Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases-Reference-Cited by-同舟云学术

Order-disorder transitions of cytoplasmic N-termini in the mechanisms of P-type ATPases

Published:2021 Issue: Volume:232 Page:172-187
ISSN:1359-6640
Container-title:Faraday Discussions
language:en
Short-container-title:Faraday Discuss.

Author:

Hossain Khondker R.¹^ORCID,Clayton Daniel¹,Goodchild Sophia C.²^ORCID,Rodger Alison²^ORCID,Payne Richard J.¹^ORCID,Cornelius Flemming³^ORCID,Clarke Ronald J.¹⁴^ORCID

Affiliation:

1. School of Chemistry, University of Sydney, Sydney, NSW 2006, Australia

2. Department of Molecular Sciences, Macquarie University, Sydney, NSW 2109, Australia

3. Department of Biomedicine, University of Aarhus, DK-8000 Aarhus C, Denmark

4. The University of Sydney Nano Institute, Sydney, NSW 2006, Australia

Abstract

Circular dichroism of an H+, K+-ATPase N-terminal peptide at varying trifluoroethanol concentrations is investigated, indicating that its secondary structure is environmentally sensitive.

Funder

Australian Research Council

Sundhed og Sygdom, Det Frie Forskningsråd

Novo Nordisk Fonden

Publisher

Royal Society of Chemistry (RSC)

Subject

Physical and Theoretical Chemistry

Link

http://pubs.rsc.org/en/content/articlepdf/2021/FD/D0FD00040J

Reference45 articles.

1. P-type ATPases at a glance

2. General and specific interactions of the phospholipid bilayer with P-type ATPases

3. Biochemical Aspects of Active Transport

4. Activation by Adenosine Triphosphate in the Phosphorylation Kinetics of Sodium and Potassium Ion Transport Adenosine Triphosphatase

5. The influence of some cations on an adenosine triphosphatase from peripheral nerves

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