Are Peptides Good Two-State Folders?

Are Peptides Good Two-State Folders?

Item
http://www.wikidata.org/entity/Q37122041
Inclusion of many-body effects in the additive CHARMM protein CMAP potential results in enhanced cooperativity of α-helix and β-hairpin formationAlzheimer Aβ peptide interactions with lipid membranes: fibrils, oligomers and polymorphic amyloid channels.Influence of Glu/Arg, Asp/Arg, and Glu/Lys Salt Bridges on α-Helical Stability and Folding KineticsSolvent-Exposed Salt Bridges Influence the Kinetics of α-Helix Folding and Unfolding.Note: network random walk model of two-state protein folding: test of the theory.Peptide dimerization-dissociation rates from replica exchange molecular dynamics.The role of entropy in initializing the aggregation of peptides: a first principle study on oligopeptide oligomerization.Variational Identification of Markovian Transition StatesConformational analysis of replica exchange MD: Temperature-dependent Markov networks for FF amyloid peptides
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Are Peptides Good Two-State Folders?

Item
http://www.wikidata.org/entity/Q37122041
description
article científic
@ca
article scientifique
@fr
articolo scientifico
@it
artigo científico
@pt
bilimsel makale
@tr
scientific article published on 25 July 2011
@en
vedecký článok
@sk
vetenskaplig artikel
@sv
videnskabelig artikel
@da
vědecký článek
@cs
name
Are Peptides Good Two-State Folders?
@en
Are Peptides Good Two-State Folders?
@nl
type
label
Are Peptides Good Two-State Folders?
@en
Are Peptides Good Two-State Folders?
@nl
prefLabel
Are Peptides Good Two-State Folders?
@en
Are Peptides Good Two-State Folders?
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
Are Peptides Good Two-State Folders?
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932