Fourier transform infrared techniques for probing membrane protein structure.
about
Human p8 is a HMG-I/Y-like protein with DNA binding activity enhanced by phosphorylationProtein stability and interaction of the nicotinic acetylcholine receptor with cholinergic ligands studied by Fourier-transform infrared spectroscopyMaximum entropy deconvolution of infrared spectra: use of a novel entropy expression without sign restriction.Role of aspartate-96 in proton translocation by bacteriorhodopsin.Vibrational spectra of individual millimeter-size membrane patches using miniature infrared waveguides.Incorporation of the nicotinic acetylcholine receptor into planar multilamellar films: characterization by fluorescence and Fourier transform infrared difference spectroscopyMolecular reaction mechanisms of proteins monitored by time-resolved FTIR-spectroscopy.Characterization of surfaces presenting covalently immobilized oligopeptides using near-edge X-ray absorption fine structure spectroscopyComparison of the secondary structures of human class I and class II major histocompatibility complex antigens by Fourier transform infrared and circular dichroism spectroscopyFourier transform infrared spectroscopy and site-directed isotope labeling as a probe of local secondary structure in the transmembrane domain of phospholamban.The infrared dichroism of transmembrane helical polypeptides.Probing conformational changes in the nicotinic acetylcholine receptor by Fourier transform infrared difference spectroscopy.Alpha-helical hydrophobic polypeptides form proton-selective channels in lipid bilayers.Fourier transform infrared evidence for a predominantly alpha-helical structure of the membrane bound channel forming COOH-terminal peptide of colicin E1.Photoactivation of rhodopsin causes an increased hydrogen-deuterium exchange of buried peptide groups.The protein environment surrounding tyrosyl radicals D. and Z. in photosystem II: a difference Fourier-transform infrared spectroscopic study.A Difference Fourier transform infrared study of tyrosyl radical Z* decay in photosystem IIFourier transform infrared evidence for proline structural changes during the bacteriorhodopsin photocycle.Ultraviolet resonance Raman spectroscopy of bacteriorhodopsin.Conformation of the synaptobrevin transmembrane domainConformational heterogeneity within the Michaelis complex of lactate dehydrogenaseStructure and dynamics of polypeptides and proteins in lipid membranes.The molecular mechanism of membrane proteins probed by evanescent infrared waves.Mutational studies of protein structures and their stabilities.Proteins in action monitored by time-resolved FTIR spectroscopy.A difference Fourier-transform infrared study of two redox-active tyrosine residues in photosystem II.An approximate model and empirical energy function for solute interactions with a water-phosphatidylcholine interface.Synthesis and FTIR conformational studies of peptides from the basic region of c-Jun: a critical analysis on the basis of CD and NMR data.Participation of bacteriorhodopsin active-site lysine backbone in vibrations associated with retinal photochemistry.Vibrational spectra of rhodopsin and bacteriorhodopsin.Biophysical Characterization of α-Synuclein and Rotenone Interaction.vpu transmembrane peptide structure obtained by site-specific fourier transform infrared dichroism and global molecular dynamics searching.Site-specific dichroism analysis utilizing transmission FTIR.Spectrochemical analysis of sycamore (Acer pseudoplatanus) leaves for environmental health monitoring.Tyrosine structural changes detected during the photoactivation of rhodopsin.Magic angle spinning NMR spectroscopy of membrane proteins.Hydrogen bonding changes of internal water molecules in rhodopsin during metarhodopsin I and metarhodopsin II formation.Proton uptake mechanism of bacteriorhodopsin as determined by time-resolved stroboscopic-FTIR-spectroscopy.Isotope-edited FTIR of alkaline phosphatase resolves paradoxical ligand binding properties and suggests a role for ground-state destabilization.The inactivating factor of glutamine synthetase, IF7, is a "natively unfolded" protein.
P2860
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P2860
Fourier transform infrared techniques for probing membrane protein structure.
description
1988 nî lūn-bûn
@nan
1988 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
1988 թվականի հունվարին հրատարակված գիտական հոդված
@hy
1988年の論文
@ja
1988年論文
@yue
1988年論文
@zh-hant
1988年論文
@zh-hk
1988年論文
@zh-mo
1988年論文
@zh-tw
1988年论文
@wuu
name
Fourier transform infrared techniques for probing membrane protein structure.
@ast
Fourier transform infrared techniques for probing membrane protein structure.
@en
type
label
Fourier transform infrared techniques for probing membrane protein structure.
@ast
Fourier transform infrared techniques for probing membrane protein structure.
@en
prefLabel
Fourier transform infrared techniques for probing membrane protein structure.
@ast
Fourier transform infrared techniques for probing membrane protein structure.
@en
P1476
Fourier transform infrared techniques for probing membrane protein structure.
@en
P2093
Braiman MS
Rothschild KJ
P304
P356
10.1146/ANNUREV.BB.17.060188.002545
P577
1988-01-01T00:00:00Z