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rdf:type |
|
|
lifeskim:mentions |
|
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pubmed:issue |
3
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pubmed:dateCreated |
1998-2-2
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pubmed:abstractText |
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.
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pubmed:language |
eng
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pubmed:journal |
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|
pubmed:citationSubset |
IM
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|
pubmed:chemical |
|
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pubmed:status |
MEDLINE
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|
pubmed:month |
Jun
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|
pubmed:issn |
0301-1208
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pubmed:author |
|
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pubmed:issnType |
Print
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pubmed:volume |
34
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pubmed:owner |
NLM
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|
pubmed:authorsComplete |
Y
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pubmed:pagination |
235-40
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
|
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pubmed:year |
1997
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pubmed:articleTitle |
Structural and conformational study of peptides containing glycine and alanine residues by 13C CPMAS NMR spectroscopy in solid state.
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pubmed:affiliation |
Department of NMR, All India Institute of Medical Sciences, New Delhi, India.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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