A second look at mini-protein stability: analysis of FSD-1 using circular dichroism, differential scanning calorimetry, and simulations.
about
Protein design with a comprehensive statistical energy function and boosted by experimental selection for foldabilityOn the origins of the weak folding cooperativity of a designed ββα ultrafast protein FSD-1.Finding multiple reaction pathways via global optimization of action.Stability and folding behavior analysis of zinc-finger using simple models.
P2860
A second look at mini-protein stability: analysis of FSD-1 using circular dichroism, differential scanning calorimetry, and simulations.
description
2009 nî lūn-bûn
@nan
2009年の論文
@ja
2009年学术文章
@wuu
2009年学术文章
@zh-cn
2009年学术文章
@zh-hans
2009年学术文章
@zh-my
2009年学术文章
@zh-sg
2009年學術文章
@yue
2009年學術文章
@zh
2009年學術文章
@zh-hant
name
A second look at mini-protein ...... calorimetry, and simulations.
@en
A second look at mini-protein ...... calorimetry, and simulations.
@nl
type
label
A second look at mini-protein ...... calorimetry, and simulations.
@en
A second look at mini-protein ...... calorimetry, and simulations.
@nl
prefLabel
A second look at mini-protein ...... calorimetry, and simulations.
@en
A second look at mini-protein ...... calorimetry, and simulations.
@nl
P2860
P1433
P1476
A second look at mini-protein ...... g calorimetry, and simulations
@en
P2093
Jianwen A Feng
P2860
P304
P356
10.1016/J.BPJ.2009.08.046
P407
P577
2009-11-01T00:00:00Z