Maximum allowed solvent accessibilites of residues in proteins
about
A local average distance descriptor for flexible protein structure comparisonCauses of evolutionary rate variation among protein sitesFunctional Sites Induce Long-Range Evolutionary Constraints in EnzymesDiversification and coevolution of the ghrelin/growth hormone secretagogue receptor system in vertebratesGenome of the pitcher plant Cephalotus reveals genetic changes associated with carnivoryAmino-acid site variability among natural and designed proteinsIdentification of diagnostic peptide regions that distinguish Zika virus from related mosquito-borne FlavivirusesPredicting evolutionary site variability from structure in viral proteins: buriedness, packing, flexibility, and design.Temperature dependence of amino acid hydrophobicities.The utility of protein structure as a predictor of site-wise dN/dS varies widely among HIV-1 proteins.Dissecting the roles of local packing density and longer-range effects in protein sequence evolutionEstimation of Position Specific Energy as a Feature of Protein Residues from Sequence Alone for Structural ClassificationDetermination of antigenicity-altering patches on the major surface protein of human influenza A/H3N2 virusesBiophysical Models of Protein Evolution: Understanding the Patterns of Evolutionary Sequence Divergence.The Impact of Native State Switching on Protein Sequence Evolution.Computational prediction of the tolerance to amino-acid deletion in green-fluorescent protein.On the Relationship between Residue Structural Environment and Sequence Conservation in Proteins.An experimentally determined evolutionary model dramatically improves phylogenetic fit.The inherent mutational tolerance and antigenic evolvability of influenza hemagglutinin.Local packing density is the main structural determinant of the rate of protein sequence evolution at site level.An experimentally informed evolutionary model improves phylogenetic fit to divergent lactamase homologsCoevolutionary Landscape Inference and the Context-Dependence of Mutations in Beta-Lactamase TEM-1.Too packed to change: side-chain packing and site-specific substitution rates in protein evolutionUniversal distribution of mutational effects on protein stability, uncoupling of protein robustness from sequence evolution and distinct evolutionary modes of prokaryotic and eukaryotic proteins.Geometric Constraints Dominate the Antigenic Evolution of Influenza H3N2 HemagglutininFunctional Constraint Profiling of a Viral Protein Reveals Discordance of Evolutionary Conservation and FunctionalityCoupling high-throughput genetics with phylogenetic information reveals an epistatic interaction on the influenza A virus M segment.Experimental Estimation of the Effects of All Amino-Acid Mutations to HIV's Envelope Protein on Viral Replication in Cell CultureSequence amplification via cell passaging creates spurious signals of positive adaptation in influenza virus H3N2 hemagglutininPrion protein β2-α2 loop conformational landscape.Annotating Protein Functional Residues by Coupling High-Throughput Fitness Profile and Homologous-Structure Analysis.Properties of Two Enterovirus Antibodies that are Utilized in Diabetes Research.Intermediate divergence levels maximize the strength of structure-sequence correlations in enzymes and viral proteins.Correlation of fitness landscapes from three orthologous TIM barrels originates from sequence and structure constraints.Membrane environment imposes unique selection pressures on transmembrane domains of G protein-coupled receptorsCharacterization of Fluorescein Arsenical Hairpin (FlAsH) as a Probe for Single-Molecule Fluorescence Spectroscopy.Net Evolutionary Loss of Residue Polarity in Drosophilid Protein Cores Indicates Ongoing Optimization of Amino Acid Composition.Measuring evolutionary rates of proteins in a structural context.Comprehensive review and empirical analysis of hallmarks of DNA-, RNA- and protein-binding residues in protein chains.Effects of force fields on the conformational and dynamic properties of amyloid β(1-40) dimer explored by replica exchange molecular dynamics simulations.
P2860
Q24567921-DAAE046A-E9B1-4349-B253-D1E6E6C40451Q26771275-36D15722-16CD-45DE-B272-6E1DAD03E73AQ28551771-8A53869F-401D-49BF-800A-4F99631BA367Q28602437-8A49912B-1E00-4637-B01C-CA19838B8978Q28709882-3A7DC0FD-D7DC-4130-97D6-004CDE7C8416Q28914724-6D3E78B9-64E3-4989-B4C4-D48E5F5D2E44Q30145545-289A05CE-CCC1-46E9-9560-53B1518E7F96Q30366748-983A6722-A8A8-4A7D-9135-22610C6B9472Q30375205-0E0DA731-4A8B-46B1-AA0A-2BC591C2DC6BQ30380281-0824ECF8-0AB6-452C-84F1-07071FB37F73Q30385799-6719F6F8-78A6-416C-9862-2FF428CF2037Q30392517-280CEC02-D874-434D-B318-98E7BFB72B5FQ30394447-6654F231-E2C4-4BF7-A97B-4986FFCD8B54Q30399998-A8620D87-E2D4-4875-A3F9-7E17CB2FBD44Q30400233-B8F35D30-DA9F-47FE-91B5-203D54F134CDQ30400620-BB377371-4284-4FF7-B9C9-A77FE43E5143Q30402886-1CFFCC7F-B717-439C-9FD1-82FE39EF5CABQ33923545-038D851E-A0F1-44B8-B3E0-091C44F62345Q33943327-9929294B-A2B5-459B-A527-14943F8DBB0EQ33994037-550B00BC-B9E9-45BD-B6D1-57B0F3D9CCFDQ34201879-D803AD7D-09FF-49CB-83D9-383EA6464F33Q34497324-61FED5FD-B75D-4988-A204-7D3CCF051B9FQ35544008-999BF106-22C5-494D-BBD4-3D73D684EE16Q35618960-77433BB7-0DBD-4321-AA65-2D2F60F0ADF3Q35644907-A91C5805-583F-419E-83E4-BC7E251EC3F2Q35680145-351F54E1-5C68-460F-9DA8-63C2388BC851Q35891196-0D25F88E-A533-48FD-ACC4-12CD270187E5Q36222292-F6BCE0CE-2969-412C-B0B5-8B968B9455ADQ37309428-3FE186A6-BC07-41EF-9CDF-868669E1FEF3Q38615490-1521030B-AE2A-4466-A3CD-7AB97A4A1196Q39226164-9AB59230-1A90-40AE-93A2-53D772549348Q40318281-80B565A1-693E-4930-B173-926FF826CB2BQ40856694-8DD5DAC6-09F6-427B-98DD-3E010C507448Q41768727-81778B52-FA6D-4551-938D-8186851DB292Q42146149-4989B04A-2891-439B-93BC-2174CC5A6E39Q42376076-AA1A831A-2B7A-4C60-8A69-460970C56E40Q46292727-489BCC4B-CA9A-43ED-B916-BA30F177A595Q47171147-B5643671-E4A8-4328-8E71-DC526B9F5815Q47281430-8BD52EE1-C615-4C6C-B051-E5283C70D96CQ47299318-D91D4611-6071-4277-A47F-DDB5C9BDB4A4
P2860
Maximum allowed solvent accessibilites of residues in proteins
description
2013 nî lūn-bûn
@nan
2013 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2013 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2013年の論文
@ja
2013年論文
@yue
2013年論文
@zh-hant
2013年論文
@zh-hk
2013年論文
@zh-mo
2013年論文
@zh-tw
2013年论文
@wuu
name
Maximum allowed solvent accessibilites of residues in proteins
@ast
Maximum allowed solvent accessibilites of residues in proteins
@en
type
label
Maximum allowed solvent accessibilites of residues in proteins
@ast
Maximum allowed solvent accessibilites of residues in proteins
@en
prefLabel
Maximum allowed solvent accessibilites of residues in proteins
@ast
Maximum allowed solvent accessibilites of residues in proteins
@en
P2860
P50
P1433
P1476
Maximum allowed solvent accessibilites of residues in proteins
@en
P2860
P304
P356
10.1371/JOURNAL.PONE.0080635
P407
P577
2013-11-21T00:00:00Z