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Energetics of protein hydrogen bondsStructural and Functional Studies of Truncated Hemolysin A from Proteus mirabilisMolecular mechanisms for protein-encoded inheritanceContribution of hydrogen bonds to protein stabilityInter-species cross-seeding: stability and assembly of rat-human amylin aggregatesSequential unfolding of the hemolysin two-partner secretion domain from Proteus mirabilis.TtOmp85, a β-barrel assembly protein, functions by barrel augmentationNucleation-dependent tau filament formation: the importance of dimerization and an estimation of elementary rate constantsExceptional rigidity and biomechanics of amyloid revealed by 4D electron microscopy.Thermodynamic selection of steric zipper patterns in the amyloid cross-beta spineThe importance of hydrogen bonding between the glutamine side chains to the formation of amyloid VQIVYK parallel beta-sheets: an ONIOM DFT/AM1 study.Mechanism of fiber assembly: treatment of Aβ peptide aggregation with a coarse-grained united-residue force field.Structural characterization of GNNQQNY amyloid fibrils by magic angle spinning NMRProtein amyloids develop an intrinsic fluorescence signature during aggregation.Nanomechanics and intermolecular forces of amyloid revealed by four-dimensional electron microscopy.Structural complexity of a composite amyloid fibril.The zipper groups of the amyloid state of proteins.Implications for Alzheimer's disease of an atomic resolution structure of amyloid-β(1-42) fibrils.Dynamics of locking of peptides onto growing amyloid fibrils.A medicinal chemist's guide to molecular interactionsMembrane protein folding: how important are hydrogen bonds?The amyloid state of proteins in human diseases.Forces stabilizing proteinsStructural Evidence of Amyloid Fibril Formation in the Putative Aggregation Domain of TDP-43.The activities of amyloids from a structural perspective.Prion-Like Characteristics of Polyglutamine-Containing Proteins.Rationalizing tight ligand binding through cooperative interaction networks.Insights into stability and toxicity of amyloid-like oligomers by replica exchange molecular dynamics analyses.Sequence-Dependent Self-Assembly and Structural Diversity of Islet Amyloid Polypeptide-Derived β-Sheet Fibrils.Counting peptide-water hydrogen bonds in unfolded proteins.Characterization of the nucleation barriers for protein aggregation and amyloid formation.Asparagine and glutamine ladders promote cross-species prion conversion.Insights into structure, stability, and toxicity of monomeric and aggregated polyglutamine models from molecular dynamics simulations.Modelling and analysis of early aggregation events of BMHP1-derived self-assembling peptides.Molecular level studies on binding modes of labeling molecules with polyalanine peptides.Electrostatics in the stability and misfolding of the prion protein: salt bridges, self energy, and solvation.Combined effects of solvation and aggregation propensity on the final supramolecular structures adopted by hydrophobic, glycine-rich, elastin-like polypeptides.Proteolysis of truncated hemolysin A yields a stable dimerization interface.Cooperative deformation of hydrogen bonds in beta-strands and beta-sheet nanocrystals.Scrutiny of chain-length and N-terminal effects in α-helix folding: a molecular dynamics study on polyalanine peptides.
P2860
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P2860
description
2007 nî lūn-bûn
@nan
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
2007年论文
@zh
2007年论文
@zh-cn
name
Cooperative hydrogen bonding in amyloid formation.
@en
type
label
Cooperative hydrogen bonding in amyloid formation.
@en
prefLabel
Cooperative hydrogen bonding in amyloid formation.
@en
P2093
P2860
P356
P1433
P1476
Cooperative hydrogen bonding in amyloid formation.
@en
P2093
David Eisenberg
Kiril Tsemekhman
Lukasz Goldschmidt
P2860
P304
P356
10.1110/PS.062609607
P50
P577
2007-02-27T00:00:00Z