About: Bacteriorhodopsin in ice

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scientific article published on 01 December 1990

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rdf:type	Item
description	wetenschappelijk artikel (nl) bài báo khoa học (vi) наукова стаття, опублікована в грудні 1990 (uk) article scientifique publié en 1990 (fr) im Dezember 1990 veröffentlichter wissenschaftlicher Artikel (de) artículu científicu espublizáu n'avientu de 1990 (ast) scientific article published on 01 December 1990 (en)
publication date	wds:Q57637178-C1A586F7-9013-4685-82F5-FB7D9AAB4877
publication date	1990-12-01 00:00:00Z (xsd:dateTime)
language of work or name	wds:Q57637178-C503043B-BB55-4C86-941D-8990DC844F4D
language of work or name	English
cites work	wds:Q57637178-09CAE414-34BE-4D8F-8DD7-65C5301358FE wds:Q57637178-2012BADC-715B-4A6E-9CF4-73337E7A53F6 wds:Q57637178-279DE139-533D-4006-A588-AE94A6727828 wds:Q57637178-417B470A-547B-4114-AC1E-D724211181FA wds:Q57637178-4BD22045-E88F-4590-B3F8-4B1E9A0BEEED wds:Q57637178-7350BAC7-70B6-4B90-B9B3-2C6FBE9610C5 wds:Q57637178-8307A607-7F82-4E56-B495-032EF0FE80BF wds:Q57637178-98A012DC-F612-4D08-BC49-F375B16320AF wds:Q57637178-B6EBFAA0-B3C0-42F7-AB1F-D5F27302589C wds:Q57637178-D4013BA6-1E83-406B-B47E-B0E4EC0772F4 wds:Q57637178-E9BA53C1-4222-4CD9-9660-F052ADF6A765 wds:Q57637178-F732F1BD-74FC-4A95-96FE-A162F7724E0F wds:Q57637178-F7944807-DBB4-4003-A645-E1651FCD6D70 wds:Q57637178-FBE55D58-16C7-4E4D-9452-27260018F906
cites work	Protonation and deprotonation of the M, N, and O intermediates during the bacteriorhodopsin photocycle. Role of water in bacteriorhodopsin's chromophore: resonance Raman study Isolation of the cell membrane of Halobacterium halobium and its fractionation into red and purple membrane Dependency of delta pH-relaxation across vesicular membranes on the buffering power of bulk solutions and lipids Monomeric and aggregated bacteriorhodopsin: Single-turnover proton transport stoichiometry and photochemistry Aspartic acid-96 is the internal proton donor in the reprotonation of the Schiff base of bacteriorhodopsin The role of back-reactions and proton uptake during the N----O transition in bacteriorhodopsin's photocycle: a kinetic resonance Raman study Two pumps, one principle: light-driven ion transport in halobacteria Resolution of heterogeneous fluorescence into component decay-associated excitation spectra. Application to subtilisins Evidence for chromophore-chromophore interactions in the purple membrane from reconstitution experiments of the chromophore-free membrane Ionization of phospholipids and phospholipid-supported interfacial lateral diffusion of protons in membrane model systems Water molecules and exchangeable hydrogen ions at the active centre of bacteriorhodopsin localized by neutron diffraction. Elements of the proton pathway? [56] Determination of the net proton-hydroxide ion permeability across vesicular lipid bilayers and membrane proteins by optical probes Bacteriorhodopsin precursor is processed in two steps
author name string	wds:Q57637178-CEEC8F67-2B1A-43EA-B6E3-4D9B9FEF9BD2
author name string	Dencher NA
rdfs:label	Bacteriorhodopsin in ice (en) Bacteriorhodopsin in ice (nl)
skos:prefLabel	Bacteriorhodopsin in ice (en) Bacteriorhodopsin in ice (nl)
name	Bacteriorhodopsin in ice (en) Bacteriorhodopsin in ice (nl)
author	wds:Q57637178-65141224-7030-4E38-85E8-088AF228A111
author	Joachim Heberle
title	wds:Q57637178-6A87C46B-95E2-4317-AACE-E1CBF7C58B57
title	Bacteriorhodopsin in ice. Accelerated proton transfer from the purple membrane surface (en)
page(s)	wds:Q57637178-045ABEBD-E7A8-43A9-9725-3F407CD2A229
page(s)	277-280
instance of	wds:Q57637178-3168E328-8EA9-4FC1-B24A-3954178D6EBB
instance of	scholarly article
main subject	wds:Q57637178-263C48CE-365F-4695-A7A4-B49093FBF854 wds:Q57637178-7E77AF38-4B8F-4FFF-A693-F7703E62C799 wds:Q57637178-F169DDAB-68F3-4119-90CA-4160011413D0 wds:Q57637178-FFF0E2B7-90D0-4835-A576-0E78222E9C9F
main subject	cell biology biophysics molecular biology structural biology
PubMed ID	wds:Q57637178-606A6DAB-640C-4A34-9021-BAF39A343431
PubMed ID	http://rdf.ncbi.nlm.nih.gov/pubchem/reference/2269364
PubMed ID	2269364
published in	wds:Q57637178-6838389F-300D-459B-98F4-B0BFFA66C10B
published in	FEBS Letters
issue	wds:Q57637178-34B7F745-C0E9-44BC-A01E-5CECD69A001E
volume	wds:Q57637178-FC9E6CD5-8554-458C-8A31-6EEEFB22D5C8
issue	1-2
volume	277
DOI	wds:Q57637178-72B74D5E-BCB8-472F-9C96-10B6C1BD8E46
DOI	http://dx.doi.org/10.1016/0014-5793(90)80864-F
DOI	10.1016/0014-5793(90)80864-F
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q57637178
is cites work of	Proton transfer reactions across bacteriorhodopsin and along the membrane Proton migration along the membrane surface and retarded surface to bulk transfer Experimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst Atr/Ft-Ir Difference Spectroscopy of Biological Matter with Microsecond Time Resolution PROTON TRANSLOCATION and CONFORMATIONAL CHANGES DURING THE BACTERIORHODOPSIN PHOTOCYCLE: TIME-RESOLVED STUDIES WITH MEMBRANE-BOUND OPTICAL PROBES and X-RAY DIFFRACTION Quantitative evaluation of the dynamics of proton transfer from photoactivated bacteriorhodopsin to the bulk Relationship of proton release at the extracellular surface to deprotonation of the schiff base in the bacteriorhodopsin photocycle A unifying concept for ion translocation by retinal proteins Proton transfer and energy coupling in the bacteriorhodopsin photocycle Protonation dynamics of the extracellular and cytoplasmic surface of bacteriorhodopsin in the purple membrane Mutation of a surface residue, lysine-129, reverses the order of proton release and uptake in bacteriorhodopsin; guanidine hydrochloride restores it Asp85 is the only internal aspartic acid that gets protonated in the M intermediate and the purple&#x2010;to&#x2010;blue transition of bacteriorhodopsin A solid&#x2010;state13C CP&#x2010;MAS NMR investigation Decoupling of photo- and proton cycle in the Asp85-->Glu mutant of bacteriorhodopsin. Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycle Opening the Schiff base moiety of bacteriorhodopsin by mutation of the four extracellular Glu side chains Water and bacteriorhodopsin: structure, dynamics, and function Bacteriorhodopsin expressed in Schizosaccharomyces pombe pumps protons through the plasma membrane. Bacteriorhodopsin: the functional details of a molecular machine are being resolved pH-sensitive vibrational probe reveals a cytoplasmic protonated cluster in bacteriorhodopsin. Time-resolved Fourier transform infrared spectroscopy of the polarizable proton continua and the proton pump mechanism of bacteriorhodopsin Buffer effects on electric signals of light-excited bacteriorhodopsin Site specific labeling of Rhodobacter sphaeroides reaction centers with dye probes for surface pH measurements.
is cites work of	wds:Q33919262-61CFA847-7F3B-440A-8627-0796232C3C06

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