Folding kinetics of mammalian ribonucleases

FEBS Letters

Lang, Kurt²  Schmid, Franz X.²  Wrba, Alex²  Krebs, Herbert²  Beintema, Jaap J.¹ 

[1] Biochemisch Laboratorium, Rijksuniversiteit Groningen, Nijenborgh 16, NL-9747 AG Groningen, The Netherlands;Institut für Biophysik und Physikalische Biochemie, Universität Regensburg, D-8400 Regensburg, FRG

关键词: Protein folding;    RNase;    Stopped-flow kinetics;    Protein stability;    Proline isomerization;    RNase;    pancreatic ribonuclease (EC 3.1.27.5);    N;    native protein;    UF;    Us;    fast- and slow-refolding species of unfolded RNases;    respectively;    GdmCl;    guanidinium chloride;    τ;    time constant of a chemical reaction or phase;    α;    relative amplitude of a kinetic phase;   

DOI  :  10.1016/0014-5793(86)81401-6

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The folding kinetics of seven different pancreatic ribonucleases are compared both under native conditions and within the unfolding transition. In general, the folding kinetics of these proteins are similar despite numerous amino acid substitutions. Ribonucleases with 4–6 proline residues show 80% slow-folding species. For three ribonucleases with 7 prolines this number increases to 90%. Porcine ribonuclease with a unique Pro 114-Pro 115 sequence folds significantly slower than other ribonucleases which do not show this sequence.

【 授权许可】

Unknown