about
Balancing solvation and intramolecular interactions: toward a consistent generalized Born force fieldNecessity of high-resolution for coarse-grained modeling of flexible proteins.Variational Optimization of an All-Atom Implicit Solvent Force Field to Match Explicit Solvent Simulation Data.Structural reorganisation and potential toxicity of oligomeric species formed during the assembly of amyloid fibrils.Finite size effects in simulations of protein aggregation.Formation and growth of oligomers: a Monte Carlo study of an amyloid tau fragmentDissecting the mechanical unfolding of ubiquitin.Amyloid peptide Aβ40 inhibits aggregation of Aβ42: evidence from molecular dynamics simulations.Folding of proteins with diverse foldsApplication of the maximum entropy principle to determine ensembles of intrinsically disordered proteins from residual dipolar couplings.A Monte Carlo Study of the Early Steps of Functional Amyloid FormationAchieving secondary structural resolution in kinetic measurements of protein folding: a case study of the folding mechanism of Trp-cage.Discrete molecular dynamics: an efficient and versatile simulation method for fine protein characterization.A water-explicit lattice model of heat-, cold-, and pressure-induced protein unfoldingFurther optimization of a hybrid united-atom and coarse-grained force field for folding simulations: Improved backbone hydration and interactions between charged side chains.PRIMO: A Transferable Coarse-grained Force Field for Proteins.Using D-Amino Acids to Delineate the Mechanism of Protein Folding: Application to Trp-cage.Simulation of Top7-CFr: a transient helix extension guides folding.An effective all-atom potential for proteinsChanging the mechanical unfolding pathway of FnIII10 by tuning the pulling strength.Microscopic mechanism of specific peptide adhesion to semiconductor substrates.Folding of Top7 in unbiased all-atom Monte Carlo simulations.Canonical and micro-canonical analysis of folding of trpzip2: an all-atom replica exchange Monte Carlo simulation study.Hydrophobic interactions in the formation of secondary structures in small peptides
P2860
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P2860
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Folding thermodynamics of peptides.
@en
type
label
Folding thermodynamics of peptides.
@en
prefLabel
Folding thermodynamics of peptides.
@en
P2860
P1433
P1476
Folding thermodynamics of peptides.
@en
P2093
Sandipan Mohanty
P2860
P304
P356
10.1529/BIOPHYSJ.104.050427
P407
P577
2004-12-21T00:00:00Z
P5875
P698
P818
q-bio/0412007