Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
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Predicting helix-helix interactions from residue contacts in membrane proteinsWeb-based toolkits for topology prediction of transmembrane helical proteins, fold recognition, structure and binding scoring, folding-kinetics analysis and comparative analysis of domain combinationsSeqX: a tool to detect, analyze and visualize residue co-locations in protein and nucleic acid structuresComplete predicted three-dimensional structure of the facilitator transmembrane protein and hepatitis C virus receptor CD81: conserved and variable structural domains in the tetraspanin superfamily.Probabilistic grammatical model for helix‐helix contact site classificationA Specific Cholesterol Binding Site Is Established by the 2.8 Å Structure of the Human β2-Adrenergic ReceptorHeterologous expression and purification of an active human TRPV3 ion channelGenome-wide analysis of major intrinsic proteins in the tree plant Populus trichocarpa: characterization of XIP subfamily of aquaporins from evolutionary perspectiveMultipass membrane protein structure prediction using RosettaAlpha-helical topology prediction and generation of distance restraints in membrane proteins.The membrane- and soluble-protein helix-helix interactome: similar geometry via different interactions.An amino acid packing code for α-helical structure and protein designGlycines: role in α-helical membrane protein structures and a potential indicator of native conformation.Modeling the membrane environment has implications for membrane protein structure and function: influenza A M2 protein.A model of voltage gating developed using the KvAP channel crystal structure.Nuclear magnetic resonance solution structure of the Escherichia coli DNA polymerase III theta subunit.Solid-state NMR characterization of conformational plasticity within the transmembrane domain of the influenza A M2 proton channel.Role of Conserved Gly-Gly Pairs on the Periplasmic Side of LacY.Temporin-SHf, a new type of phe-rich and hydrophobic ultrashort antimicrobial peptide.Driving forces for transmembrane alpha-helix oligomerization.What is the role of amyloid precursor protein dimerization?Implications of threonine hydrogen bonding in the glycophorin A transmembrane helix dimer.Role of side-chain conformational entropy in transmembrane helix dimerization of glycophorin A.Interhelical angle and distance preferences in globular proteins.Binding of peptides with basic and aromatic residues to bilayer membranes: phenylalanine in the myristoylated alanine-rich C kinase substrate effector domain penetrates into the hydrophobic core of the bilayer.Helical packing patterns in membrane and soluble proteins.Helix packing and orientation in the transmembrane dimer of gp55-P of the spleen focus forming virus.Highly conserved tyrosine stabilizes the active state of rhodopsin.Comparison of class A and D G protein-coupled receptors: common features in structure and activation.Molecular dynamics of surfactant protein C: from single molecule to heptameric aggregates.Transmembrane peptide as potent inhibitor of oligomerization and function of human organic anion transporter 1.The GDA1_CD39 superfamily: NTPDases with diverse functions.An analysis of oligomerization interfaces in transmembrane proteins.Presenilin transmembrane domain 8 conserved AXXXAXXXG motifs are required for the activity of the γ-secretase complexInfluence of solubilizing environments on membrane protein structuresUncovering the triggers for GPCR activation using solid-state NMR spectroscopy.Stabilization of G protein-coupled receptors by point mutations.Homology modeling of major intrinsic proteins in rice, maize and Arabidopsis: comparative analysis of transmembrane helix association and aromatic/arginine selectivity filters.Developing a high-quality scoring function for membrane protein structures based on specific inter-residue interactions.The transmembrane prolines of the mitochondrial ADP/ATP carrier are involved in nucleotide binding and transport and its biogenesis
P2860
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P2860
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
description
2002 nî lūn-bûn
@nan
2002 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@ast
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@en
type
label
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@ast
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@en
prefLabel
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@ast
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@en
P2093
P2860
P1433
P1476
Comparison of helix interactions in membrane and soluble alpha-bundle proteins.
@en
P2093
Ashish B Patel
Markus Eilers
Steven O Smith
P2860
P304
P356
10.1016/S0006-3495(02)75613-0
P407
P577
2002-05-01T00:00:00Z