메뉴 건너뛰기




Volumn 367, Issue 5, 2007, Pages 1494-1510

Improved Structural Characterizations of the drkN SH3 Domain Unfolded State Suggest a Compact Ensemble with Native-like and Non-native Structure

Author keywords

ATCUN; disordered state; NMR; paramagnetic relaxation enhancement; residual structure

Indexed keywords

DROSOPHILA PROTEIN; PROTEIN DRKN; PROTEIN SH3; PROTEIN SUBUNIT; UNCLASSIFIED DRUG;

EID: 33947133083     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2007.01.038     Document Type: Article
Times cited : (102)

References (57)
  • 1
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • Dyson H.J., and Wright P.E. Intrinsically unstructured proteins and their functions. Nature Rev. Mol. Cell Biol. 6 (2005) 197-208
    • (2005) Nature Rev. Mol. Cell Biol. , vol.6 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 2
    • 1942521649 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state
    • Cho J.-H., Sato S., and Raleigh D.P. Thermodynamics and kinetics of non-native interactions in protein folding: a single point mutant significantly stabilizes the N-terminal domain of L9 by modulating non-native interactions in the denatured state. J. Mol. Biol. 338 (2004) 827-837
    • (2004) J. Mol. Biol. , vol.338 , pp. 827-837
    • Cho, J.-H.1    Sato, S.2    Raleigh, D.P.3
  • 3
    • 0035970299 scopus 로고    scopus 로고
    • Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states
    • Mok Y.K., Elisseeva E.L., Davidson A.R., and Forman-Kay J.D. Dramatic stabilization of an SH3 domain by a single substitution: roles of the folded and unfolded states. J. Mol. Biol. 307 (2001) 913-928
    • (2001) J. Mol. Biol. , vol.307 , pp. 913-928
    • Mok, Y.K.1    Elisseeva, E.L.2    Davidson, A.R.3    Forman-Kay, J.D.4
  • 5
    • 12944304172 scopus 로고    scopus 로고
    • Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations
    • Dedmon M.M., Lindorff-Larsen K., Christodoulou J., Vendruscolo M., and Dobson C.M. Mapping long-range interactions in alpha-synuclein using spin-label NMR and ensemble molecular dynamics simulations. J. Am. Chem. Soc. 127 (2005) 476-477
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 476-477
    • Dedmon, M.M.1    Lindorff-Larsen, K.2    Christodoulou, J.3    Vendruscolo, M.4    Dobson, C.M.5
  • 6
    • 0035957221 scopus 로고    scopus 로고
    • NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding
    • Yao J., Chung J., Eliezer D., Wright P.E., and Dyson H.J. NMR structural and dynamic characterization of the acid-unfolded state of apomyoglobin provides insights into the early events in protein folding. Biochemistry 40 (2001) 2571-3561
    • (2001) Biochemistry , vol.40 , pp. 2571-3561
    • Yao, J.1    Chung, J.2    Eliezer, D.3    Wright, P.E.4    Dyson, H.J.5
  • 7
    • 33751552347 scopus 로고    scopus 로고
    • Sensitivity of secondary structure propensities to sequence differences between alpha-and gamma-synuclein: implications for fibrillation
    • Marsh J.A., Singh V.K., Jia Z., and Forman-Kay J.D. Sensitivity of secondary structure propensities to sequence differences between alpha-and gamma-synuclein: implications for fibrillation. Protein Sci. 15 (2006) 2795-2804
    • (2006) Protein Sci. , vol.15 , pp. 2795-2804
    • Marsh, J.A.1    Singh, V.K.2    Jia, Z.3    Forman-Kay, J.D.4
  • 8
    • 0029961647 scopus 로고    scopus 로고
    • Structural analysis of non-native states of proteins by NMR methods
    • Shortle D.R. Structural analysis of non-native states of proteins by NMR methods. Curr. Opin. Struct. Biol. 6 (1996) 24-30
    • (1996) Curr. Opin. Struct. Biol. , vol.6 , pp. 24-30
    • Shortle, D.R.1
  • 9
    • 0035906650 scopus 로고    scopus 로고
    • Calculation of ensembles of structures representing the unfolded state of an SH3 domain
    • Choy W.Y., and Forman-Kay J.D. Calculation of ensembles of structures representing the unfolded state of an SH3 domain. J. Mol. Biol. 308 (2001) 1011-1032
    • (2001) J. Mol. Biol. , vol.308 , pp. 1011-1032
    • Choy, W.Y.1    Forman-Kay, J.D.2
  • 10
    • 24944542708 scopus 로고    scopus 로고
    • Statistical coil model of the unfolded state: resolving the reconciliation problem
    • Jha A.K., Colubri A., Freed K.F., and Sosnick T.R. Statistical coil model of the unfolded state: resolving the reconciliation problem. Proc. Natl Acad. Sci. USA 102 (2005) 13099-13104
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 13099-13104
    • Jha, A.K.1    Colubri, A.2    Freed, K.F.3    Sosnick, T.R.4
  • 11
    • 28044458515 scopus 로고    scopus 로고
    • A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering
    • Bernado P., Blanchard L., Timmins P., Marion D., Ruigrok R.W., and Blackledge M. A structural model for unfolded proteins from residual dipolar couplings and small-angle X-ray scattering. Proc. Natl Acad. Sci. USA 102 (2005) 17002-17007
    • (2005) Proc. Natl Acad. Sci. USA , vol.102 , pp. 17002-17007
    • Bernado, P.1    Blanchard, L.2    Timmins, P.3    Marion, D.4    Ruigrok, R.W.5    Blackledge, M.6
  • 12
    • 29844433240 scopus 로고    scopus 로고
    • Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings
    • Bernado P., Bertoncini C.W., Griesinger C., Zweckstetter M., and Blackledge M. Defining long-range order and local disorder in native alpha-synuclein using residual dipolar couplings. J. Am. Chem. Soc. 127 (2005) 17968-17969
    • (2005) J. Am. Chem. Soc. , vol.127 , pp. 17968-17969
    • Bernado, P.1    Bertoncini, C.W.2    Griesinger, C.3    Zweckstetter, M.4    Blackledge, M.5
  • 13
    • 0031585992 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures
    • Gillespie J.R., and Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. II. Distance restraints from paramagnetic relaxation and calculation of an ensemble of structures. J. Mol. Biol. 268 (1997) 170-184
    • (1997) J. Mol. Biol. , vol.268 , pp. 170-184
    • Gillespie, J.R.1    Shortle, D.2
  • 14
    • 0345598912 scopus 로고    scopus 로고
    • Structures and relative free energies of partially folded states of proteins
    • Vendruscolo M., Paci E., Karplus M., and Dobson C.M. Structures and relative free energies of partially folded states of proteins. Proc. Natl Acad. Sci. USA 100 (2003) 14817-14821
    • (2003) Proc. Natl Acad. Sci. USA , vol.100 , pp. 14817-14821
    • Vendruscolo, M.1    Paci, E.2    Karplus, M.3    Dobson, C.M.4
  • 15
    • 15244342213 scopus 로고    scopus 로고
    • Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies
    • Kristjansdottir S., Lindorff-Larsen K., Fieber W., Dobson C.M., Vendruscolo M., and Poulsen F.M. Formation of native and non-native interactions in ensembles of denatured ACBP molecules from paramagnetic relaxation enhancement studies. J. Mol. Biol. 347 (2005) 1053-1062
    • (2005) J. Mol. Biol. , vol.347 , pp. 1053-1062
    • Kristjansdottir, S.1    Lindorff-Larsen, K.2    Fieber, W.3    Dobson, C.M.4    Vendruscolo, M.5    Poulsen, F.M.6
  • 17
    • 33748268107 scopus 로고    scopus 로고
    • Characterization of the residual structure in the unfolded state of the Delta131Delta fragment of staphylococcal nuclease
    • Francis C.J., Lindorff-Larsen K., Best R.B., and Vendruscolo M. Characterization of the residual structure in the unfolded state of the Delta131Delta fragment of staphylococcal nuclease. Proteins: Struct. Funct. Genet. 65 (2006) 145-152
    • (2006) Proteins: Struct. Funct. Genet. , vol.65 , pp. 145-152
    • Francis, C.J.1    Lindorff-Larsen, K.2    Best, R.B.3    Vendruscolo, M.4
  • 18
    • 28244434114 scopus 로고    scopus 로고
    • Structural comparison of the unstable drkN SH3 domain and a stable mutant
    • Bezsonova I., Singer A., Choy W.Y., Tollinger M., and Forman-Kay J.D. Structural comparison of the unstable drkN SH3 domain and a stable mutant. Biochemistry 44 (2005) 15550-15560
    • (2005) Biochemistry , vol.44 , pp. 15550-15560
    • Bezsonova, I.1    Singer, A.2    Choy, W.Y.3    Tollinger, M.4    Forman-Kay, J.D.5
  • 19
    • 0030900199 scopus 로고    scopus 로고
    • NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions
    • Zhang O., and Forman-Kay J.D. NMR studies of unfolded states of an SH3 domain in aqueous solution and denaturing conditions. Biochemistry 36 (1997) 3959-3970
    • (1997) Biochemistry , vol.36 , pp. 3959-3970
    • Zhang, O.1    Forman-Kay, J.D.2
  • 20
    • 0038031645 scopus 로고    scopus 로고
    • Corrigendum to the paper by Mok et al. (1999). NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions
    • Crowhurst K.A., Choy W.Y., Mok Y.K., and Forman-Kay J.D. Corrigendum to the paper by Mok et al. (1999). NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions. J. Mol. Biol. 329 (2003) 185-187
    • (2003) J. Mol. Biol. , vol.329 , pp. 185-187
    • Crowhurst, K.A.1    Choy, W.Y.2    Mok, Y.K.3    Forman-Kay, J.D.4
  • 21
    • 0033546123 scopus 로고    scopus 로고
    • NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions
    • Mok Y.K., Kay C.M., Kay L.E., and Forman-Kay J. NOE data demonstrating a compact unfolded state for an SH3 domain under non-denaturing conditions. J. Mol. Biol. 289 (1999) 619-638
    • (1999) J. Mol. Biol. , vol.289 , pp. 619-638
    • Mok, Y.K.1    Kay, C.M.2    Kay, L.E.3    Forman-Kay, J.4
  • 22
    • 0041846681 scopus 로고    scopus 로고
    • Aromatic and methyl NOEs highlight hydrophobic clustering in the unfolded state of an SH3 domain
    • Crowhurst K.A., and Forman-Kay J.D. Aromatic and methyl NOEs highlight hydrophobic clustering in the unfolded state of an SH3 domain. Biochemistry 42 (2003) 8687-8695
    • (2003) Biochemistry , vol.42 , pp. 8687-8695
    • Crowhurst, K.A.1    Forman-Kay, J.D.2
  • 23
    • 0036966026 scopus 로고    scopus 로고
    • Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain
    • Crowhurst K.A., Tollinger M., and Forman-Kay J.D. Cooperative interactions and a non-native buried Trp in the unfolded state of an SH3 domain. J. Mol. Biol. 322 (2002) 163-178
    • (2002) J. Mol. Biol. , vol.322 , pp. 163-178
    • Crowhurst, K.A.1    Tollinger, M.2    Forman-Kay, J.D.3
  • 24
    • 26444479778 scopus 로고
    • Optimization by simulated annealing
    • Kirkpatrick S., Gelatt C.D., and Vecchi M.P. Optimization by simulated annealing. Science 221 (1983) 671-680
    • (1983) Science , vol.221 , pp. 671-680
    • Kirkpatrick, S.1    Gelatt, C.D.2    Vecchi, M.P.3
  • 26
    • 0034193509 scopus 로고    scopus 로고
    • A fast method to sample real protein conformational space
    • Feldman H.J., and Hogue C.W. A fast method to sample real protein conformational space. Proteins: Struct. Funct. Genet. 39 (2000) 112-131
    • (2000) Proteins: Struct. Funct. Genet. , vol.39 , pp. 112-131
    • Feldman, H.J.1    Hogue, C.W.2
  • 27
    • 0029884694 scopus 로고    scopus 로고
    • GOR method for predicting protein secondary structure from amino acid sequence
    • Garnier J., Gibrat J.F., and Robson B. GOR method for predicting protein secondary structure from amino acid sequence. Methods Enzymol. 266 (1996) 540-553
    • (1996) Methods Enzymol. , vol.266 , pp. 540-553
    • Garnier, J.1    Gibrat, J.F.2    Robson, B.3
  • 29
    • 0031585984 scopus 로고    scopus 로고
    • Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions
    • Simons K.T., Kooperberg C., Huang E., and Baker D. Assembly of protein tertiary structures from fragments with similar local sequences using simulated annealing and Bayesian scoring functions. J. Mol. Biol. 268 (1997) 209-225
    • (1997) J. Mol. Biol. , vol.268 , pp. 209-225
    • Simons, K.T.1    Kooperberg, C.2    Huang, E.3    Baker, D.4
  • 31
    • 0031585990 scopus 로고    scopus 로고
    • Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels
    • Gillespie J.R., and Shortle D. Characterization of long-range structure in the denatured state of staphylococcal nuclease. I. Paramagnetic relaxation enhancement by nitroxide spin labels. J. Mol. Biol. 268 (1997) 158-169
    • (1997) J. Mol. Biol. , vol.268 , pp. 158-169
    • Gillespie, J.R.1    Shortle, D.2
  • 32
    • 0035840960 scopus 로고    scopus 로고
    • Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy
    • Donaldson L.W., Skrynnikov N.R., Choy W.Y., Muhandiram D.R., Sarkar B., Forman-Kay J.D., and Kay L.E. Structural characterization of proteins with an attached ATCUN motif by paramagnetic relaxation enhancement NMR spectroscopy. J. Am. Chem. Soc. 123 (2001) 9843-9847
    • (2001) J. Am. Chem. Soc. , vol.123 , pp. 9843-9847
    • Donaldson, L.W.1    Skrynnikov, N.R.2    Choy, W.Y.3    Muhandiram, D.R.4    Sarkar, B.5    Forman-Kay, J.D.6    Kay, L.E.7
  • 33
    • 0016226901 scopus 로고
    • A peptide molecule mimicking the copper(II) transport site of human serum albumin. A comparative study between the synthetic site and albumin
    • Lau S.J., Kruck T.P., and Sarkar B. A peptide molecule mimicking the copper(II) transport site of human serum albumin. A comparative study between the synthetic site and albumin. J. Biol. Chem. 249 (1974) 5878-5884
    • (1974) J. Biol. Chem. , vol.249 , pp. 5878-5884
    • Lau, S.J.1    Kruck, T.P.2    Sarkar, B.3
  • 34
    • 2442433447 scopus 로고    scopus 로고
    • Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule
    • Iwahara J., Schwieters C.D., and Clore G.M. Ensemble approach for NMR structure refinement against (1)H paramagnetic relaxation enhancement data arising from a flexible paramagnetic group attached to a macromolecule. J. Am. Chem. Soc. 126 (2004) 5879-5896
    • (2004) J. Am. Chem. Soc. , vol.126 , pp. 5879-5896
    • Iwahara, J.1    Schwieters, C.D.2    Clore, G.M.3
  • 35
    • 0000224283 scopus 로고    scopus 로고
    • CHARMM: the energy function and its parameterization with an overview of the program
    • Schleyer P.V.R. (Ed), John Wiley & Sons, New York
    • MacKerell A.D., Brooks B., Brooks C.L., Nilsson L., Roux B., Won Y., and Karplus M. CHARMM: the energy function and its parameterization with an overview of the program. In: Schleyer P.V.R. (Ed). Encyclopedia of Computational Chemistry vol. 1 (1998), John Wiley & Sons, New York 271-277
    • (1998) Encyclopedia of Computational Chemistry , vol.1 , pp. 271-277
    • MacKerell, A.D.1    Brooks, B.2    Brooks, C.L.3    Nilsson, L.4    Roux, B.5    Won, Y.6    Karplus, M.7
  • 37
    • 0036401008 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectroscopy studies on copper proteins
    • Banci L., Pierattelli R., and Vila A.J. Nuclear magnetic resonance spectroscopy studies on copper proteins. Adv. Protein Chem. 60 (2002) 397-449
    • (2002) Adv. Protein Chem. , vol.60 , pp. 397-449
    • Banci, L.1    Pierattelli, R.2    Vila, A.J.3
  • 38
    • 36149008265 scopus 로고
    • Relaxation processes in a system of two spins
    • Solomon I. Relaxation processes in a system of two spins. Phys. Rev. 99 (1955) 559-565
    • (1955) Phys. Rev. , vol.99 , pp. 559-565
    • Solomon, I.1
  • 39
    • 36849133491 scopus 로고
    • Nuclear magnetic interactions in the HF molecule
    • Solomon I., and Bloembergen N. Nuclear magnetic interactions in the HF molecule. J. Chem. Phys. 25 (1956) 261-266
    • (1956) J. Chem. Phys. , vol.25 , pp. 261-266
    • Solomon, I.1    Bloembergen, N.2
  • 40
    • 0039573448 scopus 로고
    • Spin-label induced nuclear magnetic resonance relaxation studes of enzymes
    • Berliner L.J. (Ed), Academic Press, New York
    • Krugh T.R. Spin-label induced nuclear magnetic resonance relaxation studes of enzymes. In: Berliner L.J. (Ed). Spin Labeling: Theory and Applications vol. 1 (1976), Academic Press, New York 339-372
    • (1976) Spin Labeling: Theory and Applications , vol.1 , pp. 339-372
    • Krugh, T.R.1
  • 42
    • 0026597879 scopus 로고
    • The chemical shift index: a fast and simple method for the assignment of protein secondary structure through NMR spectroscopy
    • Wishart D.S., Sykes B.D., and Richards F.M. 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
  • 43
    • 0029207339 scopus 로고
    • 1H chemical shifts obtained as a function of temperature and trifluoroethanol concentration for the peptide series GGXGG
    • 1H 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
  • 44
    • 0029181728 scopus 로고
    • 15N random coil NMR chemical shifts of the common amino acids. I. Investigations of nearest-neighbor effects
    • 15N random coil NMR chemical shifts of the common amino acids. I. 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
  • 47
    • 0036300690 scopus 로고    scopus 로고
    • Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques
    • Choy W.Y., Mulder F.A., Crowhurst K.A., Muhandiram D.R., Millett I.S., Doniach S., et al. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. J. Mol. Biol. 316 (2002) 101-112
    • (2002) J. Mol. Biol. , vol.316 , pp. 101-112
    • Choy, W.Y.1    Mulder, F.A.2    Crowhurst, K.A.3    Muhandiram, D.R.4    Millett, I.S.5    Doniach, S.6
  • 48
    • 0001229341 scopus 로고    scopus 로고
    • Calculation of hydrodynamic properties of globular proteins from their atomic-level structure
    • Garcia De La Torre J., Huertas M.L., and Carrasco B. Calculation of hydrodynamic properties of globular proteins from their atomic-level structure. Biophys. J. 78 (2000) 719-730
    • (2000) Biophys. J. , vol.78 , pp. 719-730
    • Garcia De La Torre, J.1    Huertas, M.L.2    Carrasco, B.3
  • 50
    • 33846941955 scopus 로고    scopus 로고
    • Bezsonova, I., Evanics, F., Marsh, J. A., Forman-Kay, J. D. & Prosser, R. S. (2007). Oxygen as a paramagnetic probe of clustering and solvent exposure in folded and unfolded states of an SH3 domain. J. Am. Chem. Soc. In the press [Electronic publication ahead of print, Jan. 25/07].
  • 51
    • 0001144784 scopus 로고    scopus 로고
    • Monitoring macromolecular motions on microsecond to millisecond time scales by R1rho-R1 constant relaxation time NMR spectroscopy
    • Akke M., and Palmer A.G. Monitoring macromolecular motions on microsecond to millisecond time scales by R1rho-R1 constant relaxation time NMR spectroscopy. J. Am. Chem. Soc. 118 (1996) 911912
    • (1996) J. Am. Chem. Soc. , vol.118 , pp. 911912
    • Akke, M.1    Palmer, A.G.2
  • 54
    • 34249765651 scopus 로고
    • NMRView: a computer program for the visualization and analysis of NMR data
    • Johnson B., and Blevins R. NMRView: a computer program for the visualization and analysis of NMR data. J. Biol. NMR 4 (1994) 603-614
    • (1994) J. Biol. NMR , vol.4 , pp. 603-614
    • Johnson, B.1    Blevins, R.2
  • 55
    • 0033637626 scopus 로고    scopus 로고
    • A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment
    • Mueller G.A., Choy W.Y., Skrynnikov N.R., and Kay L.E. A method for incorporating dipolar couplings into structure calculations in cases of (near) axial symmetry of alignment. J. Biomol. NMR 18 (2000) 183-188
    • (2000) J. Biomol. NMR , vol.18 , pp. 183-188
    • Mueller, G.A.1    Choy, W.Y.2    Skrynnikov, N.R.3    Kay, L.E.4
  • 56
    • 0042511005 scopus 로고    scopus 로고
    • A graph-theory algorithm for rapid protein side-chain prediction
    • Canutescu A.A., Shelenkov A.A., and Dunbrack Jr. R.L. A graph-theory algorithm for rapid protein side-chain prediction. Protein Sci. 12 (2003) 2001-2014
    • (2003) Protein Sci. , vol.12 , pp. 2001-2014
    • Canutescu, A.A.1    Shelenkov, A.A.2    Dunbrack Jr., R.L.3
  • 57
    • 0033614004 scopus 로고    scopus 로고
    • Asparagine and glutamine: using hydrogen atom contacts in the choice of side-chain amide orientation
    • Word J.M., Lovell S.C., Richardson J.S., and Richardson D.C. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.