Evidence for a molten globule state as a general intermediate in protein folding

FEBS Letters

Ptitsyn, O.B.²  Zerovnik, E.¹  Pain, R.H.¹  Semisotnov, G.V.²  Razgulyaev, O.I.² 

[1] Department of Biochemistry and Genetics, University of Newcastle upon Tyne NE2 4HH, England;Institute of Protein Research, Academy of Sciences of the USSR, 142292 Pushchino, Moscow Region, USSR

关键词: Protein folding;    Folding intermediate;    Folding kinetics;    Framework model;    GdmCl;    guanidinium chloride;    MES;    2[N-Morpholino]jethanesolphonic acid;    near UV c.d.;    near ultraviolet circular dichroism;    DTT;    dithiothreitol;    CAB;    bovine carbonic anhydrase;    αLA;    α-lactalbumin;    BLG;    β-lactoglobulin;    PGK;    phosphoglycerate kinase;    βLase;    β lactamase;    IL-1β;    recombinant human interleukin 1β;    Ve;    elution volume;    N;    native state;    U;    fully unfolded state;    ANS;    8-anilino-1-naphthalene-sulfonate;    S;    secondary structure;    G;    intermediate globular state;   

DOI  :  10.1016/0014-5793(90)80143-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We propose that the formation of the transient molten globule state occurs early on the pathway of folding of all globular proteins.

【 授权许可】

Unknown