Cracking the folding code. Why do some proteins adopt partially folded conformations, whereas other don't?

FEBS Letters

Uversky, Vladimir N¹ 

[1] Institute for Biological Instrumentation, Russian Academy of Sciences, 142290 Pushchino, Moscow Region, Russia

关键词: Protein folding;    Partially folded intermediate;    All-or-none transition;    Net charge;    Hydrophobicity;   

DOI  :  10.1016/S0014-5793(02)02359-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Many, but not all, globular proteins have been shown to have compact intermediate state(s) under equilibrium conditions in vitro, giving rise to the question: why do some proteins adopt partially folded conformations, whereas other do not? Here we show that charge to hydrophobicity ratio of a polypeptide chain may represent a key determinant in this respect, as proteins known to form equilibrium partially folded intermediates are specifically localized within a unique region of charge–hydrophobicity space. Thus, the competence of a protein to form equilibrium intermediate(s) may be determined by the bulk content of hydrophobic and charged amino acid residues rather than by the positioning of amino acids within the sequence.

【 授权许可】

Unknown