Predicting the protein folding nucleus from a sequence

FEBS Letters

Poupon, Anne¹  Mornon, Jean-Paul¹ 

[1] Systèmes Moléculaires et Biologie Structurale, LMCP, CNRS UMR C7590, Universités P6 et P7, T16, Case 115, 4, place Jussieu, 75232 Paris Cedex 05, France

关键词: Protein folding;    Folding intermediate;    Hydrophobic packing;    Sequence similarity;   

DOI  :  10.1016/S0014-5793(99)00622-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Understanding the mechanism of protein folding would allow prediction of the three-dimensional structure from sequence data alone. It has been shown that small proteins fold in a small number of kinetic steps and that significantly populated intermediate states exist for some of them. Studies of these intermediates have demonstrated the existence of specific interactions established during the initial stages of folding. Comparison of the amino acids participating in these specific and essential interactions and constituting the folding nucleus with conserved hydrophobic positions of a given fold shows a striking correspondence. This finding opens the perspective of predicting the folding nucleus knowing only a set of divergent sequences of a protein family.

【 授权许可】

Unknown