biopolymers , vol.17 , pp. 2133-2141
    • Richarz, R.1    Wüthrich, K.2
  • 80
    • 84985733652 scopus 로고
    • 1H NMR parameters of the common amino acid aresidues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-LAla-OH
    • 1H NMR parameters of the common amino acid aresidues measured in aqueous solutions of the linear tetrapeptides H-Gly-Gly-X-LAla-OH Biopolymers 18 1979 285 297
    • (1979) Biopolymers , vol.18 , pp. 285-297
    • Bundi, A.1    Wüthrich, K.2
  • 82
    • 0024423002 scopus 로고
    • 15N chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin
    • 15N chemical shifts of backbone amides in bovine pancreatic trypsin inhibitor and apamin J. Am. Chem. Soc. 111 1989 7716 7722
    • (1989) J. Am. Chem. Soc. , vol.111 , pp. 7716-7722
    • Glushka, J.1    Lee, M.2    Coffin, S.3    Cowburn, D.4
  • 84
    • 0027928701 scopus 로고
    • 13C chemical shifts of amino acids in aqueous solution containing organic solvents: Application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution
    • 13C chemical shifts of amino acids in aqueous solution containing organic solvents: application to the secondary structure characterization of peptides in aqueous trifluoroethanol solution J. Biomol. NMR 4 1994 47 59
    • (1994) J. Biomol. NMR , vol.4 , pp. 47-59
    • Thanabal, V.1    Omecinsky, D.O.2    Reily, M.D.3    Cody, W.L.4
  • 85
    • 0000084729 scopus 로고
    • Sequence-corrected N-15 random coil chemical shifts
    • D. Braun, G. Wider, and K. Wüthrich Sequence-corrected N-15 random coil chemical shifts J. Am. Chem. Soc. 8466 1994 8466 8469
    • (1994) J. Am. Chem. Soc. , vol.8466 , pp. 8466-8469
    • Braun, D.1    Wider, G.2    Wüthrich, K.3
  • 86
    • 0029181728 scopus 로고
    • H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids.1. Investigations of nearest-neighbor effects
    • D.S. Wishart, C.G. Bigam, A. Holm, R.S. Hodges, and B.D. Sykes H-1, C-13 and N-15 random coil NMR chemical shifts of the common amino acids.1. Investigations of nearest-neighbor effects J. Biomol. NMR 5 1995 67 81
    • (1995) J. Biomol. NMR , vol.5 , pp. 67-81
    • Wishart, D.S.1    Bigam, C.G.2    Holm, A.3    Hodges, R.S.4    Sykes, B.D.5
  • 87
    • 0029207339 scopus 로고
    • Random coil H-1 chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGxGG
    • G. Merutka, H.J. Dyson, and P.E. Wright Random coil H-1 chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGxGG J. Biomol. NMR 5 1995 14 24
    • (1995) J. Biomol. NMR , vol.5 , pp. 14-24
    • Merutka, G.1    Dyson, H.J.2    Wright, P.E.3
  • 88
    • 0001078545 scopus 로고    scopus 로고
    • The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG
    • K.W. Plaxco, C.J. Morton, S.B. Grimshaw, J.A. Jones, M. Pitkeathly, I.D. Campbell, and C.M. Dobson The effects of guanidine hydrochloride on the 'random coil' conformations and NMR chemical shifts of the peptide series GGXGG J. Biomol. NMR 10 1997 221 230
    • (1997) J. Biomol. NMR , vol.10 , pp. 221-230
    • Plaxco, K.W.1    Morton, C.J.2    Grimshaw, S.B.3    Jones, J.A.4    Pitkeathly, M.5    Campbell, I.D.6    Dobson, C.M.7
  • 89
    • 0033794319 scopus 로고    scopus 로고
    • Random coil chemical shifts in acidic 8 M urea: Implementation of random coil shift data in NMRView
    • S. Schwarzinger, G.J.A. Kroon, T.R. Foss, P.E. Wright, and H.J. Dyson Random coil chemical shifts in acidic 8 M urea: implementation of random coil shift data in NMRView J. Biomol. NMR 18 2000 43 48
    • (2000) J. Biomol. NMR , vol.18 , pp. 43-48
    • Schwarzinger, S.1    Kroon, G.J.A.2    Foss, T.R.3    Wright, P.E.4    Dyson, H.J.5
  • 90
    • 77951665349 scopus 로고    scopus 로고
    • The predictive accuracy of secondary chemical shifts is more affected by protein secondary structure than solvent environment
    • M.L. Tremblay, A.W. Banks, and J.K. Rainey The predictive accuracy of secondary chemical shifts is more affected by protein secondary structure than solvent environment J. Biomol. NMR 46 2010 257 270
    • (2010) J. Biomol. NMR , vol.46 , pp. 257-270
    • Tremblay, M.L.1    Banks, A.W.2    Rainey, J.K.3
  • 91
    • 0033377656 scopus 로고    scopus 로고
    • Random-coil chemical shifts of phosphorylated amino acids
    • E.A. Bienkiewicz, and K.J. Lumb Random-coil chemical shifts of phosphorylated amino acids J. Biomol. NMR 15 1999 203 206
    • (1999) J. Biomol. NMR , vol.15 , pp. 203-206
    • Bienkiewicz, E.A.1    Lumb, K.J.2
  • 92
    • 0037007467 scopus 로고    scopus 로고
    • 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa.
    • 1H-NMR parameters of common amino acid residues measured in aqueous solutions of the linear tetrapeptides Gly-Gly-X-Ala at pressures between 0.1 and 200 MPa. Biophys. Chem. 96 2002 129 140
    • (2002) Biophys. Chem. , vol.96 , pp. 129-140
    • Arnold, M.R.1    Kremer, W.2    Lüdemann, H.D.3    Kalbitzer, H.R.4
  • 93
    • 33846488586 scopus 로고    scopus 로고
    • Effect of pH, urea, peptide length, and neighboring amino acids on alanine alpha-proton random coil chemical shifts
    • E.A. Carlisle, J.L. Holder, A.M. Maranda, A.R. de Alwis, E.L. Selkie, and S.L. McKay Effect of pH, urea, peptide length, and neighboring amino acids on alanine alpha-proton random coil chemical shifts Biopolymers 85 2007 72 80
    • (2007) Biopolymers , vol.85 , pp. 72-80
    • Carlisle, E.A.1    Holder, J.L.2    Maranda, A.M.3    De Alwis, A.R.4    Selkie, E.L.5    McKay, S.L.6
  • 95
    • 0036129107 scopus 로고    scopus 로고
    • Probability-based protein secondary structure identification using combined NMR chemical-shift data
    • Y.J. Wang, and O. Jardetzky Probability-based protein secondary structure identification using combined NMR chemical-shift data Protein Sci. 11 2002 852 861
    • (2002) Protein Sci. , vol.11 , pp. 852-861
    • Wang, Y.J.1    Jardetzky, O.2
  • 96
    • 0014202630 scopus 로고
    • Nuclear magnetic resonance studies of helix-coil transitions in polyamino acids
    • J.L. Markley, D.H. Meadows, and O. Jardetzky Nuclear magnetic resonance studies of helix-coil transitions in polyamino acids J. Mol. Biol. 27 1967 25 40
    • (1967) J. Mol. Biol. , vol.27 , pp. 25-40
    • Markley, J.L.1    Meadows, D.H.2    Jardetzky, O.3
  • 98
    • 0021105573 scopus 로고
    • Protein conformation and proton nuclear-magnetic-resonance chemical shifts
    • A. Pardi, G. Wagner, and K. Wüthrich Protein conformation and proton nuclear-magnetic-resonance chemical shifts Eur. J. Biochem. 137 1983 445 454
    • (1983) Eur. J. Biochem. , vol.137 , pp. 445-454
    • Pardi, A.1    Wagner, G.2    Wüthrich, K.3
  • 99
    • 0028434564 scopus 로고
    • 15N NMR chemical shifts in proteins and secondary structure
    • 15N NMR chemical shifts in proteins and secondary structure J. Biomol. NMR 4 1994 341 348
    • (1994) J. Biomol. NMR , vol.4 , pp. 341-348
    • Le, H.1    Oldfield, E.2
  • 100
    • 0000635348 scopus 로고
    • The relationship between amide proton chemical shifts and secondary structure in proteins
    • T. Asakura, K. Taoka, M. Demura, and M.P. Williamson The relationship between amide proton chemical shifts and secondary structure in proteins J. Biomol. NMR 6 1995 227 236
    • (1995) J. Biomol. NMR , vol.6 , pp. 227-236
    • Asakura, T.1    Taoka, K.2    Demura, M.3    Williamson, M.P.4
  • 101
    • 33751430523 scopus 로고    scopus 로고
    • Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: A tool for target selection in structural proteomics
    • V.H. Moreau, A.P. Valente, and F.C.L. Almeida Prediction of the amount of secondary structure of proteins using unassigned NMR spectra: a tool for target selection in structural proteomics Genet. Mol. Biol. 29 2006 762 770
    • (2006) Genet. Mol. Biol. , vol.29 , pp. 762-770
    • Moreau, V.H.1    Valente, A.P.2    Almeida, F.C.L.3
  • 102
    • 0242661071 scopus 로고    scopus 로고
    • Protein structural class identification directly from NMR spectra using averaged chemical shifts
    • S.P. Mielke, and V.V. Krishnan Protein structural class identification directly from NMR spectra using averaged chemical shifts Bioinformatics 19 2003 2054 2064
    • (2003) Bioinformatics , vol.19 , pp. 2054-2064
    • Mielke, S.P.1    Krishnan, V.V.2
  • 103
    • 33646475910 scopus 로고    scopus 로고
    • Estimation of protein secondary structure content directly from NMR spectra using an improved empirical correlation with averaged chemical shift
    • S.P. Mielke, and V.V. Krishnan Estimation of protein secondary structure content directly from NMR spectra using an improved empirical correlation with averaged chemical shift J. Struct. Funct. Genomics. 6 2005 281 285
    • (2005) J. Struct. Funct. Genomics. , vol.6 , pp. 281-285
    • Mielke, S.P.1    Krishnan, V.V.2
  • 104
    • 0023661664 scopus 로고
    • Secondary structure determination in proteins from deep (192-223 nm) ultraviolet Raman spectroscopy
    • R.A. Copeland, and T.G. Spiro Secondary structure determination in proteins from deep (192-223 nm) ultraviolet Raman spectroscopy Biochemistry 26 1987 2134 2139
    • (1987) Biochemistry , vol.26 , pp. 2134-2139
    • Copeland, R.A.1    Spiro, T.G.2
  • 105
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the conformation of proteins and polypeptides from circular dichroism data
    • N.J. Greenfield Methods to estimate the conformation of proteins and polypeptides from circular dichroism data Anal. Biochem. 235 1996 1 10
    • (1996) Anal. Biochem. , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 106
    • 0029018548 scopus 로고
    • The use and misuse of FTIR spectroscopy in the determination of protein structure
    • M. Jackson, and H.H. Mantsch The use and misuse of FTIR spectroscopy in the determination of protein structure Crit. Rev. Biochem. Mol. Biol. 30 1995 95 120
    • (1995) Crit. Rev. Biochem. Mol. Biol. , vol.30 , pp. 95-120
    • Jackson, M.1    Mantsch, H.H.2
  • 107
    • 0001006731 scopus 로고
    • Structure-induced carbon-13 chemical shifts: A sensitive measure of transient localized secondary structure in peptides
    • M.D. Reily, V. Thanabal, and D.O. Omecinsky Structure-induced carbon-13 chemical shifts: a sensitive measure of transient localized secondary structure in peptides J. Am. Chem. Soc. 114 1992 6251 6252
    • (1992) J. Am. Chem. Soc. , vol.114 , pp. 6251-6252
    • Reily, M.D.1    Thanabal, V.2    Omecinsky, D.O.3
  • 108
    • 32944464105 scopus 로고    scopus 로고
    • An evaluation of chemical shift index-based secondary structure determination in proteins: Influence of random coil chemical shifts
    • S.P. Mielke, and V.V. Krishnan An evaluation of chemical shift index-based secondary structure determination in proteins: influence of random coil chemical shifts J. Biomol. NMR 30 2004 143 153
    • (2004) J. Biomol. NMR , vol.30 , pp. 143-153
    • Mielke, S.P.1    Krishnan, V.V.2
  • 109
    • 34547563370 scopus 로고    scopus 로고
    • The RCI server: Rapid and accurate calculation of protein flexibility using chemical shifts
    • M.V. Berjanskii, and D.S. Wishart The RCI server: rapid and accurate calculation of protein flexibility using chemical shifts Nucleic Acids Res. 35 2007 W531 537
    • (2007) Nucleic Acids Res. , vol.35 , pp. 531-537
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 110
    • 48449095850 scopus 로고    scopus 로고
    • CS23D: A web server for rapid protein structure generation using NMR chemical shifts and sequence data
    • D.S. Wishart, D. Arndt, M. Berjanskii, P. Tang, J. Zhou, and G. Lin CS23D: a web server for rapid protein structure generation using NMR chemical shifts and sequence data Nucleic Acids Res. 36 2008 W496 502
    • (2008) Nucleic Acids Res. , vol.36 , pp. 496-502
    • Wishart, D.S.1    Arndt, D.2    Berjanskii, M.3    Tang, P.4    Zhou, J.5    Lin, G.6
  • 111
    • 0037304379 scopus 로고    scopus 로고
    • Accurate and automated classification of protein secondary structure with PsiCSI
    • L.H. Hung, and R. Samudrala Accurate and automated classification of protein secondary structure with PsiCSI Protein Sci. 12 2003 288 295
    • (2003) Protein Sci. , vol.12 , pp. 288-295
    • Hung, L.H.1    Samudrala, R.2
  • 112
    • 0037266712 scopus 로고    scopus 로고
    • Prediction algorithm for amino acid types with their secondary structure in proteins (PLATON) using chemical shifts
    • D. Labudde, D. Leitner, M. Kruger, and H. Oschkinat Prediction algorithm for amino acid types with their secondary structure in proteins (PLATON) using chemical shifts J. Biomol. NMR 25 2003 41 53
    • (2003) J. Biomol. NMR , vol.25 , pp. 41-53
    • Labudde, D.1    Leitner, D.2    Kruger, M.3    Oschkinat, H.4
  • 113
    • 23144437542 scopus 로고    scopus 로고
    • Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements
    • H.R. Eghbalnia, L. Wang, A. Bahrami, A. Assadi, and J.L. Markley Protein energetic conformational analysis from NMR chemical shifts (PECAN) and its use in determining secondary structural elements J. Biomol. NMR 32 2005 71 81
    • (2005) J. Biomol. NMR , vol.32 , pp. 71-81
    • Eghbalnia, H.R.1    Wang, L.2    Bahrami, A.3    Assadi, A.4    Markley, J.L.5
  • 114
    • 34248590986 scopus 로고    scopus 로고
    • 2DCSi: Identification of protein secondary structure and redox state using 2D cluster analysis of NMR chemical shifts
    • C.C. Wang, J.H. Chen, W.C. Lai, and W.J. Chuang 2DCSi: identification of protein secondary structure and redox state using 2D cluster analysis of NMR chemical shifts J. Biomol. NMR 38 2007 57 63
    • (2007) J. Biomol. NMR , vol.38 , pp. 57-63
    • Wang, C.C.1    Chen, J.H.2    Lai, W.C.3    Chuang, W.J.4
  • 115
    • 0034744426 scopus 로고    scopus 로고
    • 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides
    • 13C(beta) chemical shifts as a tool to delineate beta-hairpin structures in peptides J. Biomol. NMR 19 2001 331 345
    • (2001) J. Biomol. NMR , vol.19 , pp. 331-345
    • Santiveri, C.M.1    Rico, M.2    Jiménez, M.A.3
  • 118
    • 33745465576 scopus 로고    scopus 로고
    • 13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy
    • 13C-labeled microcrystalline protein by three-dimensional magic-angle spinning nuclear magnetic resonance spectroscopy J. Phys. Chem. B 110 2006 10926 10936
    • (2006) J. Phys. Chem. B , vol.110 , pp. 10926-10936
    • Wylie, B.J.1    Franks, W.T.2    Rienstra, C.M.3
  • 119
    • 33846999342 scopus 로고    scopus 로고
    • Secondary structures of peptides and proteins via NMR chemical-shielding anisotropy (CSA) parameters
    • E. Czinki, A.G. Császár, G. Magyarfalvi, P.R. Schreiner, and W.D. Allen Secondary structures of peptides and proteins via NMR chemical-shielding anisotropy (CSA) parameters J. Am. Chem. Soc. 129 2007 1568 1577
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 1568-1577
    • Czinki, E.1    Császár, A.G.2    Magyarfalvi, G.3    Schreiner, P.R.4    Allen, W.D.5
  • 120
    • 77955499564 scopus 로고    scopus 로고
    • Using the chemical shift anisotropy tensor of carbonyl backbone nuclei as a probe of secondary structure in proteins
    • S.B. Elavarasi, A. Kumari, and K. Dorai Using the chemical shift anisotropy tensor of carbonyl backbone nuclei as a probe of secondary structure in proteins J. Phys. Chem. A. 114 2010 5830 5837
    • (2010) J. Phys. Chem. A. , vol.114 , pp. 5830-5837
    • Elavarasi, S.B.1    Kumari, A.2    Dorai, K.3
  • 121
    • 75149166570 scopus 로고    scopus 로고
    • Mapping NMR chemical shift anisotropy parameters of backbone nuclei onto secondary structure elements in proteins
    • S.B. Elavarasi, and K. Dorai Mapping NMR chemical shift anisotropy parameters of backbone nuclei onto secondary structure elements in proteins J. Biomol. Struct. Dyn. 27 2010 561 572
    • (2010) J. Biomol. Struct. Dyn. , vol.27 , pp. 561-572
    • Elavarasi, S.B.1    Dorai, K.2
  • 122
    • 76549252207 scopus 로고
    • The structure of proteins; Two hydrogen-bonded helical configurations of the polypeptide chain
    • L. Pauling, R.B. Corey, and H.R. Branson The structure of proteins; two hydrogen-bonded helical configurations of the polypeptide chain Proc. Natl. Acad. Sci. USA 37 1951 205 211
    • (1951) Proc. Natl. Acad. Sci. USA , vol.37 , pp. 205-211
    • Pauling, L.1    Corey, R.B.2    Branson, H.R.3
  • 124
    • 26444452027 scopus 로고    scopus 로고
    • Protein secondary structure assignment revisited: A detailed analysis of different assignment methods
    • J. Martin, G. Letellier, A. Marin, J.F. Taly, A.G. de Brevern, and J.F. Gibrat Protein secondary structure assignment revisited: a detailed analysis of different assignment methods BMC Struct. Biol. 5 2005 17
    • (2005) BMC Struct. Biol. , vol.5 , pp. 17
    • Martin, J.1    Letellier, G.2    Marin, A.3    Taly, J.F.4    De Brevern, A.G.5    Gibrat, J.F.6
  • 125
    • 0020997912 scopus 로고
    • Dictionary of protein secondary structure: Pattern recognition of hydrogen-bonded and geometrical features
    • W. Kabsch, and C. Sander Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features Biopolymers 22 1983 2577 2637
    • (1983) Biopolymers , vol.22 , pp. 2577-2637
    • Kabsch, W.1    Sander, C.2
  • 126
    • 0029619259 scopus 로고
    • Knowledge-based protein secondary structure assignment
    • D. Frishman, and P. Argos Knowledge-based protein secondary structure assignment Proteins 23 1995 566 579
    • (1995) Proteins , vol.23 , pp. 566-579
    • Frishman, D.1    Argos, P.2
  • 127
    • 0036276409 scopus 로고    scopus 로고
    • Occurrence, conformational features and amino acid propensities for the pi-helix
    • M.N. Fodje, and S. Al-Karadaghi Occurrence, conformational features and amino acid propensities for the pi-helix Protein Eng. 15 2002 353 358
    • (2002) Protein Eng. , vol.15 , pp. 353-358
    • Fodje, M.N.1    Al-Karadaghi, S.2
  • 128
    • 0017701604 scopus 로고
    • Automatic identification of secondary structure in globular proteins
    • M. Levitt, and J. Greer Automatic identification of secondary structure in globular proteins J. Mol. Biol. 114 1977 181 239
    • (1977) J. Mol. Biol. , vol.114 , pp. 181-239
    • Levitt, M.1    Greer, J.2
  • 129
    • 0023927904 scopus 로고
    • Identification of structural motifs from protein coordinate data: Secondary structure and first-level supersecondary structure
    • F.M. Richards, and C.E. Kundrot Identification of structural motifs from protein coordinate data: secondary structure and first-level supersecondary structure Proteins 3 1988 71 84
    • (1988) Proteins , vol.3 , pp. 71-84
    • Richards, F.M.1    Kundrot, C.E.2
  • 130
    • 0024821134 scopus 로고
    • Describing protein structure: A general algorithm yielding complete helicoidal parameters and a unique overall axis
    • H. Sklenar, C. Etchebest, and R. Lavery Describing protein structure: a general algorithm yielding complete helicoidal parameters and a unique overall axis Proteins: Struct. Funct. Genet. 6 1989 46 60
    • (1989) Proteins: Struct. Funct. Genet. , vol.6 , pp. 46-60
    • Sklenar, H.1    Etchebest, C.2    Lavery, R.3
  • 131
    • 0030998184 scopus 로고    scopus 로고
    • P-SEA: A new efficient assignment of secondary structure from C alpha trace of proteins
    • G. Labesse, N. Colloc'h, J. Pothier, and J.P. Mornon P-SEA: a new efficient assignment of secondary structure from C alpha trace of proteins Comput. Appl. Biosci. 13 1997 291 295
    • (1997) Comput. Appl. Biosci. , vol.13 , pp. 291-295
    • Labesse, G.1    Colloc'H, N.2    Pothier, J.3    Mornon, J.P.4
  • 132
    • 0033562619 scopus 로고    scopus 로고
    • Assigning secondary structure from protein coordinate data
    • S.M. King, and W.C. Johnson Assigning secondary structure from protein coordinate data Proteins 3 1999 313 320
    • (1999) Proteins , vol.3 , pp. 313-320
    • King, S.M.1    Johnson, W.C.2
  • 133
    • 0027207221 scopus 로고
    • Comparison of three algorithms for the assignment of secondary structure in proteins: The advantages of a consensus assignment
    • N. Colloc'h, C. Etchebest, E. Thoreau, B. Henrissat, and J.P. Mornon Comparison of three algorithms for the assignment of secondary structure in proteins: the advantages of a consensus assignment Protein Eng. 6 1993 377 382
    • (1993) Protein Eng. , vol.6 , pp. 377-382
    • Colloc'H, N.1    Etchebest, C.2    Thoreau, E.3    Henrissat, B.4    Mornon, J.P.5
  • 135
    • 35448929112 scopus 로고    scopus 로고
    • A large data set comparison of protein structures determined by crystallography and NMR: Statistical test for structural differences and the effect of crystal packing
    • M. Andrec, D.A. Snyder, Z. Zhou, J. Young, G.T. Montelione, and R.M. Levy A large data set comparison of protein structures determined by crystallography and NMR: statistical test for structural differences and the effect of crystal packing Proteins 69 2007 449 465
    • (2007) Proteins , vol.69 , pp. 449-465
    • Andrec, M.1    Snyder, D.A.2    Zhou, Z.3    Young, J.4    Montelione, G.T.5    Levy, R.M.6
  • 139
    • 0030764469 scopus 로고    scopus 로고
    • Determination of phi and chi(1) angles in proteins from C-13-C-13 three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond?
    • J.S. Hu, and A. Bax Determination of phi and chi(1) angles in proteins from C-13-C-13 three-bond J couplings measured by three-dimensional heteronuclear NMR. How planar is the peptide bond? J. Am. Chem. Soc. 119 1997 6360 6368
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 6360-6368
    • Hu, J.S.1    Bax, A.2
  • 140
    • 0032527727 scopus 로고    scopus 로고
    • Determination of the dihedral angle psi based on J coupling measurements in N-15/C-13-labeled proteins
    • M. Pellecchia, R. Fattorusso, and G. Wider Determination of the dihedral angle psi based on J coupling measurements in N-15/C-13-labeled proteins J. Am. Chem. Soc. 120 1998 6824 6825
    • (1998) J. Am. Chem. Soc. , vol.120 , pp. 6824-6825
    • Pellecchia, M.1    Fattorusso, R.2    Wider, G.3
  • 141
    • 0032584772 scopus 로고    scopus 로고
    • Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences
    • N.J. West, and L.J. Smith Side-chains in native and random coil protein conformations. Analysis of NMR coupling constants and chi1 torsion angle preferences J. Mol. Biol. 280 1998 867 877
    • (1998) J. Mol. Biol. , vol.280 , pp. 867-877
    • West, N.J.1    Smith, L.J.2
  • 142
    • 0036234486 scopus 로고    scopus 로고
    • Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation
    • K. Kloiber, W. Schuler, and R. Konrat Automated NMR determination of protein backbone dihedral angles from cross-correlated spin relaxation J. Biomol. NMR 22 2002 349 363
    • (2002) J. Biomol. NMR , vol.22 , pp. 349-363
    • Kloiber, K.1    Schuler, W.2    Konrat, R.3
  • 143
    • 0042386784 scopus 로고    scopus 로고
    • Measuring the chi 1 torsion angle in protein by CH-CH cross-correlated relaxation: A new resolution-optimised experiment
    • T. Carlomagno, W. Bermel, and C. Griesinger Measuring the chi 1 torsion angle in protein by CH-CH cross-correlated relaxation: a new resolution-optimised experiment J. Biomol. NMR 27 2003 151 157
    • (2003) J. Biomol. NMR , vol.27 , pp. 151-157
    • Carlomagno, T.1    Bermel, W.2    Griesinger, C.3
  • 144
    • 0031217977 scopus 로고    scopus 로고
    • Protein phi and psi dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structures
    • R.D. Beger, and P.H. Bolton Protein phi and psi dihedral restraints determined from multidimensional hypersurface correlations of backbone chemical shifts and their use in the determination of protein tertiary structures J. Biomol. NMR 10 1997 129 142
    • (1997) J. Biomol. NMR , vol.10 , pp. 129-142
    • Beger, R.D.1    Bolton, P.H.2
  • 145
    • 72449187567 scopus 로고    scopus 로고
    • DANGLE: A Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure
    • M.S. Cheung, M.L. Maguire, T.J. Stevens, and R.W. Broadhurst DANGLE: a Bayesian inferential method for predicting protein backbone dihedral angles and secondary structure J. Magn. Reson. 202 2010 223 233
    • (2010) J. Magn. Reson. , vol.202 , pp. 223-233
    • Cheung, M.S.1    Maguire, M.L.2    Stevens, T.J.3    Broadhurst, R.W.4
  • 146
    • 33746256561 scopus 로고    scopus 로고
    • Accurate prediction of protein torsion angles using chemical shifts and sequence homology
    • S. Neal, M. Berjanskii, H. Zhang, and D.S. Wishart Accurate prediction of protein torsion angles using chemical shifts and sequence homology Magn. Reson. Chem. 44 2006 S158 167
    • (2006) Magn. Reson. Chem. , vol.44 , pp. 158-167
    • Neal, S.1    Berjanskii, M.2    Zhang, H.3    Wishart, D.S.4
  • 147
    • 33747831881 scopus 로고    scopus 로고
    • PREDITOR: A web server for predicting protein torsion angle restraints
    • M.V. Berjanskii, S. Neal, and D.S. Wishart PREDITOR: a web server for predicting protein torsion angle restraints Nucleic Acids Res. 34 2006 W63 W69
    • (2006) Nucleic Acids Res. , vol.34
    • Berjanskii, M.V.1    Neal, S.2    Wishart, D.S.3
  • 148
    • 77951666856 scopus 로고    scopus 로고
    • Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts
    • Y. Shen, and A. Bax Prediction of Xaa-Pro peptide bond conformation from sequence and chemical shifts J. Biomol. NMR 46 2010 199 204
    • (2010) J. Biomol. NMR , vol.46 , pp. 199-204
    • Shen, Y.1    Bax, A.2
  • 149
    • 79451474913 scopus 로고    scopus 로고
    • personal communication, August 26
    • R.W. Broadhurst, personal communication, August 26, 2009.
    • (2009)
    • Broadhurst, R.W.1
  • 151
    • 50249158519 scopus 로고    scopus 로고
    • 13C shifts on dihedral angle: Application to conformational analysis
    • 13C shifts on dihedral angle: application to conformational analysis J. Am. Chem. Soc. 130 2008 11097 11105
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 11097-11105
    • London, R.E.1    Wingad, B.D.2    Mueller, G.A.3
  • 152
    • 74849091641 scopus 로고    scopus 로고
    • Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion
    • D.F. Hansen, P. Neudecker, P. Vallurupalli, F.A. Mulder, and L.E. Kay Determination of Leu side-chain conformations in excited protein states by NMR relaxation dispersion J. Am. Chem. Soc. 132 2010 42 43
    • (2010) J. Am. Chem. Soc. , vol.132 , pp. 42-43
    • Hansen, D.F.1    Neudecker, P.2    Vallurupalli, P.3    Mulder, F.A.4    Kay, L.E.5
  • 155
    • 17844408143 scopus 로고    scopus 로고
    • Analysis of correlated domain motions in IgG light chain reveals possible mechanisms of immunological signal transduction
    • M. Król, I. Roterman, B. Piekarska, L. Konieczny, J. Rybarska, B. Stopa, and P. Spólnik Analysis of correlated domain motions in IgG light chain reveals possible mechanisms of immunological signal transduction Proteins 59 2005 545 554
    • (2005) Proteins , vol.59 , pp. 545-554
    • Król, M.1    Roterman, I.2    Piekarska, B.3    Konieczny, L.4    Rybarska, J.5    Stopa, B.6    Spólnik, P.7
  • 156
    • 0019201754 scopus 로고
    • Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes
    • G. Lipari, and A. Szabo Effect of librational motion on fluorescence depolarization and nuclear magnetic resonance relaxation in macromolecules and membranes Biophys. J. 30 1980 489 506
    • (1980) Biophys. J. , vol.30 , pp. 489-506
    • Lipari, G.1    Szabo, A.2
  • 157
    • 0037202183 scopus 로고    scopus 로고
    • Contact model for the prediction of NMR N-H order parameters in globular proteins
    • F. Zhang, and R. Brüschweiler Contact model for the prediction of NMR N-H order parameters in globular proteins J. Am. Chem. Soc. 124 2002 12654 12655
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 12654-12655
    • Zhang, F.1    Brüschweiler, R.2
  • 158
    • 34547679071 scopus 로고    scopus 로고
    • NMR: Prediction of protein flexibility
    • M. Berjanskii, and D.S. Wishart NMR: prediction of protein flexibility Nat. Protoc. 1 2006 683 688
    • (2006) Nat. Protoc. , vol.1 , pp. 683-688
    • Berjanskii, M.1    Wishart, D.S.2
  • 159
    • 37848999781 scopus 로고    scopus 로고
    • Application of the random coil index to studying protein flexibility
    • M.V. Berjanskii, and D.S. Wishart Application of the random coil index to studying protein flexibility J. Biomol. NMR 40 2008 31 48
    • (2008) J. Biomol. NMR , vol.40 , pp. 31-48
    • Berjanskii, M.V.1    Wishart, D.S.2
  • 160
    • 0004579606 scopus 로고
    • C-13 NMR of protected tetrapeptides TFA-GLY-GLY-L-X-L-ALA-OCH3, where X stands for 20 common amino-acids
    • C. Grathwoh, and K. Wüthrich C-13 NMR of protected tetrapeptides TFA-GLY-GLY-L-X-L-ALA-OCH3, where X stands for 20 common amino-acids J. Magn. Reson. 13 1974 217 225
    • (1974) J. Magn. Reson. , vol.13 , pp. 217-225
    • Grathwoh, C.1    Wüthrich, K.2
  • 161
    • 49549138511 scopus 로고
    • Proton NMR of protected tetrapeptides TFA-GLY-GLY-L-X-L-ALA-OCH3, where X stands for one of 20 common amino-acids
    • A. Bundi, C. Grathwohl, J. Hochmann, G. Keller, G. Wagner, and K. Wüthrich Proton NMR of protected tetrapeptides TFA-GLY-GLY-L-X-L-ALA-OCH3, where X stands for one of 20 common amino-acids J. Magn. Reson. 18 1975 191 198
    • (1975) J. Magn. Reson. , vol.18 , pp. 191-198
    • Bundi, A.1    Grathwohl, C.2    Hochmann, J.3    Keller, G.4    Wagner, G.5    Wüthrich, K.6
  • 162
    • 0036874286 scopus 로고    scopus 로고
    • Unblocked statistical-coil tetrapeptides and pentapeptides in aqueous solution: A theoretical study
    • J.A. Vila, D.R. Ripoll, H.A. Baldoni, and H.A. Scheraga Unblocked statistical-coil tetrapeptides and pentapeptides in aqueous solution: a theoretical study J. Biomol. NMR 24 2002 245 262
    • (2002) J. Biomol. NMR , vol.24 , pp. 245-262
    • Vila, J.A.1    Ripoll, D.R.2    Baldoni, H.A.3    Scheraga, H.A.4
  • 163
    • 0031014714 scopus 로고    scopus 로고
    • NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein
    • A. Lecroisey, P. Martineau, M. Hofnung, and M. Delepierre NMR studies on the flexibility of the poliovirus C3 linear epitope inserted into different sites of the maltose-binding protein J. Biol. Chem. 272 1997 362 368
    • (1997) J. Biol. Chem. , vol.272 , pp. 362-368
    • Lecroisey, A.1    Martineau, P.2    Hofnung, M.3    Delepierre, M.4
  • 167
    • 61749092017 scopus 로고    scopus 로고
    • Structural domains and main-chain flexibility in prion proteins
    • N. Blinov, M. Berjanskii, D.S. Wishart, and M. Stepanova Structural domains and main-chain flexibility in prion proteins Biochemistry 48 2009 1488 1497
    • (2009) Biochemistry , vol.48 , pp. 1488-1497
    • Blinov, N.1    Berjanskii, M.2    Wishart, D.S.3    Stepanova, M.4
  • 168
    • 3142716857 scopus 로고    scopus 로고
    • Accelerated molecular dynamics: A promising and efficient simulation method for biomolecules
    • D. Hamelberg, J. Mongan, and J.A. McCammon Accelerated molecular dynamics: a promising and efficient simulation method for biomolecules J. Chem. Phys. 120 2004 11919 11929
    • (2004) J. Chem. Phys. , vol.120 , pp. 11919-11929
    • Hamelberg, D.1    Mongan, J.2    McCammon, J.A.3
  • 169
    • 36749036031 scopus 로고    scopus 로고
    • Dynamics of essential collective motions in proteins: Theory
    • M. Stepanova Dynamics of essential collective motions in proteins: theory Phys. Rev.E Stat. Nonlin. Soft Matter Phys. 76 2007 051918
    • (2007) Phys. Rev.E Stat. Nonlin. Soft Matter Phys. , vol.76 , pp. 051918
    • Stepanova, M.1
  • 170
    • 0035544152 scopus 로고    scopus 로고
    • 13C′ chemical shifts in proteins using a density functional database
    • 13C′ chemical shifts in proteins using a density functional database J. Biomol. NMR 21 2001 321 333
    • (2001) J. Biomol. NMR , vol.21 , pp. 321-333
    • Xu, X.P.1    Case, D.A.2
  • 171
    • 0026611767 scopus 로고
    • 1H NMR chemical shift calculations to diastereotopic groups in proteins
    • 1H NMR chemical shift calculations to diastereotopic groups in proteins FEBS Lett. 302 1992 185 188
    • (1992) FEBS Lett. , vol.302 , pp. 185-188
    • Williamson, M.P.1    Asakura, T.2
  • 173
    • 0027661418 scopus 로고
    • NMR chemical shifts and structure refinement in proteins
    • D.D. Laws, A.C. de Dios, and E. Oldfield NMR chemical shifts and structure refinement in proteins J. Biomol. NMR 3 1993 607 612
    • (1993) J. Biomol. NMR , vol.3 , pp. 607-612
    • Laws, D.D.1    De Dios, A.C.2    Oldfield, E.3
  • 174
    • 0028127028 scopus 로고
    • Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints
    • K. Osapay, Y. Theriault, P.E. Wright, and D.A. Case Solution structure of carbonmonoxy myoglobin determined from nuclear magnetic resonance distance and chemical shift constraints J. Mol. Biol. 244 1994 183 197
    • (1994) J. Mol. Biol. , vol.244 , pp. 183-197
    • Osapay, K.1    Theriault, Y.2    Wright, P.E.3    Case, D.A.4
  • 176
    • 0032532218 scopus 로고    scopus 로고
    • The structure of the melittin tetramer at different temperatures-an NOE-based calculation with chemical shift refinement
    • M. Iwadate, T. Asakura, and M.P. Williamson The structure of the melittin tetramer at different temperatures-an NOE-based calculation with chemical shift refinement Eur. J. Biochem. 257 1998 479 487
    • (1998) Eur. J. Biochem. , vol.257 , pp. 479-487
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 178
    • 0031637532 scopus 로고    scopus 로고
    • Chemical shift homology in proteins
    • B.C. Potts, and W.J. Chazin Chemical shift homology in proteins J. Biomol. NMR 11 1998 45 57
    • (1998) J. Biomol. NMR , vol.11 , pp. 45-57
    • Potts, B.C.1    Chazin, W.J.2
  • 179
    • 0014757386 scopus 로고
    • A general method applicable to the search for similarities in the amino acid sequence of two proteins
    • S.B. Needleman, and C.D. Wunsch A general method applicable to the search for similarities in the amino acid sequence of two proteins J. Mol. Biol. 48 1970 443 453
    • (1970) J. Mol. Biol. , vol.48 , pp. 443-453
    • Needleman, S.B.1    Wunsch, C.D.2
  • 181
    • 0038703404 scopus 로고    scopus 로고
    • PROSHIFT: Protein chemical shift prediction using artificial neural networks
    • J. Meiler PROSHIFT: protein chemical shift prediction using artificial neural networks J. Biomol. NMR 26 2003 25 37
    • (2003) J. Biomol. NMR , vol.26 , pp. 25-37
    • Meiler, J.1
  • 182
    • 10944271376 scopus 로고
    • Calculation of nuclear magnetic resonance spectra of aromatic hydrocarbons
    • C.E. Johnson, and F.A. Bovey Calculation of nuclear magnetic resonance spectra of aromatic hydrocarbons J. Chem. Phys. 29 1958 1012 1014
    • (1958) J. Chem. Phys. , vol.29 , pp. 1012-1014
    • Johnson, C.E.1    Bovey, F.A.2
  • 183
    • 0018801741 scopus 로고
    • Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor
    • S.J. Perkins, and K. Wüthrich Ring current effects in the conformation dependent NMR chemical shifts of aliphatic protons in the basic pancreatic trypsin inhibitor Biochim. Biophys. Acta. 576 1979 409 423
    • (1979) Biochim. Biophys. Acta. , vol.576 , pp. 409-423
    • Perkins, S.J.1    Wüthrich, K.2
  • 184
    • 0039009032 scopus 로고
    • Calculation of chemical shifts of protons on alpha carbons in proteins
    • M.P. Williamson, and T. Asakura Calculation of chemical shifts of protons on alpha carbons in proteins J. Magn. Reson. 94 1991 557 562
    • (1991) J. Magn. Reson. , vol.94 , pp. 557-562
    • Williamson, M.P.1    Asakura, T.2
  • 186
    • 0029437665 scopus 로고
    • Calibration of ring-current effects in proteins and nucleic acids
    • D.A. Case Calibration of ring-current effects in proteins and nucleic acids J. Biomol. NMR 6 1995 341 346
    • (1995) J. Biomol. NMR , vol.6 , pp. 341-346
    • Case, D.A.1
  • 187
    • 0028988451 scopus 로고
    • Application of H-1 NMR chemical shifts to measure the quality of protein structures
    • M.P. Williamson, J. Kikuchi, and T. Asakura Application of H-1 NMR chemical shifts to measure the quality of protein structures J. Mol. Biol. 247 1995 541 546
    • (1995) J. Mol. Biol. , vol.247 , pp. 541-546
    • Williamson, M.P.1    Kikuchi, J.2    Asakura, T.3
  • 189
    • 0027308278 scopus 로고
    • Secondary and tertiary structural effects on protein NMR chemical shifts: An ab initio approach
    • A.C. de Dios, J.G. Pearson, and E. Oldfield Secondary and tertiary structural effects on protein NMR chemical shifts: an ab initio approach Science 260 1993 1491 1496
    • (1993) Science , vol.260 , pp. 1491-1496
    • De Dios, A.C.1    Pearson, J.G.2    Oldfield, E.3
  • 190
    • 0037114648 scopus 로고    scopus 로고
    • 13C′ chemical shift is peptides using density functional theory
    • 13C′ chemical shift is peptides using density functional theory Biopolymers 65 2002 408 423
    • (2002) Biopolymers , vol.65 , pp. 408-423
    • Xu, X.P.1    Case, D.A.2
  • 191
    • 0037094144 scopus 로고    scopus 로고
    • Carbon-13 NMR shielding in the twenty common amino acids: Comparisons with experimental results in proteins
    • H. Sun, L.K. Sanders, and E. Oldfield Carbon-13 NMR shielding in the twenty common amino acids: comparisons with experimental results in proteins J. Am. Chem. Soc. 124 2002 5486 5495
    • (2002) J. Am. Chem. Soc. , vol.124 , pp. 5486-5495
    • Sun, H.1    Sanders, L.K.2    Oldfield, E.3
  • 192
    • 0036025444 scopus 로고    scopus 로고
    • Chemical shifts in amino acids, peptides, and proteins: From quantum chemistry to drug design
    • E. Oldfield Chemical shifts in amino acids, peptides, and proteins: from quantum chemistry to drug design Annu. Rev. Phys. Chem. 53 2002 349 378
    • (2002) Annu. Rev. Phys. Chem. , vol.53 , pp. 349-378
    • Oldfield, E.1
  • 193
    • 67651230413 scopus 로고    scopus 로고
    • Protein NMR chemical shift calculations based on the automated fragmentation QM/MM approach
    • X. He, B. Wang, and K.M. Merz Jr. Protein NMR chemical shift calculations based on the automated fragmentation QM/MM approach J. Phys. Chem. B. 113 2009 10380 10388
    • (2009) J. Phys. Chem. B. , vol.113 , pp. 10380-10388
    • He, X.1    Wang, B.2    Merz Jr., K.M.3
  • 195
    • 0033064395 scopus 로고    scopus 로고
    • C-alpha and C-beta carbon-13 chemical shifts in proteins from an empirical database
    • M. Iwadate, T. Asakura, and M.P. Williamson C-alpha and C-beta carbon-13 chemical shifts in proteins from an empirical database J. Biomol. NMR 13 1999 199 211
    • (1999) J. Biomol. NMR , vol.13 , pp. 199-211
    • Iwadate, M.1    Asakura, T.2    Williamson, M.P.3
  • 196
    • 70349627256 scopus 로고    scopus 로고
    • Fast and accurate predictions of protein NMR chemical shifts from interatomic distances
    • K.J. Kohlhoff, P. Robustelli, A. Cavalli, X. Salvatella, and M. Vendruscolo Fast and accurate predictions of protein NMR chemical shifts from interatomic distances J. Am. Chem. Soc. 131 2009 13894 13895
    • (2009) J. Am. Chem. Soc. , vol.131 , pp. 13894-13895
    • Kohlhoff, K.J.1    Robustelli, P.2    Cavalli, A.3    Salvatella, X.4    Vendruscolo, M.5
  • 197
    • 34249098127 scopus 로고    scopus 로고
    • A new model for chemical shifts of amide hydrogens in proteins
    • S. Moon, and D.A. Case A new model for chemical shifts of amide hydrogens in proteins J. Biomol. NMR 38 2007 139 150
    • (2007) J. Biomol. NMR , vol.38 , pp. 139-150
    • Moon, S.1    Case, D.A.2
  • 198
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: Using hydrogen atom contacts in the choice of side-chain amide orientation
    • J.M. Word, S.C. Lovell, J.S. Richardson, and D.C. Richardson Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation J. Mol. Biol. 285 1999 1735 1747
    • (1999) J. Mol. Biol. , vol.285 , pp. 1735-1747
    • Word, J.M.1    Lovell, S.C.2    Richardson, J.S.3    Richardson, D.C.4
  • 201
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • R.A. Laskowski, J.A. Rullmannn, M.W. MacArthur, R. Kaptein, and J.M. Thornton AQUA and PROCHECK-NMR: programs for checking the quality of protein structures solved by NMR J. Biomol. NMR 8 1996 477 486
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 202
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • DOI 10.1023/A:1021614115432
    • T. Herrmann, P. Güntert, and K. Wüthrich Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS J. Biomol. NMR 24 2002 171 189 (Pubitemid 36113646)
    • (2002) Journal of Biomolecular NMR , vol.24 , Issue.3 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 203
    • 4644340524 scopus 로고    scopus 로고
    • Automated NMR structure calculation with CYANA
    • P. Güntert Automated NMR structure calculation with CYANA Methods Mol. Biol. 278 2004 353 378
    • (2004) Methods Mol. Biol. , vol.278 , pp. 353-378
    • Güntert, P.1
  • 207
    • 0029314335 scopus 로고
    • The impact of direct refinement against proton chemical shifts on protein structure determination by NMR
    • J. Kuszewski, A.M. Gronenborn, and G.M. Clore The impact of direct refinement against proton chemical shifts on protein structure determination by NMR J. Magn. Reson. B 107 1995 293 297
    • (1995) J. Magn. Reson. B , vol.107 , pp. 293-297
    • Kuszewski, J.1    Gronenborn, A.M.2    Clore, G.M.3
  • 209
    • 0031940562 scopus 로고    scopus 로고
    • GENFOLD: A genetic algorithm for folding protein structures using NMR restraints
    • M.J. Bayley, G. Jones, P. Willett, and M.P. Williamson GENFOLD: a genetic algorithm for folding protein structures using NMR restraints Protein Sci. 7 1998 491 499
    • (1998) Protein Sci. , vol.7 , pp. 491-499
    • Bayley, M.J.1    Jones, G.2    Willett, P.3    Williamson, M.P.4
  • 210
    • 0032568556 scopus 로고    scopus 로고
    • New methods of structure refinement for macromolecular structure determination by NMR
    • G.M. Clore, and A.M. Gronenborn New methods of structure refinement for macromolecular structure determination by NMR Proc. Natl. Acad. Sci. USA 95 1998 5891 5898
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 5891-5898
    • Clore, G.M.1    Gronenborn, A.M.2
  • 211
    • 0031450809 scopus 로고    scopus 로고
    • Predicting chemical shifts in proteins: Structure refinement of valine residues using ab initio and empirical geometry optimizations
    • J.G. Pearson, H. Le, L.K. Sanders, N. Godbout, R.H. Havlin, and E. Oldfield Predicting chemical shifts in proteins: structure refinement of valine residues using ab initio and empirical geometry optimizations J. Am. Chem. Soc. 119 1997 11941 11950
    • (1997) J. Am. Chem. Soc. , vol.119 , pp. 11941-11950
    • Pearson, J.G.1    Le, H.2    Sanders, L.K.3    Godbout, N.4    Havlin, R.H.5    Oldfield, E.6
  • 212
    • 0019074845 scopus 로고
    • Strategies for the uses of lanthanide NMR shift probes in the determination of protein structure in solutio. Application to the EF calcium binding site of carp parvalbumin
    • L. Lee, and B.D. Sykes Strategies for the uses of lanthanide NMR shift probes in the determination of protein structure in solutio. Application to the EF calcium binding site of carp parvalbumin Biophys. J. 32 1980 193 210
    • (1980) Biophys. J. , vol.32 , pp. 193-210
    • Lee, L.1    Sykes, B.D.2
  • 213
    • 0028900809 scopus 로고
    • Protein structure refinement based on paramagnetic NMR shifts: Applications to wild-type and mutant forms of cytochrome c
    • M. Gochin, and H. Roder Protein structure refinement based on paramagnetic NMR shifts: applications to wild-type and mutant forms of cytochrome c Protein Sci. 4 1995 296 305
    • (1995) Protein Sci. , vol.4 , pp. 296-305
    • Gochin, M.1    Roder, H.2
  • 214
    • 0030954693 scopus 로고    scopus 로고
    • Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins
    • L. Banci, I. Bertini, G.G. Savellini, A. Romagnoli, P. Turano, M.A. Cremonini, C. Luchinat, and H.B. Gray Pseudocontact shifts as constraints for energy minimization and molecular dynamics calculations on solution structures of paramagnetic metalloproteins Proteins 29 1997 68 76
    • (1997) Proteins , vol.29 , pp. 68-76
    • Banci, L.1    Bertini, I.2    Savellini, G.G.3    Romagnoli, A.4    Turano, P.5    Cremonini, M.A.6    Luchinat, C.7    Gray, H.B.8
  • 216
    • 3042807889 scopus 로고    scopus 로고
    • Site-specific labelling with a metal chelator for protein-structure refinement
    • G. Pintacuda, A. Moshref, A. Leonchiks, A. Sharipo, and G. Otting Site-specific labelling with a metal chelator for protein-structure refinement J. Biomol. NMR 29 2004 351 361
    • (2004) J. Biomol. NMR , vol.29 , pp. 351-361
    • Pintacuda, G.1    Moshref, A.2    Leonchiks, A.3    Sharipo, A.4    Otting, G.5
  • 217
  • 218
    • 0036175913 scopus 로고    scopus 로고
    • Efficiency of paramagnetism-based constraints to determine the spatial arrangement of alpha-helical secondary structure elements
    • I. Bertini, M. Longinetti, C. Luchinat, G. Parigi, and L. Sgheri Efficiency of paramagnetism-based constraints to determine the spatial arrangement of alpha-helical secondary structure elements J. Biomol. NMR 22 2002 123 136
    • (2002) J. Biomol. NMR , vol.22 , pp. 123-136
    • Bertini, I.1    Longinetti, M.2    Luchinat, C.3    Parigi, G.4    Sgheri, L.5
  • 219
  • 220
    • 0034328688 scopus 로고    scopus 로고
    • 3D-1D threading methods for protein fold recognition
    • R. David, M.J. Korenberg, and I.W. Hunter 3D-1D threading methods for protein fold recognition Pharmacogenomics 1 2000 445 455
    • (2000) Pharmacogenomics , vol.1 , pp. 445-455
    • David, R.1    Korenberg, M.J.2    Hunter, I.W.3
  • 221
    • 0032828469 scopus 로고    scopus 로고
    • Analysis and assessment of ab initio three-dimensional prediction, secondary structure, and contacts prediction
    • C.A. Orengo, J.E. Bray, T. Hubbard, L. LoConte, and I. Sillitoe Analysis and assessment of ab initio three-dimensional prediction, secondary structure, and contacts prediction Proteins Suppl. 3 1999 149 170
    • (1999) Proteins Suppl. , vol.3 , pp. 149-170
    • Orengo, C.A.1    Bray, J.E.2    Hubbard, T.3    Loconte, L.4    Sillitoe, I.5
  • 223
    • 50649095790 scopus 로고    scopus 로고
    • Macromolecular modeling with Rosetta
    • R. Das, and D. Baker Macromolecular modeling with Rosetta Annu. Rev. Biochem. 77 2008 363 382
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 363-382
    • Das, R.1    Baker, D.2
  • 224
    • 30344488120 scopus 로고    scopus 로고
    • TASSER: An automated method for the prediction of protein tertiary structures in CASP6
    • Y. Zhang, A.K. Arakaki, and J. Skolnick TASSER: an automated method for the prediction of protein tertiary structures in CASP6 Proteins Suppl. 7 2005 91 98
    • (2005) Proteins Suppl. , vol.7 , pp. 91-98
    • Zhang, Y.1    Arakaki, A.K.2    Skolnick, J.3
  • 225
    • 0346103679 scopus 로고    scopus 로고
    • Rapid protein fold determination using unassigned NMR data
    • J. Meiler, and D. Baker Rapid protein fold determination using unassigned NMR data Proc. Natl. Acad. Sci. USA 100 2003 15404 15409
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 15404-15409
    • Meiler, J.1    Baker, D.2
  • 227
    • 34547572386 scopus 로고    scopus 로고
    • Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly
    • H. Gong, Y. Shen, and G.D. Rose Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly Protein Sci. 16 2007 1515 1521
    • (2007) Protein Sci. , vol.16 , pp. 1515-1521
    • Gong, H.1    Shen, Y.2    Rose, G.D.3
  • 229
    • 58149468410 scopus 로고    scopus 로고
    • De novo protein structure generation from incomplete chemical shift assignments
    • Y. Shen, R. Vernon, D. Baker, and A. Bax De novo protein structure generation from incomplete chemical shift assignments J. Biomol. NMR 43 2009 63 78
    • (2009) J. Biomol. NMR , vol.43 , pp. 63-78
    • Shen, Y.1    Vernon, R.2    Baker, D.3    Bax, A.4
  • 230
    • 76749107198 scopus 로고    scopus 로고
    • De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds
    • Y. Shen, P.N. Bryan, Y. He, J. Orban, D. Baker, and A. Bax De novo structure generation using chemical shifts for proteins with high-sequence identity but different folds Protein Sci. 19 2010 349 356
    • (2010) Protein Sci. , vol.19 , pp. 349-356
    • Shen, Y.1    Bryan, P.N.2    He, Y.3    Orban, J.4    Baker, D.5    Bax, A.6


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