Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.
about
Catalytic mechanism of a mammalian Rab{middle dot}RabGAP complex in atomic detailConformational changes in gastric H+/K+-ATPase monitored by difference Fourier-transform infrared spectroscopy and hydrogen/deuterium exchangeStructural changes in bacteriorhodopsin during the photocycle measured by time-resolved polarized Fourier transform infrared spectroscopyA large photolysis-induced pKa increase of the chromophore counterion in bacteriorhodopsin: implications for ion transport mechanisms of retinal proteins.Protein dynamics in the bacteriorhodopsin photocycle: submillisecond Fourier transform infrared spectra of the L, M, and N photointermediates.Structural changes in the L photointermediate of bacteriorhodopsin.The back photoreaction of the M intermediate in the photocycle of bacteriorhodopsin: mechanism and evidence for two M species.Alternative translocation of protons and halide ions by bacteriorhodopsin.Surface-bound optical probes monitor protein translocation and surface potential changes during the bacteriorhodopsin photocycleMolecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.Proton binding within a membrane protein by a protonated water clusterA delocalized proton-binding site within a membrane proteinpH-induced structural changes in bacteriorhodopsin studied by Fourier transform infrared spectroscopyLight-induced reorientation in the purple membrane.Thermal equilibration between the M and N intermediates in the photocycle of bacteriorhodopsinStudy of the photocycle and charge motions of the bacteriorhodopsin mutant D96N.Arginine-82 regulates the pKa of the group responsible for the light-driven proton release in bacteriorhodopsin.Electrostatic coupling between retinal isomerization and the ionization state of Glu-204: a general mechanism for proton release in bacteriorhodopsinCorrelation between absorption maxima and thermal isomerization rates in bacteriorhodopsin.A residue substitution near the beta-ionone ring of the retinal affects the M substates of bacteriorhodopsinDeriving the intermediate spectra and photocycle kinetics from time-resolved difference spectra of bacteriorhodopsin. The simpler case of the recombinant D96N proteinIn channelrhodopsin-2 Glu-90 is crucial for ion selectivity and is deprotonated during the photocycle.Voltage dependence of proton pumping by bacteriorhodopsin is regulated by the voltage-sensitive ratio of M1 to M2Contribution of proton release to the B2 photocurrent of bacteriorhodopsinConnectivity of the retinal Schiff base to Asp85 and Asp96 during the bacteriorhodopsin photocycle: the local-access modelExperimental evidence for hydrogen-bonded network proton transfer in bacteriorhodopsin shown by Fourier-transform infrared spectroscopy using azide as catalyst.The photoreceptor sensory rhodopsin I as a two-photon-driven proton pump.Proton transfer via a transient linear water-molecule chain in a membrane protein.Proton storage site in bacteriorhodopsin: new insights from quantum mechanics/molecular mechanics simulations of microscopic pK(a) and infrared spectraThe molecular mechanism of membrane proteins probed by evanescent infrared waves.Light-driven proton or chloride pumping by halorhodopsin.Structure changes upon deprotonation of the proton release group in the bacteriorhodopsin photocycle.Lifetimes of intermediates in the beta -sheet to alpha -helix transition of beta -lactoglobulin by using a diffusional IR mixer.Tuning the Photocycle Kinetics of Bacteriorhodopsin in Lipid Nanodiscs.In situ determination of transient pKa changes of internal amino acids of bacteriorhodopsin by using time-resolved attenuated total reflection Fourier-transform infrared spectroscopyWater as a cofactor in the unidirectional light-driven proton transfer steps in bacteriorhodopsin.Structural and energetic determinants of primary proton transfer in bacteriorhodopsin.Monitoring the GAP catalyzed H-Ras GTPase reaction at atomic resolution in real time.The GAP arginine finger movement into the catalytic site of Ras increases the activation entropyA local electrostatic change is the cause of the large-scale protein conformation shift in bacteriorhodopsin.
P2860
Q27675470-54854716-1502-42E3-9801-5A806F430C1EQ28257467-5A7E6C96-2A21-438D-A6B3-E120EF5A18F2Q28365218-490F1A33-3105-4CEA-9273-B7F4AFD6137AQ30447600-AF2CF797-9B80-4BFA-8A9C-4EA84A034C75Q30449911-C51776EB-427A-41F3-9734-39093465E34DQ30479275-98DEC5C9-E2C0-4477-B031-95FB205FF1A7Q31007242-65554762-2D19-49F0-9068-96DCB25FF858Q33233584-8794A0C8-7AD9-470E-8FD5-C7866EFA6C5EQ33612274-BE4B39B0-C5C1-4662-B98B-A76DFBA08FB9Q33737300-822E840B-44AC-47CB-A24F-4E169EBB1D41Q33928561-4FE4E4A1-3BDE-4985-9529-41E94A9A69C5Q33990967-7EFA36CF-F625-4D14-8EBF-A46F59A3B4FEQ34018770-2EDFAEA6-D90B-4A1A-978E-AB7A42109E57Q34019618-B38D6B51-8390-438A-A046-4C468114388AQ34019739-33D7DF89-09F2-4F1E-967C-6786C4C7AE38Q34020206-B3AA4A68-EB5B-4C22-8A71-9E0C9FC0ADA3Q34040394-4BE567BA-53C5-42C5-89B5-FD0542E1E391Q34040476-AE0D59A0-D8EC-4470-B4A2-05FA50D116E6Q34087697-1C9B71E5-A01F-4410-B0C9-9B26609C926FQ34088543-ACDB360C-59D2-44DF-A3A3-784888690163Q34092032-748DE223-614A-4C3C-84C3-A2F91B3A3939Q34118883-E80B221D-9B92-4FF0-9449-86A3F715EC2CQ34167136-C4235156-2FDB-4F31-BC5A-969CD60BB90EQ34168433-4862A985-1954-4CB6-96E6-91C677FB9FA3Q34168939-A30DB13E-D20B-4447-A2EF-E8E0C2D58F8DQ34278113-3C373224-C44C-4902-B237-4E8079DF1616Q34383717-A78172B2-5723-41DA-8B9F-AF7E03022810Q35105201-F0CA90C9-D71F-46D8-9E15-EB63983698BAQ35228068-B018E218-603D-4B15-BBB5-E227C57E6F8EQ35797626-65161773-F532-4723-955C-132C30D3731AQ36065154-1B420EDE-664A-4073-8B6C-9F396991B8ACQ36150767-1EE6DC17-889B-4143-A3A2-15D62B90AA84Q36230626-0CE4956C-6091-4EB2-969F-53B79B1EA975Q36275345-326A54CF-0994-4803-8EFB-1A34EA8D95B9Q36354305-0C919447-B695-430D-B5D3-801966868550Q36458345-CA5E052B-3172-46E4-95B1-1EBA3A82D789Q36500209-31FB21ED-C985-4EC1-8B09-58AAFC73129BQ36521874-5A8C8A8D-FA1F-417F-944C-CA833783FDC8Q36609155-7BED6E68-E3BA-45EF-98AE-A1BB854B080DQ36764695-E23AAAF1-E35D-47BA-A2B9-8F23A61D38EA
P2860
Simultaneous monitoring of light-induced changes in protein side-group protonation, chromophore isomerization, and backbone motion of bacteriorhodopsin by time-resolved Fourier-transform infrared spectroscopy.
description
1990 nî lūn-bûn
@nan
1990 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
1990 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
1990年の論文
@ja
1990年学术文章
@wuu
1990年学术文章
@zh-cn
1990年学术文章
@zh-hans
1990年学术文章
@zh-my
1990年学术文章
@zh-sg
1990年學術文章
@yue
name
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@ast
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@en
type
label
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@ast
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@en
prefLabel
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@ast
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@en
P2093
P2860
P356
P1476
Simultaneous monitoring of lig ...... ansform infrared spectroscopy.
@en
P2093
P2860
P304
P356
10.1073/PNAS.87.24.9774
P407
P577
1990-12-01T00:00:00Z