Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.
about
Missense mutation Lys18Asn in dystrophin that triggers X-linked dilated cardiomyopathy decreases protein stability, increases protein unfolding, and perturbs protein structure, but does not affect protein function.The N-terminal actin-binding tandem calponin-homology (CH) domain of dystrophin is in a closed conformation in solution and when bound to F-actin.Flexibility in the N-terminal actin-binding domain: clues from in silico mutations and molecular dynamics.Investigation of effects of terpene skin penetration enhancers on stability and biological activity of lysozyme.
P2860
Thermodynamic stability, unfolding kinetics, and aggregation of the N-terminal actin-binding domains of utrophin and dystrophin.
description
2012 nî lūn-bûn
@nan
2012年の論文
@ja
2012年論文
@yue
2012年論文
@zh-hant
2012年論文
@zh-hk
2012年論文
@zh-mo
2012年論文
@zh-tw
2012年论文
@wuu
2012年论文
@zh
2012年论文
@zh-cn
name
Thermodynamic stability, unfol ...... ns of utrophin and dystrophin.
@en
type
label
Thermodynamic stability, unfol ...... ns of utrophin and dystrophin.
@en
prefLabel
Thermodynamic stability, unfol ...... ns of utrophin and dystrophin.
@en
P2093
P2860
P356
P1433
P1476
Thermodynamic stability, unfol ...... ins of utrophin and dystrophin
@en
P2093
Geoffrey S Armstrong
Justine F Molas
Narsimulu Kongari
Steve J Winder
Surinder M Singh
Swati Bandi
P2860
P304
P356
10.1002/PROT.24033
P407
P577
2012-02-17T00:00:00Z