Proton translocation by bacteriorhodopsin in the absence of substantial conformational changes.
about
Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsinDeprotonation of D96 in Bacteriorhodopsin Opens the Proton Uptake PathwayActivation of G protein-coupled receptors: beyond two-state models and tertiary conformational changes.High-field EPR spectroscopy applied to biological systems: characterization of molecular switches for electron and ion transfer.Gas-Assisted Annular Microsprayer for Sample Preparation for Time-Resolved Cryo-Electron MicroscopyVoltage dependence of proton pumping by bacteriorhodopsin mutants with altered lifetime of the M intermediate.Proton transfer dynamics on the surface of the late M state of bacteriorhodopsin.How environment supports a state: molecular dynamics simulations of two states in bacteriorhodopsin suggest lipid and water compensation.Proteomic analysis of acidic chaperones, and stress proteins in extreme halophile Halobacterium NRC-1: a comparative proteomic approach to study heat shock response.A three-dimensional movie of structural changes in bacteriorhodopsin.Studies of the bacteriorhodopsin photocycle without the use of light: clues to proton transfer coupled reactions.A Schiff base connectivity switch in sensory rhodopsin signaling.Microbial and animal rhodopsins: structures, functions, and molecular mechanisms.Stable closure of the cytoplasmic half-channel is required for efficient proton transport at physiological membrane potentials in the bacteriorhodopsin catalytic cycle.Decoupled side chain and backbone dynamics for proton translocation - M2 of influenza A.Monitoring light-induced structural changes of Channelrhodopsin-2 by UV-visible and Fourier transform infrared spectroscopy.
P2860
Q27642312-1745E7F8-FDF8-4A51-88EA-BF5D68B46902Q27676244-4588B210-698E-4FBD-9B6F-C12EFE9F137DQ30364526-7D3063B9-A145-4F49-ADB8-295177A2C484Q30381116-11EE2203-FF69-4DBA-AE53-5F9E1A8CAABDQ30399921-8E2D6D6C-4537-4060-9424-90C739DE0074Q31137506-14256EF0-A980-4059-B989-E12BF3E2B287Q32141328-CE8A65A2-A01B-46F1-9D0E-6BDCD0E96434Q34186188-0F53E921-5952-4630-ADE0-8FC8F1B1F312Q34665825-41DA84BC-7278-493F-AE3E-E88712A402BDQ36232010-FE68E7A1-FB99-427E-A697-B743B8C0A09FQ36857919-9515E6D8-BAC6-4053-AA7A-F393EA39DABAQ36945117-526FF16C-41F8-4D36-B559-362F75778FCBQ37691765-2CF57C26-8278-4EC8-97CE-0D0EA117FF64Q37731529-4D81CB84-B084-471B-8689-DB16E59EBD51Q38711091-E821685F-D643-4D6D-8249-82D866753C8EQ40456359-885BB99D-4462-4109-8FE6-A2DCE993D371
P2860
Proton translocation by bacteriorhodopsin in the absence of substantial conformational changes.
description
2002 nî lūn-bûn
@nan
2002年の論文
@ja
2002年学术文章
@wuu
2002年学术文章
@zh
2002年学术文章
@zh-cn
2002年学术文章
@zh-hans
2002年学术文章
@zh-my
2002年学术文章
@zh-sg
2002年學術文章
@yue
2002年學術文章
@zh-hant
name
Proton translocation by bacter ...... antial conformational changes.
@en
Proton translocation by bacter ...... antial conformational changes.
@nl
type
label
Proton translocation by bacter ...... antial conformational changes.
@en
Proton translocation by bacter ...... antial conformational changes.
@nl
prefLabel
Proton translocation by bacter ...... antial conformational changes.
@en
Proton translocation by bacter ...... antial conformational changes.
@nl
P2093
P1476
Proton translocation by bacter ...... tantial conformational changes
@en
P2093
P304
P356
10.1016/S0022-2836(02)00307-8
P407
P577
2002-05-01T00:00:00Z