Coordination geometry of nonbonded residues in globular proteins.
about
Cooperative transition between open and closed conformations in potassium channelsRational Structure-Based Rescaffolding Approach to De Novo Design of Interleukin 10 (IL-10) Receptor-1 MimeticsEnvironment-dependent residue contact energies for proteins.Explicit orientation dependence in empirical potentials and its significance to side-chain modelingOrientation-dependent backbone-only residue pair scoring functions for fixed backbone protein design.An amino acid packing code for α-helical structure and protein designThermal stability limits of proteins in solution and adsorbed on a hydrophobic surface.New Dynamic Rotamer Libraries: Data-Driven Analysis of Side-Chain Conformational Propensities.Interactions of hydrophobic peptides with lipid bilayers: Monte Carlo simulations with M2delta.Comparative study of the effectiveness and limitations of current methods for detecting sequence coevolutionEmpirical solvent-mediated potentials hold for both intra-molecular and inter-molecular inter-residue interactionsOrientational potentials extracted from protein structures improve native fold recognition.Measures of residue density in protein structuresHow do side chains orient globally in protein structures?Monte Carlo studies of folding, dynamics, and stability in alpha-helices.Conformational dynamics of subtilisin-chymotrypsin inhibitor 2 complex by coarse-grained simulations.Identification of computational hot spots in protein interfaces: combining solvent accessibility and inter-residue potentials improves the accuracy.Optimum folding pathways of proteins: their determination and properties.
P2860
Q28473610-2FB2F985-28C4-4349-BA92-B50C840C6AAEQ28551658-FC67F28F-EDC5-4A23-B9A2-9221AD35BEC3Q30326368-A22107D4-F0B0-4123-8D81-F50A05AC5878Q30377118-762421C6-3FA9-4DB6-B2E3-C68183593EC9Q30388171-F8833DAC-F794-4C39-8AEF-F6612A3FB90CQ30414380-AFB003FE-EE19-4A16-8F82-3E87CC6CE03CQ30416194-9DE87CD5-37F8-400E-97FA-FE86A5EC62B8Q31035956-8F7468F6-41A5-44C9-A7DB-B29F362FD1A0Q33195458-F95226BB-B5E8-4203-8827-AA1ED339FFE6Q35784933-0BC98765-7F8C-4C8D-8EA1-1C0D84144BFDQ36280764-EBA17189-20A3-4E82-8F96-A34476D86DC5Q36519520-78C92DB5-0B22-4E9A-8889-BA8069B0FB06Q36543170-4475E963-6F39-4AB3-BBC7-1ABB735B98FBQ40191460-63836458-AF6C-4618-AEFD-80418B1D13AFQ40324007-74D14A5A-57C6-4354-ABFB-B180351B1025Q43595779-18A3DF0C-B70A-40EB-9A75-B249DA264D65Q45963927-CC218F79-7672-4634-8CC3-F0DA1564C0A4Q51226738-3C596AFA-5AD6-46E1-9FA3-078B0A98EAB1
P2860
Coordination geometry of nonbonded residues in globular proteins.
description
1996 nî lūn-bûn
@nan
1996 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1996 թվականի հունվարին 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
Coordination geometry of nonbonded residues in globular proteins.
@ast
Coordination geometry of nonbonded residues in globular proteins.
@en
type
label
Coordination geometry of nonbonded residues in globular proteins.
@ast
Coordination geometry of nonbonded residues in globular proteins.
@en
prefLabel
Coordination geometry of nonbonded residues in globular proteins.
@ast
Coordination geometry of nonbonded residues in globular proteins.
@en
P1433
P1476
Coordination geometry of nonbonded residues in globular proteins.
@en
P2093
P304
P356
10.1016/S1359-0278(96)00051-X
P577
1996-01-01T00:00:00Z