Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways
about
Structural Rigidity and Protein Thermostability in Variants of Lipase A from Bacillus subtilisSubstrate-induced changes in the structural properties of LacYEfficient unfolding pattern recognition in single molecule force spectroscopy data.Atomic force microscopy: a multifaceted tool to study membrane proteins and their interactions with ligands.Conservation of molecular interactions stabilizing bovine and mouse rhodopsin.Single-molecule force spectroscopy of G-protein-coupled receptors.Peptide transporter DtpA has two alternate conformations, one of which is promoted by inhibitor binding.Observing a lipid-dependent alteration in single lactose permeasesLocating an extracellular K+-dependent interaction site that modulates betaine-binding of the Na+-coupled betaine symporter BetP.Ligand-specific interactions modulate kinetic, energetic, and mechanical properties of the human β2 adrenergic receptor.Cholesterol increases kinetic, energetic, and mechanical stability of the human β2-adrenergic receptor.Role of extracellular glutamic acids in the stability and energy landscape of bacteriorhodopsinVertebrate membrane proteins: structure, function, and insights from biophysical approaches.The transition state for integral membrane protein foldingSubstrate binding tunes conformational flexibility and kinetic stability of an amino acid antiporter.Folding scene investigation: membrane proteins.Fuzzy oil drop model to interpret the structure of antifreeze proteins and their mutants.Distributions of experimental protein structures on coarse-grained free energy landscapes.Influence of proline on the thermostability of the active site and membrane arrangement of transmembrane proteins.Velocity-dependent mechanical unfolding of bacteriorhodopsin is governed by a dynamic interaction networkForced Unfolding Mechanism of Bacteriorhodopsin as Revealed by Coarse-Grained Molecular Dynamics.
P2860
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P2860
Point mutations in membrane proteins reshape energy landscape and populate different unfolding pathways
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 23 December 2007
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Point mutations in membrane pr ...... e different unfolding pathways
@en
Point mutations in membrane pr ...... different unfolding pathways.
@nl
type
label
Point mutations in membrane pr ...... e different unfolding pathways
@en
Point mutations in membrane pr ...... different unfolding pathways.
@nl
prefLabel
Point mutations in membrane pr ...... e different unfolding pathways
@en
Point mutations in membrane pr ...... different unfolding pathways.
@nl
P2093
P2860
P1476
Point mutations in membrane pr ...... e different unfolding pathways
@en
P2093
Dirk Labudde
G Prakash Balasubramanian
James U Bowie
K Tanuj Sapra
P2860
P304
P356
10.1016/J.JMB.2007.12.027
P407
P577
2007-12-23T00:00:00Z