Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A.
about
Atomistic Glimpse of the Orderly Chaos of One Protein.Protein Allostery and Conformational Dynamics.Unidirectional allostery in the regulatory subunit RIα facilitates efficient deactivation of protein kinase A.Dimension conversion and scaling of disordered protein chains.Enhanced Sampling of Intrinsic Structural Heterogeneity of the BH3-Only Protein Binding Interface of Bcl-xL.Communication: Self-assembly of a model supramolecular polymer studied by replica exchange with solute tempering.Conversion of an amide to a high-energy thioester by Staphylococcus aureus sortase A is powered by variable binding affinity for calcium
P2860
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P2860
Disorder-to-Order Transition of an Active-Site Loop Mediates the Allosteric Activation of Sortase A.
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
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@ast
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@en
type
label
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@ast
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@en
prefLabel
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@ast
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@en
P2860
P1433
P1476
Disorder-to-Order Transition o ...... teric Activation of Sortase A.
@en
P2093
Xiaodong Pang
P2860
P304
P356
10.1016/J.BPJ.2015.08.039
P407
P577
2015-10-01T00:00:00Z