An infrared spectroscopic study on the secondary structure of the black-eyed pea trypsin and chymotrypsin inhibitor - amide I-III and V bands
An. acad. bras. ciênc
;
58(3): 339-43, 1986. tab
Article
in English
| LILACS
| ID: lil-94851
ABSTRACT
The infrared spectrum of native black-eyed pea trypsin and chymotrypsin inhibitor (BTCI) in solid film was measured from 550 to 1750 cm-1 and amide I-III, and V regions have been analyzed. By comparison between the observed bands with the modes calculated for several structures (available inthe literature), the occurrence in BTCI of unordered, antipatallel ß-sheet, and ß-turn structures is suggested
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Index:
LILACS (Americas)
Main subject:
Trypsin Inhibitors
/
Alpha 1-Antichymotrypsin
/
Fabaceae
Language:
English
Journal:
An. acad. bras. ciênc
Journal subject:
Science
Year:
1986
Type:
Article
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