Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions.
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Improvement of the treatment of loop structures in the UNRES force field by inclusion of coupling between backbone- and side-chain-local conformational states.Long range Trp-Trp interaction initiates the folding pathway of a pro-angiogenic β-hairpin peptidebeta-hairpin-forming peptides; models of early stages of protein folding.Infrared study of the stability and folding kinetics of a series of β-hairpin peptides with a common NPDG turn.Thermodynamics of protein folding using a modified Wako-Saitô-Muñoz-Eaton modelUltrafast folding and molecular dynamics of a linear hydrophobic β-hairpin.
P2860
Mechanism of formation of the C-terminal beta-hairpin of the B3 domain of the immunoglobulin binding protein G from Streptococcus. III. Dynamics of long-range hydrophobic interactions.
description
2010 nî lūn-bûn
@nan
2010年の論文
@ja
2010年論文
@yue
2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
@wuu
2010年论文
@zh
2010年论文
@zh-cn
name
Mechanism of formation of the ...... ange hydrophobic interactions.
@en
Mechanism of formation of the ...... ange hydrophobic interactions.
@nl
type
label
Mechanism of formation of the ...... ange hydrophobic interactions.
@en
Mechanism of formation of the ...... ange hydrophobic interactions.
@nl
prefLabel
Mechanism of formation of the ...... ange hydrophobic interactions.
@en
Mechanism of formation of the ...... ange hydrophobic interactions.
@nl
P2860
P50
P356
P1433
P1476
Mechanism of formation of the ...... ange hydrophobic interactions.
@en
P2093
Agnieszka Lewandowska
P2860
P304
P356
10.1002/PROT.22605
P407
P577
2010-02-01T00:00:00Z