Publication | Closed Access
Isotope-edited FTIR in H2O: determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls
14
Citations
17
References
2014
Year
Isotope-edited FtirSpecific ResiduesMolecular BiologyPeptide ScienceAnalytical UltracentrifugationTotal Reflection TechniqueProtein FoldingAnalytical ChemistryBiophysicsProtein ChemistryIsotope-edited Ftir SpectroscopyBiochemistryConformational StudySolution Nmr SpectroscopyMolecular ModelingStructural BiologyNatural SciencesPeptide LibraryMass SpectrometryModel α-Helix PeptidePeptide SynthesisMedicineModel Peptide
Isotope-edited FTIR spectroscopy has been shown to be able to determine peptide's structure in the residue level in D2O, which is not a physiological solvent. Here, attenuated total reflection technique was utilized to successfully apply isotope-edited FTIR spectroscopy in H2O to determine the conformation of specific residues in a model peptide.
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