Disulphide bond exchange inhibited by air – kinetic and thermodynamic products in a library of macrocyclic cysteine derivatives-Reference-Cited by-同舟云学术

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Disulphide bond exchange inhibited by air – kinetic and thermodynamic products in a library of macrocyclic cysteine derivatives

Published:2018 Issue:14 Volume:16 Page:2411-2420
ISSN:1477-0520
Container-title:Organic & Biomolecular Chemistry
language:en
Short-container-title:Org. Biomol. Chem.

Author:

Cholewiak Agnieszka¹²³⁴^ORCID,Dobrzycki Łukasz⁵⁶⁷⁴,Jurczak Janusz¹²³⁴^ORCID,Ulatowski Filip¹²³⁴^ORCID

Affiliation:

1. Institute of Organic Chemistry

2. Polish Academy of Sciences

3. 01-224 Warsaw

4. Poland

5. Faculty of Chemistry

6. University of Warsaw

7. 02-093 Warsaw

Abstract

Oxidation of dithiols provides strained monomeric macrocycles which transform upon disulphide bond exchange into stable dimers.

Funder

Narodowe Centrum Nauki

Fundacja na rzecz Nauki Polskiej

Publisher

Royal Society of Chemistry (RSC)

Subject

Organic Chemistry,Physical and Theoretical Chemistry,Biochemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2018/OB/C7OB03123H

Reference37 articles.

1. Disulfide bonds as switches for protein function

2. Folding of small disulfide-rich proteins: clarifying the puzzle

3. Diverse Pathways of Oxidative Folding of Disulfide Proteins: Underlying Causes and Folding Models

4. Reexamination of the Folding of BPTI: Predominance of Native Intermediates

5. Protein folding guides disulfide bond formation

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