PMID: 744684Nov 1, 1978

Circular dichroism spectra of isolated soybean and chickpea trypsin-chymotrypsin inhibitors

International Journal of Peptide and Protein Research
T A Bewley, Y Birk


Circular dichroism spectra of trypsin-chymotrypsin inhibitors from soybeans and chickpeas have been determined in acidic, neutral and highly alkaline solutions. Neither protein contains alpha-helix although a small amount of beta-structure cannot be excluded. Negative dichroism above 250 nm has been assigned largely to disulfide bonds in both molecules with neither showing evidence for tyrosine residues buried in hydrophobic regions. The spectra of these inhibitors between 230 and 250 nm have been compared with the spectra of a number of structurally related proteins suggesting that previous interpretations of this region may have been incomplete or incorrect.


Aug 1, 1977·Proceedings of the National Academy of Sciences of the United States of America·J T YangC H Li
Sep 1, 1976·The Biochemical Journal·P SmirnoffS W Applebaum
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Sep 1, 1976·Proceedings of the National Academy of Sciences of the United States of America·B W LowJ S Richardson
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Oct 31, 1973·Journal of the American Chemical Society·R Nagarajan, R W Woody
Aug 23, 1972·Journal of the American Chemical Society·J P Casey, R B Martin
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Sep 1, 1967·Archives of Biochemistry and Biophysics·L P Wagner, J P Riehm
Jan 1, 1952·Advances in Protein Chemistry·G H BEAVEN, E R HOLIDAY


Feb 1, 1985·International Journal of Peptide and Protein Research·Y Birk
Jul 1, 1981·International Journal of Peptide and Protein Research·M D JibsonT A Bewley
Mar 1, 1980·International Journal of Peptide and Protein Research·Y BirkT A Bewley

Related Concepts

Circular Dichroism, Vibrational
Pharmaceutical Plants
Protein Conformation
Trypsin Inhibitor, Bowman-Birk Soybean
Trypsin Inhibitors

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