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Volumn 40, Issue 1, 2008, Pages 71-81

Influence of the fluctuations of the alignment tensor on the analysis of the structure and dynamics of proteins using residual dipolar couplings

Author keywords

Alignment tensor; Correlated motions; Protein dynamics; Residual dipolar couplings

Indexed keywords

ASPARTIC ACID; GLUTAMINE; GLYCINE; LEUCINE; UBIQUITIN;

EID: 37849041714     PISSN: 09252738     EISSN: 15735001     Source Type: Journal    
DOI: 10.1007/s10858-007-9210-6     Document Type: Article
Times cited : (25)

References (32)
  • 1
    • 0037215324 scopus 로고    scopus 로고
    • Weak alignment offers new NMR opportunities to study protein structure and dynamics
    • Bax A (2003) Weak alignment offers new NMR opportunities to study protein structure and dynamics. Prot Sci 12:1-16
    • (2003) Prot Sci , vol.12 , pp. 1-16
    • Bax, A.1
  • 2
    • 25844506708 scopus 로고    scopus 로고
    • Weak alignment NMR: A hawk-eyed view of biomolecular structure
    • Bax A, Grishaev A (2005) Weak alignment NMR: A hawk-eyed view of biomolecular structure. Curr Opin Struct Biol 15:1-8
    • (2005) Curr Opin Struct Biol , vol.15 , pp. 1-8
    • Bax, A.1    Grishaev, A.2
  • 3
    • 0034919243 scopus 로고    scopus 로고
    • Dipolar couplings in macromolecular structure determination
    • Bax A, Kontaxis G, Tjandra N (2001) Dipolar couplings in macromolecular structure determination. Meth Enzymol 339:127-174
    • (2001) Meth Enzymol , vol.339 , pp. 127-174
    • Bax, A.1    Kontaxis, G.2    Tjandra, N.3
  • 4
    • 3042588804 scopus 로고    scopus 로고
    • Local dynamic amplitudes on the protein backbone from dipolar couplings: Toward the elucidation of slower motions in biomolecules
    • Bernadó P, Blackledge M (2004) Local dynamic amplitudes on the protein backbone from dipolar couplings: Toward the elucidation of slower motions in biomolecules. J Am Chem Soc 126:7760-7761
    • (2004) J Am Chem Soc , vol.126 , pp. 7760-7761
    • Bernadó, P.1    Blackledge, M.2
  • 6
    • 3042639229 scopus 로고    scopus 로고
    • The origin of protein side-chain order parameter distribution
    • Best RB, Clarke J, Karplus M (2004) The origin of protein side-chain order parameter distribution. J Am Chem Soc 126:7734-7735
    • (2004) J Am Chem Soc , vol.126 , pp. 7734-7735
    • Best, R.B.1    Clarke, J.2    Karplus, M.3
  • 7
    • 14844353335 scopus 로고    scopus 로고
    • Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings
    • Blackledge M. (2005) Recent progress in the study of biomolecular structure and dynamics in solution from residual dipolar couplings. Prog Nucl Mag Res Spec 46:23-61
    • (2005) Prog Nucl Mag Res Spec , vol.46 , pp. 23-61
    • Blackledge, M.1
  • 9
    • 33845203743 scopus 로고    scopus 로고
    • Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings
    • Bouvignies G, Marwick P, Bruschweiler R, Blackledge M (2006) Simultaneous determination of protein backbone structure and dynamics from residual dipolar couplings. J Am Chem Soc 128:15100-15101
    • (2006) J Am Chem Soc , vol.128 , pp. 15100-15101
    • Bouvignies, G.1    Marwick, P.2    Bruschweiler, R.3    Blackledge, M.4
  • 11
    • 1542317796 scopus 로고    scopus 로고
    • How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation?
    • Clore GM, Schwieters CD (2004a) How much backbone motion in ubiquitin is required to account for dipolar coupling data measured in multiple alignment media as assessed by independent cross-validation? J Am Chem Soc 126:2923-2938
    • (2004) J Am Chem Soc , vol.126 , pp. 2923-2938
    • Clore, G.M.1    Schwieters, C.D.2
  • 12
    • 4143079167 scopus 로고    scopus 로고
    • Amplitudes of protein backbone dynamics and correlated motions in a small α/β protein: Correspondence of dipolar coupling and heteronuclear relaxation measurements
    • Clore GM, Schwieters CD (2004b) Amplitudes of protein backbone dynamics and correlated motions in a small α/β protein: Correspondence of dipolar coupling and heteronuclear relaxation measurements. Biochemistry 43:10678-10691
    • (2004) Biochemistry , vol.43 , pp. 10678-10691
    • Clore, G.M.1    Schwieters, C.D.2
  • 13
    • 0032528033 scopus 로고    scopus 로고
    • Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase
    • Cornilescu G, Marquardt JL, Ottiger M, Bax A (1998) Validation of protein structure from anisotropic carbonyl chemical shifts in a dilute liquid crystalline phase. J Am Chem Soc 120:6836-6837
    • (1998) J Am Chem Soc , vol.120 , pp. 6836-6837
    • Cornilescu, G.1    Marquardt, J.L.2    Ottiger, M.3    Bax, A.4
  • 14
    • 0037169646 scopus 로고    scopus 로고
    • NMR dipolar couplings for the structure determination of biopolymers in solution
    • de Alba E, Tjandra N (2002) NMR dipolar couplings for the structure determination of biopolymers in solution. Prog Nucl Mag Res Spec 40:175-197
    • (2002) Prog Nucl Mag Res Spec , vol.40 , pp. 175-197
    • de Alba, E.1    Tjandra, N.2
  • 15
    • 24944542708 scopus 로고    scopus 로고
    • Statistical coil model of the unfolded state: Resolving the reconciliation problem
    • Jha AK, Colubri A, Freed KF, Sosnick TR (2005) Statistical coil model of the unfolded state: Resolving the reconciliation problem. Proc Natl Acad Sci USA 102:13099-13104
    • (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
  • 16
    • 33645469988 scopus 로고    scopus 로고
    • A thorough dynamic interpretation of residual dipolar couplings in ubiquitin
    • Lakomek N, Carlomagno T, Becker S, Griesinger C, Meiler J (2006) A thorough dynamic interpretation of residual dipolar couplings in ubiquitin. J Biomol NMR 34:101-115
    • (2006) J Biomol NMR , vol.34 , pp. 101-115
    • Lakomek, N.1    Carlomagno, T.2    Becker, S.3    Griesinger, C.4    Meiler, J.5
  • 18
    • 33646719091 scopus 로고
    • Model-free approach to the interpretation of nuclear magnetic relaxation rates in macromolecules. 1. Theory and range of validity
    • Lipari G, Szabo A (1982) Model-free approach to the interpretation of nuclear magnetic relaxation rates in macromolecules. 1. Theory and range of validity. J Am Chem Soc 104:4546-4559
    • (1982) J Am Chem Soc , vol.104 , pp. 4546-4559
    • Lipari, G.1    Szabo, A.2
  • 19
    • 33645463245 scopus 로고    scopus 로고
    • Conformational fluctuations affect protein alignment in dilute liquid crystal media
    • Louhivuori M, Otten R, Lindorff-Larsen K, Annila A (2006) Conformational fluctuations affect protein alignment in dilute liquid crystal media. J Am Chem Soc 128:4371-4376
    • (2006) J Am Chem Soc , vol.128 , pp. 4371-4376
    • Louhivuori, M.1    Otten, R.2    Lindorff-Larsen, K.3    Annila, A.4
  • 20
    • 0038682826 scopus 로고    scopus 로고
    • Dipolar couplings in multiple alignments suggest α helical motion in ubiquitin
    • Meiler J, Peti W, Griesinger C (2003) Dipolar couplings in multiple alignments suggest α helical motion in ubiquitin. J Am Chem Soc 125:8072-8073
    • (2003) J Am Chem Soc , vol.125 , pp. 8072-8073
    • Meiler, J.1    Peti, W.2    Griesinger, C.3
  • 21
    • 0034820148 scopus 로고    scopus 로고
    • Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins
    • Meiler J, Prompers JJ, Peti W, Griesinger C, Bruschweiler R (2001) Model-free approach to the dynamic interpretation of residual dipolar couplings in globular proteins. J Am Chem Soc 123:6098-6107
    • (2001) J Am Chem Soc , vol.123 , pp. 6098-6107
    • Meiler, J.1    Prompers, J.J.2    Peti, W.3    Griesinger, C.4    Bruschweiler, R.5
  • 22
    • 0037157093 scopus 로고    scopus 로고
    • Model-free analysis of protein backbone motion from residual dipolar couplings
    • Peti W, Meiler J, Bruschweiler R, Griesinger C (2002) Model-free analysis of protein backbone motion from residual dipolar couplings. J Am Chem Soc 124:5822-5833
    • (2002) J Am Chem Soc , vol.124 , pp. 5822-5833
    • Peti, W.1    Meiler, J.2    Bruschweiler, R.3    Griesinger, C.4
  • 23
    • 33846532929 scopus 로고    scopus 로고
    • The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins
    • Richter B, Gsponer J, Värnai P, Salvatella X, Vendruscolo M (2007) The MUMO (minimal under-restraining minimal over-restraining) method for the determination of native state ensembles of proteins. J Biomol NMR 37:117-135
    • (2007) J Biomol NMR , vol.37 , pp. 117-135
    • Richter, B.1    Gsponer, J.2    Värnai, P.3    Salvatella, X.4    Vendruscolo, M.5
  • 25
    • 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 (1997) Direct measurement of distances and angles in biomolecules by NMR in a dilute liquid crystalline medium. Science 278:1111-1114
    • (1997) Science , vol.278 , pp. 1111-1114
    • Tjandra, N.1    Bax, A.2
  • 26
    • 33646931175 scopus 로고    scopus 로고
    • NMR residual dipolar couplings as probes of biomolecular dynamics
    • Tolman J, Ruan K (2006) NMR residual dipolar couplings as probes of biomolecular dynamics. Chem Rev 106:1720-1736
    • (2006) Chem Rev , vol.106 , pp. 1720-1736
    • Tolman, J.1    Ruan, K.2
  • 28
    • 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 (2001) Structural and dynamic analysis of residual dipolar coupling data for proteins. J Am Chem Soc 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
  • 29
    • 0023644679 scopus 로고
    • Structure of ubiquitin refined at 1.8 Å resolution
    • Vijay-Kumar S, Bugg CE, Cook WJ (1987) Structure of ubiquitin refined at 1.8 Å resolution. J Mol Biol 194:531-544
    • (1987) J Mol Biol , vol.194 , pp. 531-544
    • Vijay-Kumar, S.1    Bugg, C.E.2    Cook, W.J.3
  • 30
    • 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 (2000) Prediction of sterically induced alignment in a dilute liquid crystalline phase: Aid to protein structure determination by NMR. J Am Chem Soc 122:3791-3792
    • (2000) J Am Chem Soc , vol.122 , pp. 3791-3792
    • Zweckstetter, M.1    Bax, A.2
  • 31
    • 0035996721 scopus 로고    scopus 로고
    • Evaluation of uncertainty in alignment tensors obtained from dipolar couplings
    • Zweckstetter M, Bax A (2002) Evaluation of uncertainty in alignment tensors obtained from dipolar couplings. J Biomol NMR 23:127-137
    • (2002) J Biomol NMR , vol.23 , pp. 127-137
    • Zweckstetter, M.1    Bax, A.2
  • 32
    • 2942653357 scopus 로고    scopus 로고
    • Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases
    • Zweckstetter M, Hummer F, Bax A (2004) Prediction of charge-induced molecular alignment of biomolecules dissolved in dilute liquid-crystalline phases. Biophys J 86:2039-2046
    • (2004) Biophys J , vol.86 , pp. 2039-2046
    • Zweckstetter, M.1    Hummer, F.2    Bax, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.