Structural and conformational study of peptides containing glycine and alanine residues by 13C CPMAS NMR spectroscopy in solid state.
Indian J Biochem Biophys
;
1997 Jun; 34(3): 235-40
Article
in English
| IMSEAR
| ID: sea-28045
ABSTRACT
The results of the structural and conformational studies carried out using 13C CPMAS NMR technique on several glycine and alanine containing peptides in the solid state are reported. The study demonstrates the effects of variations in 13C chemical shifts due to conformation and hydrogen bonding. The possibility of applying this technique to obtain insight into the conformational characteristics of peptides of unknown structures is discussed.
Full text:
Available
Index:
IMSEAR (South-East Asia)
Main subject:
Peptides
/
Protein Conformation
/
Carbon Isotopes
/
Magnetic Resonance Spectroscopy
/
Protein Structure, Secondary
/
Alanine
/
Glycine
Language:
English
Journal:
Indian J Biochem Biophys
Year:
1997
Type:
Article
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