Membrane Environment Reduces the Accessible Conformational Space Available to an Integral Membrane Protein-Reference-Cited by-同舟云学术

Membrane Environment Reduces the Accessible Conformational Space Available to an Integral Membrane Protein

Published:2002-12-07 Issue:1 Volume:107 Page:338-343
ISSN:1520-6106
Container-title:The Journal of Physical Chemistry B
language:en
Short-container-title:J. Phys. Chem. B

Author:

Gerken Uwe¹,Jelezko Fedor¹,Götze Britta¹,Branschädel Marcus¹,Tietz Carsten¹,Ghosh Robin¹,Wrachtrup Jörg¹

Affiliation:

1. Institute of Physics, University of Stuttgart, Pfaffenwaldring 57, D-70550 Stuttgart, Germany, Institute of Biology, Department of Bioenergetics, University of Stuttgart, Pfaffenwaldring 57, D-70550 Stuttgart, Germany

Publisher

American Chemical Society (ACS)

Subject

Materials Chemistry,Surfaces, Coatings and Films,Physical and Theoretical Chemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/jp025903o

Reference47 articles.

1. Crystal structure of an integral membrane light-harvesting complex from photosynthetic bacteria

2. The crystal structure of the light-harvesting complex II (B800–850) from Rhodospirillum molischianum

3. Atomic model of plant light-harvesting complex by electron crystallography

4. X-ray structure of a ClC chloride channel at 3.0 Å reveals the molecular basis of anion selectivity

5. Crystal Structure of Rhodopsin: A G Protein-Coupled Receptor

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