Protein sequence entropy is closely related to packing density and hydrophobicity.
about
Causes of evolutionary rate variation among protein sitesComparing Residue Clusters from Thermophilic and Mesophilic Enzymes Reveals Adaptive MechanismsSite-specific structural constraints on protein sequence evolutionary divergence: local packing density versus solvent exposure.Exploring the aggregation propensity of γS-crystallin protein variants using two-dimensional spectroscopic toolsPredicting evolutionary site variability from structure in viral proteins: buriedness, packing, flexibility, and design.(PS)2: protein structure prediction server version 3.0.Dissecting the roles of local packing density and longer-range effects in protein sequence evolutionEvolutionary information hidden in a single protein structure.On the relationship between the sequence conservation and the packing density profiles of the protein complexes.Hydrogen bonding and packing density are factors most strongly connected to limiting sites of high flexibility in the 16S rRNA in the 30S ribosome.A mechanistic stress model of protein evolution accounts for site-specific evolutionary rates and their relationship with packing density and flexibility.Local packing density is the main structural determinant of the rate of protein sequence evolution at site level.Conservation and relative importance of residues across protein-protein interfacesComparative analysis of zinc finger proteins involved in plant disease resistanceProtein structural modularity and robustness are associated with evolvability.Packing regularities in biological structures relate to their dynamics.Measuring the functional sequence complexity of proteins.Hydrogen-bonding and packing features of membrane proteins: functional implicationsThree dimensional structure directs T-cell epitope dominance associated with allergy.Antigen structure influences helper T-cell epitope dominance in the human immune response to HIV envelope glycoprotein gp120.Signatures of the Protein Folding Pathway in Two-Dimensional Ultraviolet Spectroscopy.Relationship between protein thermodynamic constraints and variation of evolutionary rates among sites.Logistic regression models to predict solvent accessible residues using sequence- and homology-based qualitative and quantitative descriptors applied to a domain-complete X-ray structure learning set.Sequence analysis on the information of folding initiation segments in ferredoxin-like fold proteins.Intermediate divergence levels maximize the strength of structure-sequence correlations in enzymes and viral proteins.The Extent of Cooperativity of Protein Motions Observed with Elastic Network Models Is Similar for Atomic and Coarser-Grained Models.Altered dynamics upon oligomerization corresponds to key functional sites.
P2860
Q26771275-59B0BAEA-9693-4762-A242-32B57EDBFA7BQ28552190-643A5807-4725-48F4-998C-F046F02CA54FQ30354287-A6558189-E9BD-42AB-BC56-10A64AF17E28Q30355498-D6738B8D-24B1-4804-85C6-80A5B8D6AB67Q30366748-10FA040A-4185-4A3A-A253-4DA0683AC995Q30374402-EC9606A5-7F4D-4BB6-84C8-7A73CAB8B394Q30385799-874E1703-8636-4D47-B413-70759DD72359Q30414685-3EBB697B-6BF9-4BB3-9282-B677665B8FE9Q30427194-6DB43E36-9DDA-47C7-9472-2B8208699247Q33488694-0376F25E-EC66-4BC5-A1AC-9AA9EA4D04DBQ33914037-C74A1BE0-C79A-466E-9F05-BBA39EC1A81AQ33994037-ABC85BBD-D280-4D6F-A770-56AE1C241DB2Q34098437-E2212973-5730-4EE9-B4D1-72379E6AC829Q34390897-9D07B959-5917-4396-85AD-90D509E468FDQ35101254-2026A17D-26B0-4B36-8DD2-EA5825F0D174Q36087287-C415FA91-9DBF-4763-AB15-44CC3C605EA3Q36412719-A983AF22-A115-4432-A449-F3EEDB1D178FQ36481425-C12460FD-3206-4BF6-BFDF-68CF28B545B0Q36908976-3782123A-D028-4052-BD24-AD95BA475667Q37373708-F0AA258A-A0D2-44E1-83C5-4ACD85DCC73AQ37723506-92CF9ADB-CA70-470B-8B2E-241650C5DEADQ39464968-44FDD62B-021C-475A-AE1F-4910D5621C33Q40214668-EAC09CB1-18A0-4610-9391-BAC3A0D88B7EQ40650676-8F3E0185-F6BF-400F-AE8F-351FFC7866C6Q40856694-27022B38-68DF-4A3D-A676-B9976A910068Q42145221-ABACC530-5BD0-4E5D-96D4-9243DCA1B1EEQ48312992-B80262CD-2890-465D-8286-D3177FB40A14
P2860
Protein sequence entropy is closely related to packing density and hydrophobicity.
description
2005 nî lūn-bûn
@nan
2005年の論文
@ja
2005年学术文章
@wuu
2005年学术文章
@zh-cn
2005年学术文章
@zh-hans
2005年学术文章
@zh-my
2005年学术文章
@zh-sg
2005年學術文章
@yue
2005年學術文章
@zh
2005年學術文章
@zh-hant
name
Protein sequence entropy is closely related to packing density and hydrophobicity.
@en
type
label
Protein sequence entropy is closely related to packing density and hydrophobicity.
@en
prefLabel
Protein sequence entropy is closely related to packing density and hydrophobicity.
@en
P2093
P2860
P356
P1476
Protein sequence entropy is closely related to packing density and hydrophobicity.
@en
P2093
P2860
P356
10.1093/PROTEIN/GZI009
P577
2005-02-01T00:00:00Z