Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.
about
Inferring repeat-protein energetics from evolutionary information.High-Resolution Mapping of a Repeat Protein Folding Free Energy Landscape.The case for defined protein folding pathways.Detailing Protein Landscapes under Pressure.Differences in the mechanical unfolding pathways of apo- and copper-bound azurins.The consequences of cavity creation on the folding landscape of a repeat protein depend upon context
P2860
Highly polarized C-terminal transition state of the leucine-rich repeat domain of PP32 is governed by local stability.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
Highly polarized C-terminal tr ...... s governed by local stability.
@ast
Highly polarized C-terminal tr ...... s governed by local stability.
@en
type
label
Highly polarized C-terminal tr ...... s governed by local stability.
@ast
Highly polarized C-terminal tr ...... s governed by local stability.
@en
prefLabel
Highly polarized C-terminal tr ...... s governed by local stability.
@ast
Highly polarized C-terminal tr ...... s governed by local stability.
@en
P2860
P356
P1476
Highly polarized C-terminal tr ...... s governed by local stability.
@en
P2093
Ananya Majumdar
Thuy Phuong Dao
P2860
P304
P356
10.1073/PNAS.1412165112
P407
P50
P577
2015-04-20T00:00:00Z