Replacing a single atom accelerates the folding of a protein and increases its thermostability-Reference-Cited by-同舟云学术

Replacing a single atom accelerates the folding of a protein and increases its thermostability

Published:2016 Issue:28 Volume:14 Page:6780-6785
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Arnold Ulrich¹²³⁴,Raines Ronald T.⁵⁶⁷⁸⁹

Affiliation:

1. Institute of Biochemistry and Biotechnology

2. Martin-Luther-Universität Halle–Wittenberg

3. 06120 Halle

4. Germany

5. Department of Biochemistry

6. University of Wisconsin–Madison

7. Madison

8. USA

9. Department of Chemistry

Abstract

The conformational attributes of proline can have a substantial effect on the folding of polypeptide chains into a native structure and on the stability of that structure.

Funder

National Cancer Institute

National Institute of General Medical Sciences

National Institute of Arthritis and Musculoskeletal and Skin Diseases

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2016/OB/C6OB00980H

Reference60 articles.

1. Computational Enzyme Design

2. Nature Versus Nurture: Developing Enzymes That Function Under Extreme Conditions

3. Engineering the third wave of biocatalysis

4. Stabilizing biocatalysts

5. Total chemical synthesis of proteins

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