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Isotope-edited FTIR in H2O: determination of the conformation of specific residues in a model α-helix peptide by 13C labeled carbonyls
- Source :
- Chemical communications (Cambridge, England). 50(30)
- Publication Year :
- 2014
-
Abstract
- 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.
- Subjects :
- chemistry.chemical_classification
Residue (complex analysis)
Carbon Isotopes
Isotope
Stereochemistry
Protein Conformation
technology, industry, and agriculture
Metals and Alloys
Water
Peptide
General Chemistry
Catalysis
Surfaces, Coatings and Films
Electronic, Optical and Magnetic Materials
Solvent
stomatognathic system
chemistry
Attenuated total reflection
Spectroscopy, Fourier Transform Infrared
Materials Chemistry
Ceramics and Composites
Organic chemistry
Fourier transform infrared spectroscopy
Peptides
Subjects
Details
- ISSN :
- 1364548X
- Volume :
- 50
- Issue :
- 30
- Database :
- OpenAIRE
- Journal :
- Chemical communications (Cambridge, England)
- Accession number :
- edsair.doi.dedup.....f8a0473d0a7f82ca2ee66a18e08b764c