Conformational stability and thermodynamic characterization of the lipoic acid bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase.
about
Folding of the protein domain hbSBDUse of urea and glycine betaine to quantify coupled folding and probe the burial of DNA phosphates in lac repressor-lac operator binding.Structure of the subunit binding domain and dynamics of the di-domain region from the core of human branched chain alpha-ketoacid dehydrogenase complex.
P2860
Conformational stability and thermodynamic characterization of the lipoic acid bearing domain of human mitochondrial branched chain alpha-ketoacid dehydrogenase.
description
2004 nî lūn-bûn
@nan
2004 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2004 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
name
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@ast
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@en
type
label
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@ast
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@en
prefLabel
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@ast
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@en
P2860
P356
P1433
P1476
Conformational stability and t ...... alpha-ketoacid dehydrogenase.
@en
P2093
Tai-Huang Huang
P2860
P304
P356
10.1110/PS.04783104
P50
P577
2004-09-01T00:00:00Z