1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragment

FEBS Letters

Herranz, J.¹  Santoro, J.¹  Rico, M.¹  Nieto, J.L.¹  Jiménez, M.A.¹ 

[1] Instituto de Estructura de la Materia, CSIC, Serrano 119, 28006 Madrid, Spain

关键词: Peptide folding;    1H-NMR;    Protein fragment;    Helical structure;    RNase A;    CM-RNase;    S-carboxymethylated bovine pancreatic ribonuclease A (EC 3.1.27.5);    SAP;    Staphylococcus aureus protease (EC 3.4.21.19);    TFE;    trifluoroethanol;    σ-;    standard deviation;    COSY;    two-dimensional homonuclear correlated spectroscopy;    CD;    circular dichroism;    HPLC;    high-performance liquid chromatography;   

DOI  :  10.1016/0014-5793(87)80948-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

In our search for potential folding intermediates we have prepared and characterized the fragment of RNase A corresponding to residues 50–61. Proton chemical shift variations with temperature, addition of stabilizing (TFE) or denaturing agents (urea) provide a strong experimental basis for concluding that in aqueous solution this RNase fragment forms an α-helix structure similar to that in the intact RNase A crystal. This conclusion lends strong support to the idea that elements of secondary structure (mainly α-helices) can be formed in the absence of tertiary interactions and act as nucleation centers in the protein folding process.

【 授权许可】

Unknown