Structural imperatives impose diverse evolutionary constraints on helical membrane proteins
about
Structural origins of nitroxide side chain dynamics on membrane protein α-helical sites.A sequence-based computational model for the prediction of the solvent accessible surface area for α-helix and β-barrel transmembrane residues.The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.The Impact of Native State Switching on Protein Sequence Evolution.Tolerance to changes in membrane lipid composition as a selected trait of membrane proteinsPredicting residue-residue contacts and helix-helix interactions in transmembrane proteins using an integrative feature-based random forest approachCalcium-release channels in paramecium. Genomic expansion, differential positioning and partial transcriptional elimination.EvoluCode: Evolutionary Barcodes as a Unifying Framework for Multilevel Evolutionary Data.Stable folding core in the folding transition state of an alpha-helical integral membrane protein.Marginally hydrophobic transmembrane α-helices shaping membrane protein folding.Quantitative residue-level structure-evolution relationships in the yeast membrane proteomeMembrane Proteins Are Dramatically Less Conserved than Water-Soluble Proteins across the Tree of LifeMembrane proteins can have high kinetic stability.The rhomboid protease family: a decade of progress on function and mechanism.Design of self-assembling transmembrane helical bundles to elucidate principles required for membrane protein folding and ion transport.Comprehensive, structurally-informed alignment and phylogeny of vertebrate biogenic amine receptors.Reversible Unfolding of Rhomboid Intramembrane ProteasesArchitectural and thermodynamic principles underlying intramembrane protease function.Systematic Analyses and Prediction of Human Drug Side Effect Associated Proteins from the Perspective of Protein Evolution.Membrane environment imposes unique selection pressures on transmembrane domains of G protein-coupled receptorsStructural differences between thermophilic and mesophilic membrane proteins.Elucidating the genotype-phenotype relationships and network perturbations of human shared and specific disease genes from an evolutionary perspective.Protein conformational diversity correlates with evolutionary rate.Why are polar residues within the membrane core evolutionary conserved?
P2860
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P2860
Structural imperatives impose diverse evolutionary constraints on helical membrane proteins
description
2009 nî lūn-bûn
@nan
2009 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Structural imperatives impose ...... s on helical membrane proteins
@ast
Structural imperatives impose ...... s on helical membrane proteins
@en
type
label
Structural imperatives impose ...... s on helical membrane proteins
@ast
Structural imperatives impose ...... s on helical membrane proteins
@en
prefLabel
Structural imperatives impose ...... s on helical membrane proteins
@ast
Structural imperatives impose ...... s on helical membrane proteins
@en
P2093
P2860
P356
P1476
Structural imperatives impose ...... s on helical membrane proteins
@en
P2093
Amit Oberai
Frank K Pettit
James U Bowie
P2860
P304
17747-17750
P356
10.1073/PNAS.0906390106
P407
P50
P577
2009-10-06T00:00:00Z