-
2
-
-
0029900275
-
15N chemical shift anisotropy from quantitative measurement of relaxation interference effects
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15N chemical shift anisotropy from quantitative measurement of relaxation interference effects. J Am Chem Soc. 118:1996;6986-6991.
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(1996)
J Am Chem Soc
, vol.118
, pp. 6986-6991
-
-
Tjandra, N.1
Szabo, A.2
Bax, A.3
-
3
-
-
0000698894
-
Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules
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Ross A, Czisch M, King GC. Systematic errors associated with the CPMG pulse sequence and their effect on motional analysis of biomolecules. J Magn Reson. 124:1997;355-365.
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(1997)
J Magn Reson
, vol.124
, pp. 355-365
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Ross, A.1
Czisch, M.2
King, G.C.3
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6
-
-
0000517765
-
15N relaxation data from the side chains of asparagine and glutamine residues in proteins
-
15N relaxation data from the side chains of asparagine and glutamine residues in proteins. J Magn Reson Ser B. 107:1995;279-285.
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(1995)
J Magn Reson Ser B
, vol.107
, pp. 279-285
-
-
Boyd, J.1
-
8
-
-
0029905210
-
13C NMR relaxation analysis
-
12C nuclei and random fractional deuteration to obtain isolated IS spin systems. A broad range of sidechain dynamics properties are observed, including millisecond motions that are proposed to contribute to the reactivity of the active-site disulfide bond. of outstanding interest
-
12C nuclei and random fractional deuteration to obtain isolated IS spin systems. A broad range of sidechain dynamics properties are observed, including millisecond motions that are proposed to contribute to the reactivity of the active-site disulfide bond. of outstanding interest.
-
(1996)
J Am Chem Soc
, vol.118
, pp. 9263-9272
-
-
Lemaster, D.M.1
Kushlan, D.M.2
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12
-
-
0029029566
-
Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling
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Brüschweiler R, Liao X, Wright PE. Long-range motional restrictions in a multidomain zinc-finger protein from anisotropic tumbling. Science. 268:1995;886-889.
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(1995)
Science
, vol.268
, pp. 886-889
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-
Brüschweiler, R.1
Liao, X.2
Wright, P.E.3
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15
-
-
33646719091
-
Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity
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Lipari G, Szabo A. Model-free approach to the interpretation of nuclear magnetic resonance relaxation in macromolecules. 1. Theory and range of validity. J Am Chem Soc. 104:1982;4546-4559.
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(1982)
J Am Chem Soc
, vol.104
, pp. 4546-4559
-
-
Lipari, G.1
Szabo, A.2
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16
-
-
0028541223
-
A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization
-
Schurr JM, Babcock HP, Fujimoto BS. A test of the model-free formulas. Effects of anisotropic rotational diffusion and dimerization. J Magn Reson Ser B. 105:1994;211-224.
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(1994)
J Magn Reson Ser B
, vol.105
, pp. 211-224
-
-
Schurr, J.M.1
Babcock, H.P.2
Fujimoto, B.S.3
-
18
-
-
0000411902
-
NMR order parameters of biomolecules: A new analytical representation and application to the Gaussian axial fluctuation model
-
Brüschweiler R, Wright PE. NMR order parameters of biomolecules: a new analytical representation and application to the Gaussian axial fluctuation model. J Am Chem Soc. 116:1994;8426-8427.
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(1994)
J Am Chem Soc
, vol.116
, pp. 8426-8427
-
-
Brüschweiler, R.1
Wright, P.E.2
-
19
-
-
0343697622
-
A protocol for the interpretation of side-chain dynamics based on NMR relaxation: Application to phenylalanines in antamanide
-
Bremi T, Brüschweiler R, Ernst RR. A protocol for the interpretation of side-chain dynamics based on NMR relaxation: application to phenylalanines in antamanide. J Am Chem Soc. 119:1997;4272-4284.
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(1997)
J Am Chem Soc
, vol.119
, pp. 4272-4284
-
-
Bremi, T.1
Brüschweiler, R.2
Ernst, R.R.3
-
21
-
-
0030473440
-
Insights into the local residual entropy of proteins provided by NMR relaxation
-
2 measured by NMR relaxation methods and the local configurational entropy of proteins. of special interest
-
2 measured by NMR relaxation methods and the local configurational entropy of proteins. of special interest.
-
(1996)
Protein Sci
, vol.5
, pp. 2647-2650
-
-
Li, Z.1
Raychaudhuri, S.2
Wand, A.J.3
-
22
-
-
0030601792
-
Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: Application to protein folding
-
The relationship between order parameters derived from NMR spin relaxation experiments and the contribution to conformational entropy from picosecond/nanosecond timescale bond vector dynamics is evaluated using classical and quantum mechanical models of bond vector motions. The local entropies and order parameters calculated from a 1.12 ns molecular dynamics trajectory of E. coli ribonuclease H are reproduced by using a simple expression based on the diffusion-in-a-cone model. of special interest
-
Yang D, Kay LE. Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding. J Mol Biol. 263:1996;369-382 The relationship between order parameters derived from NMR spin relaxation experiments and the contribution to conformational entropy from picosecond/nanosecond timescale bond vector dynamics is evaluated using classical and quantum mechanical models of bond vector motions. The local entropies and order parameters calculated from a 1.12 ns molecular dynamics trajectory of E. coli ribonuclease H are reproduced by using a simple expression based on the diffusion-in-a-cone model. of special interest.
-
(1996)
J Mol Biol
, vol.263
, pp. 369-382
-
-
Yang, D.1
Kay, L.E.2
-
23
-
-
0030445011
-
Dynamics of ribonuclease H: Temperature dependence of motions on multiple time scales
-
ex characterize the energetics of conformational fluctuations on picosecond/nanosecond and microsecond/millisecond timescales. of outstanding interest
-
ex characterize the energetics of conformational fluctuations on picosecond/nanosecond and microsecond/millisecond timescales. of outstanding interest.
-
(1996)
Biochemistry
, vol.35
, pp. 16009-16023
-
-
Mandel, A.M.1
Akke, M.2
Palmer, A.G.3
-
24
-
-
0029623152
-
Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields
-
Peng J, Wagner G. Frequency spectrum of NH bonds in eglin c from spectral density mapping at multiple fields. Biochemistry. 34:1995;16733-16752.
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(1995)
Biochemistry
, vol.34
, pp. 16733-16752
-
-
Peng, J.1
Wagner, G.2
-
26
-
-
0000808109
-
Dynamic studies of a fibronectin type I module pair at three frequencies: Anisotropic modeling and direct determination of conformational exchange
-
Phan IQH, Boyd J, Campbell ID. Dynamic studies of a fibronectin type I module pair at three frequencies: anisotropic modeling and direct determination of conformational exchange. J Biomol NMR. 8:1996;369-378.
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(1996)
J Biomol NMR
, vol.8
, pp. 369-378
-
-
Phan, I.Q.H.1
Boyd, J.2
Campbell, I.D.3
-
27
-
-
0001144784
-
1 constant-relaxation-time NMR spectroscopy
-
1 constant-relaxation-time NMR spectroscopy. J Am Chem Soc. 118:1996;911-912.
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(1996)
J Am Chem Soc
, vol.118
, pp. 911-912
-
-
Akke, M.1
Palmer, A.G.2
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28
-
-
0003075383
-
Quasi-spectral density function analysis for nitrogen-15 nuclei in proteins
-
Ishima R, Nagayama K. Quasi-spectral density function analysis for nitrogen-15 nuclei in proteins. J Magn Reson Ser B. 108:1995;73-76.
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(1995)
J Magn Reson Ser B
, vol.108
, pp. 73-76
-
-
Ishima, R.1
Nagayama, K.2
-
29
-
-
0029872895
-
Internal mobility in the partially folded DNA binding and dimerization domains of GAL4: NMR analysis of the N-H spectral density functions
-
N) that defines the rates for overall rotation and internal motions. of special interest
-
N) that defines the rates for overall rotation and internal motions. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 2674-2686
-
-
Lefevre, J.F.1
Dayie, K.T.2
Peng, J.W.3
Wagner, G.4
-
30
-
-
0031027137
-
Characterization of the backbone dynamics of folded and denatured states of an SH3 domain
-
15N NMR relaxation parameters are used to characterize the backbone dynamics of the folded and denatured states of the N-terminal SH3 domain from the adapter protein drk in high salt or guanidinium chloride, respectively, at 14 and 30°C. The value of J(O) for the unfolded state of the domain indicates that residues in the middle of the protein sequence are considerably less mobile than those at the termini. The picosecond/nanosecond motions in the unfolded SH3 domain are affected to a greater extent by changes in temperature than in the folded state. of outstanding interest
-
15N NMR relaxation parameters are used to characterize the backbone dynamics of the folded and denatured states of the N-terminal SH3 domain from the adapter protein drk in high salt or guanidinium chloride, respectively, at 14 and 30°C. The value of J(O) for the unfolded state of the domain indicates that residues in the middle of the protein sequence are considerably less mobile than those at the termini. The picosecond/nanosecond motions in the unfolded SH3 domain are affected to a greater extent by changes in temperature than in the folded state. of outstanding interest.
-
(1997)
Biochemistry
, vol.36
, pp. 2390-2402
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
31
-
-
0029938639
-
Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3
-
Feng Y, Klein BK, McWherter CA. Three-dimensional solution structure and backbone dynamics of a variant of human interleukin-3. J Mol Biol. 259:1996;524-541.
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(1996)
J Mol Biol
, vol.259
, pp. 524-541
-
-
Feng, Y.1
Klein, B.K.2
McWherter, C.A.3
-
32
-
-
0030043573
-
Phosphotransfer and CheY-binding domains of the histidine autokinase CheA are joined by a flexible linker
-
15N spin relaxation data are measured to study the dynamic properties of the protein histidine kinase CheA from E. coli. The phosphotransfer P1 domain and the CheY-binding P2 domain reorient independently, and the linker region is highly flexible. Regulation of CheA autophosphorylation activity is proposed to depend on access of the mean position of kinase domain to the phosphotransfer domain. of special interest
-
15N spin relaxation data are measured to study the dynamic properties of the protein histidine kinase CheA from E. coli. The phosphotransfer P1 domain and the CheY-binding P2 domain reorient independently, and the linker region is highly flexible. Regulation of CheA autophosphorylation activity is proposed to depend on access of the mean position of kinase domain to the phosphotransfer domain. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 433-443
-
-
Zhou, H.1
McEvoy, M.M.2
Lowry, D.F.3
Swanson, R.V.4
Simon, M.I.5
Dahlquist, F.W.6
-
34
-
-
0030026589
-
Backbone dynamics of a domain of protein L which binds to immunoglobulin light chains
-
Wikström M, Forsén S, Drakenberg T. Backbone dynamics of a domain of protein L which binds to immunoglobulin light chains. Eur J Biochem. 235:1996;543-548.
-
(1996)
Eur J Biochem
, vol.235
, pp. 543-548
-
-
Wikström, M.1
Forsén, S.2
Drakenberg, T.3
-
35
-
-
0028941877
-
Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme
-
Mandel AM, Akke M, Palmer AG. Backbone dynamics of Escherichia coli ribonuclease HI: Correlations with structure and function in an active enzyme. J Mol Biol. 246:1995;144-163.
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(1995)
J Mol Biol
, vol.246
, pp. 144-163
-
-
Mandel, A.M.1
Akke, M.2
Palmer, A.G.3
-
37
-
-
0029142571
-
Structural and dynamic characterization of the phosphotyrosine binding region of an Src homology 2 domain - phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches
-
Pascal SM, Yamazaki T, Singer AU, Kay LE, Forman-Kay JD. Structural and dynamic characterization of the phosphotyrosine binding region of an Src homology 2 domain - phosphopeptide complex by NMR relaxation, proton exchange, and chemical shift approaches. Biochemistry. 34:1995;11353-11362.
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(1995)
Biochemistry
, vol.34
, pp. 11353-11362
-
-
Pascal, S.M.1
Yamazaki, T.2
Singer, A.U.3
Kay, L.E.4
Forman-Kay, J.D.5
-
38
-
-
0030042698
-
Correlation between dynamics and high affinity binding in an SH2 domain interaction
-
2H-enriched SH2 domain of phospholipase C γ1. Comparisons between the dynamic properties of the free protein and those of the complex with a phosphotyrosine-containing peptide indicate that the dynamic properties of residues in and C-terminal to the phosphotyrosine-binding site contribute differentially to binding affinity and specificity. of outstanding interest
-
2H-enriched SH2 domain of phospholipase C γ1. Comparisons between the dynamic properties of the free protein and those of the complex with a phosphotyrosine-containing peptide indicate that the dynamic properties of residues in and C-terminal to the phosphotyrosine-binding site contribute differentially to binding affinity and specificity. of outstanding interest.
-
(1996)
Biochemistry
, vol.35
, pp. 361-368
-
-
Kay, L.E.1
Muhandiram, D.R.2
Farrow, N.A.3
Aubin, Y.4
Forman-Kay, J.D.5
-
39
-
-
0029967685
-
15N NMR relaxation measurements of hen egg white lysozyme denatured in trifluoroethanol
-
2>0.8 but also exhibit conformational exchange on a microsecond/millisecond timescale. of special interest
-
2>0.8 but also exhibit conformational exchange on a microsecond/millisecond timescale. of special interest.
-
(1996)
J Mol Biol
, vol.257
, pp. 669-683
-
-
Buck, M.1
Schwalbe, H.2
Dobson, C.M.3
-
40
-
-
0028787226
-
Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy
-
Frank MK, Clore GM, Gronenborn AM. Structural and dynamic characterization of the urea denatured state of the immunoglobulin binding domain of streptococcal protein G by multidimensional heteronuclear NMR spectroscopy. Protein Sci. 4:1995;2605-2615.
-
(1995)
Protein Sci
, vol.4
, pp. 2605-2615
-
-
Frank, M.K.1
Clore, G.M.2
Gronenborn, A.M.3
-
41
-
-
0030602880
-
15N NMR relaxation study
-
15N mainchain dynamics are compared for four forms of staphylococcal nuclease that have different stabilities. An increase in the proportion of residues with large-amplitude internal motions is observed as the stability of the folded state decreases. of special interest
-
15N mainchain dynamics are compared for four forms of staphylococcal nuclease that have different stabilities. An increase in the proportion of residues with large-amplitude internal motions is observed as the stability of the folded state decreases. of special interest.
-
(1996)
J Mol Biol
, vol.260
, pp. 570-587
-
-
Alexandrescu, A.T.1
Jahnke, W.2
Wiltscheck, R.3
Blommers, M.J.J.4
-
42
-
-
0028951040
-
Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer
-
Farrow NA, Zhang O, Forman-Kay JD, Kay LE. Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer. Biochemistry. 34:1995;868-878.
-
(1995)
Biochemistry
, vol.34
, pp. 868-878
-
-
Farrow, N.A.1
Zhang, O.2
Forman-Kay, J.D.3
Kay, L.E.4
-
43
-
-
0030299991
-
15N NMR relaxation studies of free and inhibitor-bound 4-oxalocrotonate tautomerase: Backbone dynamics and entropy changes of an enzyme upon inhibitor binding
-
2 increase for seven residues and decrease for eight residues upon binding of the inhibitor, suggesting that changes in configurational entropy from the increased rigidity of some residues are partially compensated by the increased flexibility of others. of outstanding interest
-
2 increase for seven residues and decrease for eight residues upon binding of the inhibitor, suggesting that changes in configurational entropy from the increased rigidity of some residues are partially compensated by the increased flexibility of others. of outstanding interest.
-
(1996)
Biochemistry
, vol.35
, pp. 16036-16047
-
-
Stivers, J.T.1
Abeygunawardana, C.2
Mildvan, A.S.3
Whitman, C.P.4
-
44
-
-
0031043596
-
1H exchange
-
1H exchange NMR measurements. Increased mobility and discrete disorder observed in the backbone of the unliganded protein may permit the entry of ligand into the binding cavity. of outstanding interest
-
1H exchange NMR measurements. Increased mobility and discrete disorder observed in the backbone of the unliganded protein may permit the entry of ligand into the binding cavity. of outstanding interest.
-
(1997)
Biochemistry
, vol.36
, pp. 2278-2290
-
-
Hodsdon, M.E.1
Cistola, D.P.2
-
45
-
-
0031001259
-
Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide
-
The backbone dynamics of the insulin receptor substrate 1 phosphotyrosine-binding domain are characterized in the presence and absence of phosphotyrosine peptide. The changes in conformational flexibility observed are compared with published results for the SH2 domain of phospholipase C γ1. of outstanding interest
-
Olejniczak ET, Zhou M-M, Fesik SW. Changes in the NMR-derived motional parameters of the insulin receptor substrate 1 phosphotyrosine binding domain upon binding to an interleukin 4 receptor phosphopeptide. Biochemistry. 36:1997;4118-4124 The backbone dynamics of the insulin receptor substrate 1 phosphotyrosine-binding domain are characterized in the presence and absence of phosphotyrosine peptide. The changes in conformational flexibility observed are compared with published results for the SH2 domain of phospholipase C γ1. of outstanding interest.
-
(1997)
Biochemistry
, vol.36
, pp. 4118-4124
-
-
Olejniczak, E.T.1
Zhou, M.-M.2
Fesik, S.W.3
-
46
-
-
0029764317
-
Backbone dynamics of the C-terminal domain of Escherichia coli topoisomerase I in the absence and presence of single-stranded DNA
-
2 for the majority of the residues. of special interest
-
2 for the majority of the residues. of special interest.
-
(1996)
Biochemistry
, vol.35
, pp. 9661-9666
-
-
Yu, L.1
Zhu, C.-X.2
Tse-Dinh, Y.-C.3
Fesik, S.W.4
-
47
-
-
0031031915
-
High resolution solution structure of ribosomal protein L11-C76, a helical protein with a flexible loop that becomes structured upon binding to RNA
-
15N transverse relaxation measurements suggest that the loop between helix α1 and strand β1 is flexible on a picosecond/nanosecond timescale in the free protein but not in the protein bound to RNA. of special interest
-
15N transverse relaxation measurements suggest that the loop between helix α1 and strand β1 is flexible on a picosecond/nanosecond timescale in the free protein but not in the protein bound to RNA. of special interest.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 70-77
-
-
Markus, M.A.1
Hinck, A.P.2
Huang, S.3
Draper, D.E.4
Torchia, D.A.5
-
48
-
-
0000760810
-
Flexibility of an arginine side chain at a DNA - protein interface
-
Berglund H, Baumann H, Knapp S, Ladenstein R, Härd T. Flexibility of an arginine side chain at a DNA - protein interface. J Am Chem Soc. 117:1995;12883-12884.
-
(1995)
J Am Chem Soc
, vol.117
, pp. 12883-12884
-
-
Berglund, H.1
Baumann, H.2
Knapp, S.3
Ladenstein, R.4
Härd, T.5
-
50
-
-
0029102089
-
Dynamics of the dihydrofolate reductase - folate complex: Catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features
-
Epstein D, Benkovic SJ, Wright PE. Dynamics of the dihydrofolate reductase - folate complex: catalytic sites and regions known to undergo conformational change exhibit diverse dynamical features. Biochemistry. 34:1995;11037-11048.
-
(1995)
Biochemistry
, vol.34
, pp. 11037-11048
-
-
Epstein, D.1
Benkovic, S.J.2
Wright, P.E.3
-
52
-
-
0028921302
-
Flexibility and function in HIV-1 protease
-
Nicholson LK, Yamazaki T, Torchia DA, Grzesiek S, Bax A, Stahl S, Kaufman JD, Wingfield PT, Lam PYS, Jadhav PK, et al. Flexibility and function in HIV-1 protease. Nat Struct Biol. 2:1995;274-280.
-
(1995)
Nat Struct Biol
, vol.2
, pp. 274-280
-
-
Nicholson, L.K.1
Yamazaki, T.2
Torchia, D.A.3
Grzesiek, S.4
Bax, A.5
Stahl, S.6
Kaufman, J.D.7
Wingfield, P.T.8
Lam, P.Y.S.9
Jadhav, P.K.10
-
55
-
-
0031556949
-
Module - module interactions in the cell binding region of fibronectin: Stability, flexibility and specificity
-
Thermodynamic and NMR spectroscopic techniques are used to investigate domain - domain interactions between the ninth and tenth type III domains of fibronectin. The relative contributions of specific domain - domain interactions, long-range nonspecific interactions, and excluded volume effects in constraining the relative motions and orientations of the domains are assessed. of special interest
-
Spitzfaden C, Grant RP, Mardon HJ, Campbell ID. Module - module interactions in the cell binding region of fibronectin: stability, flexibility and specificity. J Mol Biol. 265:1997;565-579 Thermodynamic and NMR spectroscopic techniques are used to investigate domain - domain interactions between the ninth and tenth type III domains of fibronectin. The relative contributions of specific domain - domain interactions, long-range nonspecific interactions, and excluded volume effects in constraining the relative motions and orientations of the domains are assessed. of special interest.
-
(1997)
J Mol Biol
, vol.265
, pp. 565-579
-
-
Spitzfaden, C.1
Grant, R.P.2
Mardon, H.J.3
Campbell, I.D.4
-
56
-
-
0031566955
-
Heteronuclear NMR studies of E. coli translation initiation factor IF3. Evidence that the inter-domain region is disordered in solution
-
15N lysine residues demonstrates that the interdomain linker is highly flexible. Rotational diffusion of the two domains appears uncorrelated. of special interest
-
15N lysine residues demonstrates that the interdomain linker is highly flexible. Rotational diffusion of the two domains appears uncorrelated. of special interest.
-
(1997)
J Mol Biol
, vol.266
, pp. 15-22
-
-
Moreau, M.1
De Cock, E.2
Fortier, P.-L.3
Garcia, C.4
Albaret, C.5
Blanquet, S.6
Lallemand, J.-Y.7
Dardel, F.8
-
57
-
-
0030963093
-
Defining long range order in NMR structure determination from the dependence of heteronuclear relaxation times on rotational diffusion anisotropy
-
15N relaxation rate constants on rotational diffusion anisotropy is used to refine the relative orientations of the α and α/β domains of Enzyme I by using a simulated annealing protocol. of outstanding interest
-
15N relaxation rate constants on rotational diffusion anisotropy is used to refine the relative orientations of the α and α/β domains of Enzyme I by using a simulated annealing protocol. of outstanding interest.
-
(1997)
Nat Struct Biol
, vol.4
, pp. 443-449
-
-
Tjandra, N.1
Garrett, D.S.2
Gronenborn, A.M.3
Bax, A.4
Clore, G.M.5
-
59
-
-
0029996040
-
Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR
-
Williams KA, Farrow NA, Deber CM, Kay LE. Structure and dynamics of bacteriophage IKe major coat protein in MPG micelles by solution NMR. Biochemistry. 35:1996;5145-5157.
-
(1996)
Biochemistry
, vol.35
, pp. 5145-5157
-
-
Williams, K.A.1
Farrow, N.A.2
Deber, C.M.3
Kay, L.E.4
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