An entropy criterion to detect minimally frustrated intermediates in native proteins.
about
Multiresolution analysis uncovers hidden conservation of properties in structurally and functionally similar proteins.Is it possible to stabilize a thermophilic protein further using sequences and structures of mesophilic proteins: a theoretical case study concerning DgAS.Early Folding Events, Local Interactions, and Conservation of Protein Backbone Rigidity.Neural networks predict protein folding and structure: artificial intelligence faces biomolecular complexity.Dynamics of the minimally frustrated helices determine the hierarchical folding of small helical proteins.Role of evolutionary information in prediction of aromatic-backbone NH interactions in proteins.Entropic criteria for protein folding derived from recurrences: six residues patch as the basic protein word.A neural network based predictor of residue contacts in proteins.
P2860
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P2860
An entropy criterion to detect minimally frustrated intermediates in native proteins.
description
1998 nî lūn-bûn
@nan
1998年の論文
@ja
1998年学术文章
@wuu
1998年学术文章
@zh-cn
1998年学术文章
@zh-hans
1998年学术文章
@zh-my
1998年学术文章
@zh-sg
1998年學術文章
@yue
1998年學術文章
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1998年學術文章
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name
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@ast
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@en
type
label
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@ast
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@en
prefLabel
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@ast
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@en
P2093
P2860
P356
P1476
An entropy criterion to detect minimally frustrated intermediates in native proteins.
@en
P2093
Compiani M
Fariselli P
Martelli PL
P2860
P304
P356
10.1073/PNAS.95.16.9290
P407
P577
1998-08-01T00:00:00Z