Non-alpha-helical elements modulate polytopic membrane protein architecture.
about
Membrane protein prediction methodsAdvances in Determination of a High-Resolution Three-Dimensional Structure of Rhodopsin, a Model of G-Protein-Coupled Receptors (GPCRs)The evolution of transmembrane helix kinks and the structural diversity of G protein-coupled receptorsShifting hydrogen bonds may produce flexible transmembrane helices.Assembly of the transmembrane domain of E. coli PhoQ histidine kinase: implications for signal transduction from molecular simulationsHydrogen/Deuterium Exchange Mass Spectrometry of Human Green Opsin Reveals a Conserved Pro-Pro Motif in Extracellular Loop 2 of Monostable Visual G Protein-Coupled Receptors.Efficient molecular mechanics simulations of the folding, orientation, and assembly of peptides in lipid bilayers using an implicit atomic solvation model.Structural details (kinks and non-alpha conformations) in transmembrane helices are intrahelically determined and can be predicted by sequence pattern descriptorsJoint-based description of protein structure: its application to the geometric characterization of membrane proteins.TMKink: a method to predict transmembrane helix kinks.Modelling the structures of G protein-coupled receptors aided by three-dimensional validation.Studies of yeast oligosaccharyl transferase subunits using the split-ubiquitin system: topological features and in vivo interactions.Helical packing patterns in membrane and soluble proteins.The crystallographic model of rhodopsin and its use in studies of other G protein-coupled receptors.Description of local and global shape properties of protein helices.Homology modeling of opioid receptor-ligand complexes using experimental constraintsOn the accuracy of homology modeling and sequence alignment methods applied to membrane proteinsHigh-resolution modeling of transmembrane helical protein structures from distant homologuesSolving the membrane protein folding problem.Structural basis for the function of a minimembrane protein subunit of yeast oligosaccharyltransferaseImpact of helix irregularities on sequence alignment and homology modeling of G protein-coupled receptors.Side-chain to main-chain hydrogen bonding controls the intrinsic backbone dynamics of the amyloid precursor protein transmembrane helixAn Extra Amino Acid Residue in Transmembrane Domain 10 of the γ-Aminobutyric Acid (GABA) Transporter GAT-1 Is Required for Efficient Ion-coupled Transport.Alpha-bulges in G protein-coupled receptors.The web server of IBM's Bioinformatics and Pattern Discovery group: 2004 update.Contribution of topology determinants of a viral movement protein to its membrane association, intracellular traffic, and viral cell-to-cell movementBak apoptotic pores involve a flexible C-terminal region and juxtaposition of the C-terminal transmembrane domains.Computational prediction of kink properties of helices in membrane proteins.Statistical analyses and computational prediction of helical kinks in membrane proteins.Mutational and bioinformatics analysis of proline- and glycine-rich motifs in vesicular acetylcholine transporter.Peptides as Bio-inspired Molecular Electronic Materials.Unwinding of the Substrate Transmembrane Helix in Intramembrane Proteolysis.The Approach of Conformational Chimeras to Model the Role of Proline-Containing Helices on GPCR Mobility: the Fertile Case of Cys-LTR1
P2860
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P2860
Non-alpha-helical elements modulate polytopic membrane protein architecture.
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@ast
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@en
type
label
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@ast
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@en
prefLabel
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@ast
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@en
P2093
P356
P1476
Non-alpha-helical elements modulate polytopic membrane protein architecture.
@en
P2093
P304
P356
10.1006/JMBI.2000.4402
P407
P577
2001-02-01T00:00:00Z