Folding protein models with a simple hydrophobic energy function: the fundamental importance of monomer inside/outside segregation.
about
Non-native interactions, effective contact order, and protein folding: a mutational investigation with the energetically frustrated hydrophobic model.A sequence-compatible amount of native burial information is sufficient for determining the structure of small globular proteins.Elucidating protein secondary structures using alpha-carbon recurrence quantifications.Entropy reduction effect imposed by hydrogen bond formation on protein folding cooperativity: evidence from a hydrophobic minimalist model.Information and redundancy in the burial folding code of globular proteins within a wide range of shapes and sizes.
P2860
Folding protein models with a simple hydrophobic energy function: the fundamental importance of monomer inside/outside segregation.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年論文
@yue
1999年論文
@zh-hant
1999年論文
@zh-hk
1999年論文
@zh-mo
1999年論文
@zh-tw
1999年论文
@wuu
1999年论文
@zh
1999年论文
@zh-cn
name
Folding protein models with a ...... er inside/outside segregation.
@ast
Folding protein models with a ...... er inside/outside segregation.
@en
type
label
Folding protein models with a ...... er inside/outside segregation.
@ast
Folding protein models with a ...... er inside/outside segregation.
@en
prefLabel
Folding protein models with a ...... er inside/outside segregation.
@ast
Folding protein models with a ...... er inside/outside segregation.
@en
P2860
P356
P1476
Folding protein models with a ...... er inside/outside segregation.
@en
P2093
Pereira De Araújo AF
P2860
P304
12482-12487
P356
10.1073/PNAS.96.22.12482
P407
P577
1999-10-01T00:00:00Z