Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.
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The Crystal Complex of Phosphofructokinase-2 of Escherichia coli with Fructose-6-phosphateThe folding unit of phosphofructokinase-2 as defined by the biophysical properties of a monomeric mutantObservation of solvent penetration during cold denaturation of E. coli phosphofructokinase-2.Expanded monomeric intermediate upon cold and heat unfolding of phosphofructokinase-2 from Escherichia coli.Three-Dimensional Domain Swapping Changes the Folding Mechanism of the Forkhead Domain of FoxP1.Folding kinetic pathway of phosphofructokinase-2 from Escherichia coli: a homodimeric enzyme with a complex domain organization.
P2860
Reversible unfolding of dimeric phosphofructokinase-2 from Escherichia coli reveals a dominant role of inter-subunit contacts for stability.
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2009 nî lūn-bûn
@nan
2009 թուականի Մայիսին հրատարակուած գիտական յօդուած
@hyw
2009 թվականի մայիսին հրատարակված գիտական հոդված
@hy
2009年の論文
@ja
2009年論文
@yue
2009年論文
@zh-hant
2009年論文
@zh-hk
2009年論文
@zh-mo
2009年論文
@zh-tw
2009年论文
@wuu
name
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@ast
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@en
type
label
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@ast
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@en
prefLabel
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@ast
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@en
P2860
P1433
P1476
Reversible unfolding of dimeri ...... ubunit contacts for stability.
@en
P2093
Jorge Babul
Mauricio Baez
P2860
P304
P356
10.1016/J.FEBSLET.2009.05.034
P407
P577
2009-05-22T00:00:00Z