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PMID: 18266338 Published · ppublish English Comparative Study Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Mechanical properties of bovine rhodopsin and bacteriorhodopsin: possible roles in folding and function.

Langmuir : the ACS journal of surfaces and colloids ·Vol. 24 ·No. 4 ·2008-02-19 ·Pages 1330-7

Sapra KT, Park PS, Palczewski K, Muller DJ

Abstract

Molecular interactions and mechanical properties that contribute to the stability and function of proteins are complex and of fundamental importance. In this study, we used single-molecule dynamic force spectroscopy (DFS) to explore the interactions and the unfolding energy landscape of bovine rhodopsin and bacteriorhodopsin. An analysis of the experimental data enabled the extraction of parameters that provided insights into the kinetic stability and mechanical properties of these membrane proteins. Individual structural segments of rhodopsin and bacteriorhodopsin have different properties. A core of rigid structural segments was observed in rhodopsin but not in bacteriorhodopsin. This core may reflect differences in mechanisms of protein folding between the two membrane proteins. The different structural rigidity of the two proteins may also reflect their adaptation to differing functions.

MeSH Terms
Animals Bacteriorhodopsins/chemistry Cattle Kinetics Microscopy, Atomic Force/methods Protein Conformation Protein Folding Protein Structure, Tertiary Rhodopsin/chemistry Surface Properties
Chemicals
Bacteriorhodopsins Rhodopsin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Sapra K Tanuj
Biotechnology Center, University of Technology, Dresden, Germany. sapra@biotec.tu-dresden.de
Park Paul S-H
Palczewski Krzysztof
Muller Daniel J
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Article Info
Journal
Langmuir : the ACS journal of surfaces and colloids
Abbr.
Langmuir
ISSN
0743-7463
DOI
10.1021/la702299z
Email
sapra@biotec.tu-dresden.de
Published
2008-02-19
Pages
1330-7
Language
English
Region
United States
NLM ID
9882736
PMCID
PMC2504747
Subset
IM
Grants
NEI NIH HHS · EY 08061 · United States
NEI NIH HHS · K99 EY018085 · United States
NIGMS NIH HHS · R01 GM079191-02 · United States
NIGMS NIH HHS · R01 GM079191 · United States
NEI NIH HHS · K99 EY018085-01 · United States
NEI NIH HHS · R01 EY008061-22 · United States
NEI NIH HHS · K99 EY018085-02 · United States
NEI NIH HHS · R00 EY018085 · United States
NIGMS NIH HHS · GM 079191 · United States
NEI NIH HHS · R00 EY018085-04 · United States
NEI NIH HHS · EY 018085 · United States
NEI NIH HHS · R00 EY018085-05 · United States
NEI NIH HHS · R00 EY018085-03 · United States
NEI NIH HHS · R01 EY008061 · United States
External Links
PubMed source DOI: 10.1021/la702299z PMC Full Text View journal details
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