Carbon-13 Magnetic Resonance Evaluation of Polypeptide Secondary Structure and Correlation with Proton Magnetic Resonance Studies
AUTOR(ES)
Urry, D. W.
RESUMO
With the use of appropriately chosen solvent pairs it is demonstrated that solvent dependence of peptide carbonyl carbon resonances can be correlated with polypeptide secondary structure. Solvent titrations show the peptide carbonyl which is intramolecularly hydrogen bonded to exhibit less chemical shift on going from a dimethylsulfoxide solution to a solution containing a solvent which is a good proton (or deuteron) donor. Effective solvent systems are dimethylsulfoxide paired with water, trifluoroethanol, or methanol. This approach is demonstrated with the pentapeptide of elastin.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=388665Documentos Relacionados
- Carbon-13 Relaxation and Proton Nuclear Magnetic Resonance Studies of Prostaglandin F2α
- In vivo carbon-13 nuclear magnetic resonance studies of heart metabolism.
- Metabolism of Methanol in Plant Cells. Carbon-13 Nuclear Magnetic Resonance Studies
- Discrimination Between Sporothrix schenckii and Ceratocystis stenoceras Rhamnomannans by Proton and Carbon-13 Magnetic Resonance Spectroscopy
- Carbon-13 Nuclear Magnetic Resonance: Naturally Occurring Nucleosides*
