Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics


Autoria(s): Wang XH; Ren JS; Qu XG
Data(s)

2008

Resumo

Human cyclin A(2) participates in cell cycle regulation, DNA replication, and transcription. Its overexpression has been implicated in the development and progression of a variety of human cancers. However, cyclin A(2) or its truncated form is very unstable in the absence of binding partner, which makes it difficult to get a deep insight of structural basis of the interactions. Therefore, biophysical studies of the full-length human cyclin A, would provide important information regarding protein stability and folding/unfolding process.

Identificador

http://ir.ciac.jl.cn/handle/322003/10839

http://www.irgrid.ac.cn/handle/1471x/147662

Idioma(s)

英语

Fonte

Wang XH;Ren JS;Qu XG.Biophysical studies on the full-length human cyclin A(2): Protein stability and folding/unfolding thermodynamics,JOURNAL OF PHYSICAL CHEMISTRY B,2008,112(28):8346-8353

Palavras-Chave #FLUORESCENCE ENERGY-TRANSFER #LUMRY-EYRING MODELS #CELL-CYCLE #LINEAR EXTRAPOLATION #CANCER #DNA #COMPLEX #CDK2 #DENATURATION #EQUILIBRIUM
Tipo

期刊论文