Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.

Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.

Item
http://www.wikidata.org/entity/Q30165223
Theoretical and experimental demonstration of the importance of specific nonnative interactions in protein foldingA residue in helical conformation in the native state adopts a β-strand conformation in the folding transition state despite its high and canonical Φ-value.Mutational investigation of protein folding transition states by Phi-value analysis and beyond: lessons from SH3 domain folding.The effects of nonnative interactions on protein folding rates: theory and simulationCalculation of mutational free energy changes in transition states for protein folding.A Transferable Coarse Grain Non-bonded Interaction Model For Amino Acids.The folding mechanics of a knotted proteinDramatic acceleration of protein folding by stabilization of a nonnative backbone conformationbeta-Strand interactions at the domain interface critical for the stability of human lens gammaD-crystallinThe origin of nonmonotonic complex behavior and the effects of nonnative interactions on the diffusive properties of protein foldingFolding and association of a homotetrameric protein complex in an all-atom Go model.Contribution to the prediction of the fold code: application to immunoglobulin and flavodoxin cases.Native contact density and nonnative hydrophobic effects in the folding of bacterial immunity proteins.Energetic frustrations in protein folding at residue resolution: a homologous simulation study of Im9 proteins.Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: evidence from a hydrophobic minimalist model.Relevance of structural segregation and chain compaction for the thermodynamics of folding of a hydrophobic protein model.Sampling of states for estimating the folding funnel entropy and energy landscape of a model alpha-helical hairpin peptide.
P2860

Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.

Item
http://www.wikidata.org/entity/Q30165223
description
2002 nî lūn-bûn
@nan
2002 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2002 թվականի նոյեմբերին հրատարակված գիտական հոդված
@hy
2002年の論文
@ja
2002年論文
@yue
2002年論文
@zh-hant
2002年論文
@zh-hk
2002年論文
@zh-mo
2002年論文
@zh-tw
2002年论文
@wuu
name
Non-native interactions, effec ...... frustrated hydrophobic model.
@ast
Non-native interactions, effec ...... frustrated hydrophobic model.
@en
type
label
Non-native interactions, effec ...... frustrated hydrophobic model.
@ast
Non-native interactions, effec ...... frustrated hydrophobic model.
@en
prefLabel
Non-native interactions, effec ...... frustrated hydrophobic model.
@ast
Non-native interactions, effec ...... frustrated hydrophobic model.
@en
P1433
P1476
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921
P356
P1433
P1476
Non-native interactions, effec ...... frustrated hydrophobic model.
@en
P2093
P2860
P304
P31
P356
P407
P433
P478
P577
P5875
P698
P921