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Volumn 50, Issue 4, 2003, Pages 546-551

Observation of residual dipolar couplings in short peptides

Author keywords

Denatured proteins; Local steric hindrance; Molecular alignment; Residual dipolar couplings; Residual structure

Indexed keywords

MACROGOL; PEPTIDE; POLYACRYLAMIDE GEL;

EID: 0037340833     PISSN: 08873585     EISSN: None     Source Type: Journal    
DOI: 10.1002/prot.10327     Document Type: Article
Times cited : (35)

References (26)
  • 1
    • 0033200220 scopus 로고    scopus 로고
    • Establishing a degree of order: Obtaining highresolution NMR structures from molecular alignment
    • Tjandra N. Establishing a degree of order: obtaining highresolution NMR structures from molecular alignment. Structure 1999;7:R205-R211.
    • (1999) Structure , vol.7
    • Tjandra, N.1
  • 2
    • 0035919635 scopus 로고    scopus 로고
    • Persistence of native-like topology in a denatured protein in 8 M urea
    • Shortle D, Ackerman MS. Persistence of native-like topology in a denatured protein in 8 M urea. Science 2001;293:487-489.
    • (2001) Science , vol.293 , pp. 487-489
    • Shortle, D.1    Ackerman, M.S.2
  • 3
    • 0037022794 scopus 로고    scopus 로고
    • Molecular alignment of denatured states of staphylococcal nuclease with strained polyacrylamide gels and surfactant liquid crystalline phases
    • Ackerman MS, Shortle D. Molecular alignment of denatured states of staphylococcal nuclease with strained polyacrylamide gels and surfactant liquid crystalline phases. Biochemistry 2002;41:3089-3095.
    • (2002) Biochemistry , vol.41 , pp. 3089-3095
    • Ackerman, M.S.1    Shortle, D.2
  • 4
    • 0033730431 scopus 로고    scopus 로고
    • The Flory isolated-pair hypothesis is not valid for polypeptide chains: Implications for protein folding
    • Pappu RV, Srinivasan R, Rose GD. The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding. Proc Natl Acad Sci USA 2000;97:12565-12570.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 12565-12570
    • Pappu, R.V.1    Srinivasan, R.2    Rose, G.D.3
  • 5
    • 0036136694 scopus 로고    scopus 로고
    • Composites of local structure propensities: Evidence for local encoding of long-range structure
    • Shortle D. Composites of local structure propensities: evidence for local encoding of long-range structure. Protein Sci 2002;11:18-26.
    • (2002) Protein Sci , vol.11 , pp. 18-26
    • Shortle, D.1
  • 6
    • 0037551646 scopus 로고    scopus 로고
    • Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments
    • Ruckert M, Otting G. Alignment of biological macromolecules in novel nonionic liquid crystalline media for NMR experiments. J Am Chem Soc 2000;122:7793-7797.
    • (2000) J Am Chem Soc , vol.122 , pp. 7793-7797
    • Ruckert, M.1    Otting, G.2
  • 7
    • 0032042263 scopus 로고    scopus 로고
    • Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra
    • Ottiger M, Delaglio F, Bax A. Measurement of J and dipolar couplings from simplified two-dimensional NMR spectra. J Magn Reson 1998;131:373-378.
    • (1998) J Magn Reson , vol.131 , pp. 373-378
    • Ottiger, M.1    Delaglio, F.2    Bax, A.3
  • 8
    • 12644267957 scopus 로고
    • Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: Implications for studies of protein conformation
    • Kumar A, Wagner G, Ernst R, Wüthrich K. Buildup rates of the nuclear Overhauser effect measured by two-dimensional proton magnetic resonance spectroscopy: implications for studies of protein conformation. J Am Chem Soc 1981;103:3654-3658.
    • (1981) J Am Chem Soc , vol.103 , pp. 3654-3658
    • Kumar, A.1    Wagner, G.2    Ernst, R.3    Wüthrich, K.4
  • 9
    • 33748476849 scopus 로고
    • Suppresion of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence
    • Cavanagh J, Rance M. Suppresion of cross-relaxation effects in TOCSY spectra via a modified DIPSI-2 mixing sequence. J Magn Reson 1992;96:670-678.
    • (1992) J Magn Reson , vol.96 , pp. 670-678
    • Cavanagh, J.1    Rance, M.2
  • 10
    • 0024278597 scopus 로고
    • Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn
    • Dyson HJ, Rance M, Houghten RA, Lerner RA, Wright PE. Folding of immunogenic peptide fragments of proteins in water solution. I. Sequence requirements for the formation of a reverse turn. J Mol Biol 1988;201:161-200.
    • (1988) J Mol Biol , vol.201 , pp. 161-200
    • Dyson, H.J.1    Rance, M.2    Houghten, R.A.3    Lerner, R.A.4    Wright, P.E.5
  • 11
    • 0034721465 scopus 로고    scopus 로고
    • Alignment of biopolymers in strained gels: A new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR
    • Tycko R, Blanco FJ, Ishii Y. Alignment of biopolymers in strained gels: a new way to create detectable dipole-dipole couplings in high-resolution biomolecular NMR. J Am Chem Soc 2000;122:9340-9341.
    • (2000) J Am Chem Soc , vol.122 , pp. 9340-9341
    • Tycko, R.1    Blanco, F.J.2    Ishii, Y.3
  • 12
    • 0034501042 scopus 로고    scopus 로고
    • Solution NMR of proteins within polyacrylamide gels: Diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes
    • Sass HJ, Musco G, Stahl SJ, Wingfield PT, Grzesiek S. Solution NMR of proteins within polyacrylamide gels: diffusional properties and residual alignment by mechanical stress or embedding of oriented purple membranes. J Biomol NMR 2000;18:303-309.
    • (2000) J Biomol NMR , vol.18 , pp. 303-309
    • Sass, H.J.1    Musco, G.2    Stahl, S.J.3    Wingfield, P.T.4    Grzesiek, S.5
  • 13
    • 0012420595 scopus 로고    scopus 로고
    • Hercules, CA: Bio-Rad Laboratories
    • Technical bulletin 2068. Hercules, CA: Bio-Rad Laboratories; 2000.
    • (2000) Technical Bulletin 2068
  • 14
    • 0030722243 scopus 로고    scopus 로고
    • Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium
    • Tjandra N, Bax A. Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 1997;278:1111-1114.
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 15
    • 0032500340 scopus 로고    scopus 로고
    • Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium
    • Ramirez BE, Bax A. Modulation of the alignment tensor of macromolecules dissolved in a dilute liquid crystalline medium. J Am Chem Soc 1998;120:9106-9107
    • (1998) J Am Chem Soc , vol.120 , pp. 9106-9107
    • Ramirez, B.E.1    Bax, A.2
  • 16
    • 0034647237 scopus 로고    scopus 로고
    • Do bridging water molecules dictate the structure of a model dipeptide in aqueous solution?
    • Poon CD, Samulski ET, Weise CF, Weisshaar JC. Do bridging water molecules dictate the structure of a model dipeptide in aqueous solution? J Am Chem Soc 2000;122:5642-5643.
    • (2000) J Am Chem Soc , vol.122 , pp. 5642-5643
    • Poon, C.D.1    Samulski, E.T.2    Weise, C.F.3    Weisshaar, J.C.4
  • 17
    • 0034685436 scopus 로고    scopus 로고
    • Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR
    • Zweckstetter M, Bax A. Prediction of sterically induced alignment in a dilute liquid crystalline phase: aid to protein structure determination by NMR. J Am Chem Soc 2000;122:3791-3792.
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 19
    • 0014349486 scopus 로고
    • Dimensions of protein random coils
    • Miller WG, Goebel, C.V. Dimensions of protein random coils. Biochemistry 1968;7:3925-3935.
    • (1968) Biochemistry , vol.7 , pp. 3925-3935
    • Miller, W.G.1    Goebel, C.V.2
  • 20
    • 0032374091 scopus 로고    scopus 로고
    • Structural and dynamic characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus
    • Penkett CJ, Redfield C, Jones JA, Dodd I, Hubbard J, Smith RAG, Smith LJ, Dobson CM. Structural and dynamic characterization of a biologically active unfolded fibronectin-binding protein from Staphylococcus aureus. Biochemistry 1998;37:17054-17067.
    • (1998) Biochemistry , vol.37 , pp. 17054-17067
    • Penkett, C.J.1    Redfield, C.2    Jones, J.A.3    Dodd, I.4    Hubbard, J.5    Smith, R.A.G.6    Smith, L.J.7    Dobson, C.M.8
  • 22
    • 0034620764 scopus 로고    scopus 로고
    • Protein structure determination using molecular fragment replacement and NMR dipolar couplings
    • Delaglio F, Kontaxis G, Bax A. Protein structure determination using molecular fragment replacement and NMR dipolar couplings. J Am Chem Soc 2000;122:2142-2143.
    • (2000) J Am Chem Soc , vol.122 , pp. 2142-2143
    • Delaglio, F.1    Kontaxis, G.2    Bax, A.3
  • 23
    • 0035925135 scopus 로고    scopus 로고
    • Determination of protein backbone structure using only residual dipolar couplings
    • Hus JC, Marion D, Blackledge M. Determination of protein backbone structure using only residual dipolar couplings. J Am Chem Soc 2001;123:1541-1542.
    • (2001) J Am Chem Soc , vol.123 , pp. 1541-1542
    • Hus, J.C.1    Marion, D.2    Blackledge, M.3
  • 24
    • 0035925113 scopus 로고    scopus 로고
    • Structural and dynamic analysis of residual dipolar coupling data for proteins
    • Tolman JR, Al-Hashimi HM, Kay LE, Prestegard JH. Structural and dynamic analysis of residual dipolar coupling data for proteins. J Am Chem Soc 2001;123:1416-1424.
    • (2001) J Am Chem Soc , vol.123 , pp. 1416-1424
    • Tolman, J.R.1    Al-Hashimi, H.M.2    Kay, L.E.3    Prestegard, J.H.4
  • 25
    • 0034994293 scopus 로고    scopus 로고
    • The interrelationship of side-chain and main-chain conformations in proteins
    • Chakrabharti P, Pal D. The interrelationship of side-chain and main-chain conformations in proteins. Prog Biophys Mol Biol 2001;76:1-102.
    • (2001) Prog Biophys Mol Biol , vol.76 , pp. 1-102
    • Chakrabharti, P.1    Pal, D.2
  • 26
    • 0002006297 scopus 로고
    • Are there pathways for protein folding?
    • Levinthal C. Are there pathways for protein folding? J Chem Phys 1968;65:44-45.
    • (1968) J Chem Phys , vol.65 , pp. 44-45
    • Levinthal, C.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.