Constraints on the Flexibility of Bacteriorhodopsin's Carboxyl-Terminal Tail at the Purple Membrane Surface-Reference-Cited by-同舟云学术

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Constraints on the Flexibility of Bacteriorhodopsin's Carboxyl-Terminal Tail at the Purple Membrane Surface

Published:1983-01-04 Issue:1 Volume:22 Page:5-12
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Renthal Robert.

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi00270a601

Reference30 articles.

1. LINKING REGIONS BETWEEN HELICES IN BACTERIORHODOPSIN REVEALED

2. Mapping the active site of papain with the aid of peptide substrates and inhibitors

3. [56] Carbodiimide modification of proteins

4. Empirical Predictions of Protein Conformation

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1. Fluorescence spectroscopy of rhodopsins: Insights and approaches;Biochimica et Biophysica Acta (BBA) - Bioenergetics;2014-05

2. pH Optimization of Amidation via Carbodiimides;Industrial & Engineering Chemistry Research;2013-09-11

3. The Bacteriorhodopsin Carboxyl-Terminus Contributes to Proton Recruitment and Protein Stability;Biochemistry;2009-01-13

4. Site-Directed Solid-State NMR on Membrane Proteins;Annual Reports on NMR Spectroscopy;2006

5. Backbone dynamics of bacteriorhodopsin as studied by 13 C solid-state NMR spectroscopy;European Biophysics Journal;2003-10-01

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