FEBS Letters | |
1H NMR and CD evidence of the folding of the isolated ribonuclease 50–61 fragment | |
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
【 预 览 】
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