About: Isotope-edited IR spectroscopy for the study of membrane proteins

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An Entity of Type : schema:ScholarlyArticle, within Data Space : wasabi.inria.fr associated with source document(s)

Attributes	Values
type	Academic Article research paper schema:ScholarlyArticle
isDefinedBy	Covid-on-the-Web dataset
has title	Isotope-edited IR spectroscopy for the study of membrane proteins
Creator	Gazit, Ehud Tendler, Saul
Source	Elsevier; Medline; PMC
abstract	Fourier transform infrared (FTIR) spectroscopy has long been a powerful tool for structural analysis of membrane proteins. However, because of difficulties in resolving contributions from individual residues, most of the derived measurements tend to yield average properties for the system under study. Isotope editing, through its ability to resolve individual vibrations, establishes FTIR as a method that is capable of yielding accurate structural data on individual sites in a protein.
has issue date	2006-08-28(xsd:dateTime)
bibo:doi	10.1016/j.cbpa.2006.08.013
bibo:pmid	16935550
has license	no-cc
sha1sum (hex)	e674e86133ccee8afbc58add6d88115f03729966
schema:url	https://doi.org/10.1016/j.cbpa.2006.08.013
resource representing a document's title	Isotope-edited IR spectroscopy for the study of membrane proteins
has PubMed Central identifier	PMC7185810
has PubMed identifier	16935550
schema:publication	Curr Opin Chem Biol
resource representing a document's body	covid:e674e86133ccee8afbc58add6d88115f03729966#body_text
is schema:about of	named entity 'REVIEW' named entity 'EDITED' named entity 'COMES' named entity 'ANALYTICAL TECHNIQUES' named entity 'ISSUE' named entity 'kinetics' named entity 'orientational' named entity 'high-resolution' named entity 'nanogram' named entity 'T-cell receptor' named entity 'deconvolve' named entity 'selenomethionine' named entity 'vibrational mode' named entity 'spectroscopic' named entity 'L-tyrosine' named entity 'spectra' named entity 'isotope' named entity 'isotope' named entity 'isotope' named entity 'secondary structure' named entity 'quinol' named entity 'arginine' named entity 'fumarate reductase' named entity 'membrane protein' named entity 'secondary structure' named entity 'LacY' named entity 'protein' named entity 'spectral features' named entity 'biological macromolecules' named entity 'glycophorin' named entity 'spectroscopy' named entity 'secondary structure' named entity 'Excitonic' named entity 'FTIR' named entity 'membrane proteins' named entity 'arginine' named entity 'hydrogen bonding' named entity 'transition dipole moment' named entity 'isotope' named entity 'peptides' named entity 'peptide' named entity 'solvation' named entity 'spectra' named entity 'peptide backbone' named entity 'FTIR' named entity 'membrane proteins' named entity 'selenomethionine' named entity 'mechanism of action' named entity 'moiety' named entity 'spectroscopy' named entity 'amino terminal' named entity 'protein' named entity 'infrared light' named entity 'natural abundance' named entity 'FTIR' named entity 'FTIR' named entity 'amino acids' named entity 'principal axis' named entity 'dichroism' named entity 'solvent' named entity 'lipid bilayer' named entity 'Schematic' named entity 'spectroscopy' named entity 'amide' named entity 'orientational' named entity 'dichroism' named entity 'hydrophobic' named entity 'amide' named entity 'Isotope' named entity 'helical bundle' named entity 'protein' named entity 'protein' named entity 'isotopic labeling' named entity 'site-directed mutagenesis' named entity 'high-resolution' named entity 'linear dichroism' named entity 'dimeric' named entity 'arginine' named entity 'protonation' named entity 'FTIR'

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