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Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle.
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Europe PubMed Central
PMC publication ID
3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
title
Role of Arg82 in the early steps of the bacteriorhodopsin proton-pumping cycle
(English)
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Europe PubMed Central
PMC publication ID
3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
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31 January 2020
author
Ana-Nicoleta Bondar
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4
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3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
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31 January 2020
Marcus Elstner
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5
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Marcus Elstner
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Europe PubMed Central
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3135100
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31 January 2020
Qiang Cui
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3
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Qiang Cui
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Europe PubMed Central
PMC publication ID
3135100
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31 January 2020
author name string
Maike Clemens
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1
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3135100
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31 January 2020
Prasad Phatak
series ordinal
2
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PMC publication ID
3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
language of work or name
English
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publication date
11 May 2011
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Europe PubMed Central
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3135100
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retrieved
31 January 2020
published in
Journal of Physical Chemistry B
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3135100
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31 January 2020
volume
115
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PMC publication ID
3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
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31 January 2020
issue
21
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Europe PubMed Central
PMC publication ID
3135100
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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
page(s)
7129-7135
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retrieved
31 January 2020
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Structural alterations for proton translocation in the M state of wild-type bacteriorhodopsin
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Two groups control light-induced Schiff base deprotonation and the proton affinity of Asp85 in the Arg82 his mutant of bacteriorhodopsin
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Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin
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The two pKa's of aspartate-85 and control of thermal isomerization and proton release in the arginine-82 to lysine mutant of bacteriorhodopsin.
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Vibrational spectroscopy of bacteriorhodopsin mutants: light-driven proton transport involves protonation changes of aspartic acid residues 85, 96, and 212
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Tuning of Retinal Twisting in Bacteriorhodopsin Controls the Directionality of the Early Photocycle Steps
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based on heuristic
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Protein conformational changes in the bacteriorhodopsin photocycle
1 reference
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Suppression of the back proton-transfer from Asp85 to the retinal Schiff base in bacteriorhodopsin: A theoretical analysis of structural elements
1 reference
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reference URL
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based on heuristic
inferred from PubMed ID database lookup
Identifiers
DOI
10.1021/JP201865K
1 reference
stated in
Europe PubMed Central
PMC publication ID
3135100
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
PMC publication ID
3135100
1 reference
stated in
Europe PubMed Central
PMC publication ID
3135100
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
PubMed publication ID
21561116
1 reference
stated in
Europe PubMed Central
PMC publication ID
3135100
reference URL
https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:21561116%20AND%20SRC:MED&resulttype=core&format=json
retrieved
31 January 2020
ResearchGate publication ID
51116090
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