相关实验视频

Updated: May 13, 2026

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability
10:31

Residue-Specific Exchange of Proline by Proline Analogs in Fluorescent Proteins: How "Molecular Surgery" of the Backbone Affects Folding and Stability

Published on: February 3, 2022

普罗利尔异构酶SlyD是一种高效的酶,但减缓了客户蛋白质的结构折叠

Gabriel Zoldák1, Anne-Juliane Geitner, Franz X Schmid

  • 1Laboratorium für Biochemie und Bayreuther Zentrum für Molekulare Biowissenschaften, Universität Bayreuth, D-95440 Bayreuth, Germany.

Journal of the American Chemical Society
|March 1, 2013
PubMed
概括

烯基异构酶SlyD通过催化 cis/trans 烯基异构化,显著加速蛋白质折叠. 这种酶确保了快速和均的重新折叠率,无论最初的普罗林异构体状态如何.

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Coupled Assays for Monitoring Protein Refolding in Saccharomyces cerevisiae13:52

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The native conformation of a protein is formed by interactions between the side chains of its constituent amino acids. When the amino acids cannot form these interactions, the protein cannot fold by itself and needs chaperones. Notably, chaperones do not relay any additional information required for the folding of polypeptides; the native conformation of a protein is determined solely by its amino acid sequence. Chaperones catalyze protein folding without being a part of the folded protein.
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