UZH-Logo

Maintenance Infos

Salt bridges and conformational flexibility: effect on protein stability


Karshikoff, A; Jelesarov, I (2008). Salt bridges and conformational flexibility: effect on protein stability. Biotechnology and Biotechnological Equipment, 22(1):606-611.

Abstract

Salt bridges are believed to have an important role in stabilisation of native protein structure. The assessment of their contribution to the electrostatic term of the free energy is a yet unsolved task. One can point out a number of reasons: beginning with conceptual issues, such as the complex nature of the interplay between the different types of non-covalent interactions and going to details, such as the interactions of the participating groups with their environments. Here we focus on the interplay between electrostatic interactions the functional groups forming salt bridges are involved in and the conformational flexibility of the protein molecule. We show that the connection between these two factors appears to be one of the keys for a better understanding of the forces determining stability of proteins.

Salt bridges are believed to have an important role in stabilisation of native protein structure. The assessment of their contribution to the electrostatic term of the free energy is a yet unsolved task. One can point out a number of reasons: beginning with conceptual issues, such as the complex nature of the interplay between the different types of non-covalent interactions and going to details, such as the interactions of the participating groups with their environments. Here we focus on the interplay between electrostatic interactions the functional groups forming salt bridges are involved in and the conformational flexibility of the protein molecule. We show that the connection between these two factors appears to be one of the keys for a better understanding of the forces determining stability of proteins.

Citations

3 citations in Web of Science®
3 citations in Scopus®
Google Scholar™

Altmetrics

Downloads

1 download since deposited on 22 Sep 2008
0 downloads since 12 months
Detailed statistics

Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
Language:English
Date:February 2008
Deposited On:22 Sep 2008 08:38
Last Modified:05 Apr 2016 12:28
Publisher:Diagnosis Press
ISSN:1310-2818
Publisher DOI:10.1080/13102818.2008.10817520
Official URL:http://www.diagnosisp.com/dp/journals/view_abstract_ref.php?journal_id=1&archive=0&issue_id=17&article_id=471&PHPSESSID=58730fd4acdc37ccccbb8db4353f2544
Related URLs:http://www.diagnosisp.com/dp/journals/issue.php?journal_id=1&archive=0&issue_id=17&PHPSESSID=58730fd4acdc37ccccbb8db4353f2544 (Publisher)
Permanent URL: http://doi.org/10.5167/uzh-3734

Download

[img]
Content: Accepted Version
Filetype: PDF - Registered users only
Size: 1MB
View at publisher

TrendTerms

TrendTerms displays relevant terms of the abstract of this publication and related documents on a map. The terms and their relations were extracted from ZORA using word statistics. Their timelines are taken from ZORA as well. The bubble size of a term is proportional to the number of documents where the term occurs. Red, orange, yellow and green colors are used for terms that occur in the current document; red indicates high interlinkedness of a term with other terms, orange, yellow and green decreasing interlinkedness. Blue is used for terms that have a relation with the terms in this document, but occur in other documents.
You can navigate and zoom the map. Mouse-hovering a term displays its timeline, clicking it yields the associated documents.

Author Collaborations