Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle.
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Spectroscopic Studies on Organic Matter from Triassic Reptile Bones, Upper Silesia, PolandSimultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.Polarized Fourier transform infrared spectroscopy of bacteriorhodopsin. Transmembrane alpha helices are resistant to hydrogen/deuterium exchangeBacterioopsin, haloopsin, and sensory opsin I of the halobacterial isolate Halobacterium sp. strain SG1: three new members of a growing family.Infrared spectroscopic demonstration of a conformational change in bacteriorhodopsin involved in proton pumping.Photoreactions and structural changes of anabaena sensory rhodopsin.Further evidence that cyclosporin A protects mitochondria from calcium overload by inhibiting a matrix peptidyl-prolyl cis-trans isomerase. Implications for the immunosuppressive and toxic effects of cyclosporin.Magic angle spinning NMR spectroscopy of membrane proteins.The structures of bacteriorhodopsin with different retinal-Schiff base orientations--computer modeling and energy minimization studies.Effects of mutagenetic substitution of prolines on the rate of deprotonation and reprotonation of the Schiff base during the photocycle of bacteriorhodopsin.FTIR Analysis of a Light-driven Inward Proton-pumping Rhodopsin at 77 K.Self-recovering caddisfly silk: energy dissipating, Ca(2+)-dependent, double dynamic network fibers.
P2860
Q28602635-D378C8DF-12B9-4BF7-926A-5F4A53289633Q33926063-14128DE9-BF3C-427F-8D9A-C5FC7944AD76Q34126834-2DD2CDF5-B410-4279-9DE3-51BA35CD695EQ36099745-85E1A573-78EE-49B7-8E89-9AB764882A78Q37372605-7380E0FB-21D0-446A-AD79-C06F8B0294D1Q40692426-96086E13-C7D6-400B-A6A2-7AD6DAA356A4Q41138584-64EFE8DA-9B11-493E-ABB2-6F503EA826B8Q41395666-9F885BBE-5FD6-40A4-9AE9-B09166C50ED4Q41635351-A3D980F6-0F92-4FB9-B3C1-FE9D5526478AQ46442033-27FD4796-0BAF-44F0-9DC0-A555EAF20FEEQ50211566-4E83276E-B6DB-4153-8A04-27E6CAA869BAQ52786024-4E31ACA6-8DC1-4EAC-A300-E6FD5F2BC7F4
P2860
Fourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle.
description
1989 nî lūn-bûn
@nan
1989 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1989 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1989年の論文
@ja
1989年論文
@yue
1989年論文
@zh-hant
1989年論文
@zh-hk
1989年論文
@zh-mo
1989年論文
@zh-tw
1989年论文
@wuu
name
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@ast
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@en
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@nl
type
label
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@ast
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@en
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@nl
prefLabel
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@ast
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@en
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@nl
P2093
P2860
P356
P1476
Fourier transform infrared evi ...... bacteriorhodopsin photocycle.
@en
P2093
J Herzfeld
K J Rothschild
S L Pelletier
P2860
P304
P356
10.1073/PNAS.86.24.9832
P407
P577
1989-12-01T00:00:00Z