Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
about
Correlation as a determinant of configurational entropy in supramolecular and protein systemsStatistical thermodynamics of hindered rotation from computer simulationsLarge-scale molecular dynamics simulations of general anesthetic effects on the ion channel in the fully hydrated membrane: the implication of molecular mechanisms of general anesthesia.CHARMM: the biomolecular simulation programThe ensemble nature of allosteryNMR insights into protein allosteryProtein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3Solution Structure and Dynamics of the I214V Mutant of the Rabbit Prion ProteinMannosylglycerate stabilizes staphylococcal nuclease with restriction of slow β-sheet motionsSolution Structure and Dynamics of Human Hemoglobin in the Carbonmonoxy FormFringe-mediated extension of O-linked fucose in the ligand-binding region of Notch1 increases binding to mammalian Notch ligandsSolution structure, dynamics and binding studies of a family 11 carbohydrate-binding module from Clostridium thermocellum (CtCBM11)Chimeric Avidin – NMR Structure and Dynamics of a 56 kDa Homotetrameric Thermostable ProteinStructural characterization of zinc-bound Zmp1, a zinc-dependent metalloprotease secreted by Clostridium difficileBasis of Mutual Domain Inhibition in a Bacterial Response RegulatorTheory of free energy and entropy in noncovalent bindingConfigurational entropy in protein-peptide binding: computational study of Tsg101 ubiquitin E2 variant domain with an HIV-derived PTAP nonapeptideOn the relationship between NMR-derived amide order parameters and protein backbone entropy changesLoss of conformational entropy in protein folding calculated using realistic ensembles and its implications for NMR-based calculationsUltrafast NMR T1 relaxation measurements: probing molecular properties in real timeQuantitative comparison of errors in 15N transverse relaxation rates measured using various CPMG phasing schemesExtraction of configurational entropy from molecular simulations via an expansion approximationBinding Mechanism of the N-Terminal SH3 Domain of CrkII and Proline-Rich Motifs in cAblChanging the topology of protein backbone: the effect of backbone cyclization on the structure and dynamics of a SH3 domain.Characterizing the role of ensemble modulation in mutation-induced changes in binding affinityThe response of internal dynamics to hydrophobic core mutations in the SH3 domain from the Fyn tyrosine kinaseLigand-induced changes in dynamics in the RT loop of the C-terminal SH3 domain of Sem-5 indicate cooperative conformational coupling.Simultaneous determination of protein structure and dynamics.Internal dynamics of dynactin CAP-Gly is regulated by microtubules and plus end tracking protein EB1.Hydrophobic core mutations in CI2 globally perturb fast side-chain dynamics similarly without regard to position.The role of slow and fast protein motions in allosteric interactions.Conformational dynamics and thermodynamics of protein-ligand binding studied by NMR relaxation.Protein activity regulation by conformational entropy.Insight into the allosteric mechanism of Scapharca dimeric hemoglobinMolecular basis for the Cu2+ binding-induced destabilization of beta2-microglobulin revealed by molecular dynamics simulation.Rapid Determination of Fast Protein Dynamics from NMR Chemical Exchange Saturation Transfer DataInsights into equilibrium dynamics of proteins from comparison of NMR and X-ray data with computational predictions.Protein side-chain dynamics and residual conformational entropyThe physical basis of model-free analysis of NMR relaxation data from proteins and complex fluids.A surprising role for conformational entropy in protein function.
P2860
Q23909908-CB0A57CE-98B1-44AB-9809-BDBFF7EC5C97Q23912671-A668344B-0B61-44AD-9707-25FE655B66C5Q24541482-6AF25E4F-8310-4A2A-8BB6-E1DC274A3C05Q24658108-4483F0F1-5F66-4503-A379-C9D683698243Q26862004-6AD3031C-8ADC-4840-A948-4FAE70258362Q26863171-C69C4F57-BE40-48B4-A555-CC49D48BFF54Q27664681-4F529BD3-14BC-435F-B872-AFD2B0B8227FQ27665069-08E62480-0D1E-4458-BF4C-26E8D5619B22Q27679258-B3E43D30-DFE3-41B2-918E-A560E8C87151Q27679297-4DA5341D-A74C-4E65-B8ED-9AD05474E7D8Q27683660-0A578419-756C-4578-BD9E-7C3CF1B6AD70Q27683844-F1DDB0EF-4525-4754-8CB3-74FF9AF4F59CQ27684454-29FBC59A-72C3-454A-AAA3-848C56DD1A41Q27703263-9BC8023B-76A1-4760-9BFB-7AC268A3F3D5Q27727690-331859AD-2B78-43DD-97BF-CFC733C5BA9FQ28383645-8FD89F7F-39B5-48D6-8CD9-60E46769EC42Q28391435-1D6DFBA8-838B-4892-A375-610B69B931B3Q28391996-BCF85831-FE44-4083-B080-1B53F5D14085Q28397040-A71F4539-86B1-424F-8010-9E3BA3A76CE8Q28828614-AB080A13-4B6C-4B7D-B30B-131F93E35A96Q28833810-334691DE-E36D-43FB-9563-D32FC6039297Q29030427-67637658-9F7F-4B1A-94C7-96D6D51734A0Q30008899-DCFF2F7B-B1DC-4C5D-9AD4-12683103E63DQ30009183-054A7FA6-922C-4A4B-8B6C-9109B02EB9F1Q30157282-AE554EAA-8B90-495E-B196-BFF079285E0FQ30164208-783FCF5C-99A9-4E56-BEA6-1ADF4B34E3C4Q30164760-86478DF8-F5ED-474C-B501-B9A60128408EQ30349988-15FC1102-21AB-4436-A389-09BB966681E3Q30369179-77807819-DDDB-47ED-BD92-1E338F87F04FQ30370941-54DB6C1C-19D8-4530-BB2E-699D7364BB9CQ30402037-ABDBF325-D782-4DC7-B4C2-8E626165B123Q30414491-615B54E3-1216-43BA-8F9D-18A06D31F7CEQ30419233-96DFFC52-804D-46C7-A038-57BC6F992DA6Q30865627-628371C5-0C76-486F-AE66-F5264428738DQ31033432-7DCF6559-BE18-4836-913E-9075C8E87825Q31040837-26CE5267-44DB-43AE-AD36-1EB2EF0833A0Q31115351-F7FCFFFF-793B-4E8A-BAF0-E6C77A75E35AQ33395463-9EA222F3-E3A1-4A89-B761-D89E0FCA14D4Q33517752-0A69E31F-2E6A-4057-A878-30119132CA05Q33737180-EF25391C-26D7-4795-B2B9-0EC3B06F1901
P2860
Contributions to conformational entropy arising from bond vector fluctuations measured from NMR-derived order parameters: application to protein folding.
description
1996 nî lūn-bûn
@nan
1996 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
1996年の論文
@ja
1996年論文
@yue
1996年論文
@zh-hant
1996年論文
@zh-hk
1996年論文
@zh-mo
1996年論文
@zh-tw
1996年论文
@wuu
name
Contributions to conformationa ...... pplication to protein folding.
@ast
Contributions to conformationa ...... pplication to protein folding.
@en
type
label
Contributions to conformationa ...... pplication to protein folding.
@ast
Contributions to conformationa ...... pplication to protein folding.
@en
prefLabel
Contributions to conformationa ...... pplication to protein folding.
@ast
Contributions to conformationa ...... pplication to protein folding.
@en
P356
P1476
Contributions to conformationa ...... pplication to protein folding.
@en
P304
P356
10.1006/JMBI.1996.0581
P407
P577
1996-10-01T00:00:00Z