Secondary structure of bacteriorhodopsin fragments. External sequence constraints specify the conformation of transmembrane helices (Q77458427)

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5 December 2019

title

Secondary structure of bacteriorhodopsin fragments. External sequence constraints specify the conformation of transmembrane helices (English)

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5 December 2019

author name string

J Lüneberg

1

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5 December 2019

M Widmann

2

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5 December 2019

M Dathe

3

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5 December 2019

T Marti

4

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5 December 2019

language of work or name

English

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publication date

1 October 1998

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Journal of Biological Chemistry

5 December 2019

number of pages

9

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based on heuristic

inferred from page(s)

published in

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5 December 2019

volume

273

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5 December 2019

issue

44

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page(s)

28822-28830

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A simple method for displaying the hydropathic character of a protein

5 December 2019

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Bacteriorhodopsin and Related Pigments of Halobacteria

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Electron-crystallographic refinement of the structure of bacteriorhodopsin

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X-ray structure of bacteriorhodopsin at 2.5 angstroms from microcrystals grown in lipidic cubic phases

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Surface of bacteriorhodopsin revealed by high-resolution electron crystallography

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Proton transfer pathways in bacteriorhodopsin at 2.3 angstrom resolution

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Two light-transducing membrane proteins: bacteriorhodopsin and the mammalian rhodopsin

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Refolding of bacteriorhodopsin in lipid bilayers. A thermodynamically controlled two-stage process

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Refolding of bacteriorhodopsin. Protease V8 fragmentation and chromophore reconstitution from proteolytic V8 fragments

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Thermodynamic measurements of the contributions of helix-connecting loops and of retinal to the stability of bacteriorhodopsin

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Identifiers

DOI

10.1074/JBC.273.44.28822

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9786882%20AND%20SRC:MED&resulttype=core&format=json

5 December 2019

1 reference