Theoretical study of the contribution of aromatic side chains to the circular dichroism of basic bovine pancreatic trypsin inhibitor
- 17 October 1989
- journal article
- research article
- Published by American Chemical Society (ACS) in Biochemistry
- Vol. 28 (21) , 8609-8613
- https://doi.org/10.1021/bi00447a051
Abstract
Note: In lieu of an abstract, this is the article's first page.This publication has 5 references indexed in Scilit:
- Conformations of intermediates in the folding of the pancreatic trypsin inhibitorJournal of Molecular Biology, 1987
- Structure of bovine pancreatic trypsin inhibitorJournal of Molecular Biology, 1984
- Ultraviolet difference spectroscopy of intermediates trapped in unfolding and refolding of bovine pancreatic trypsin inhibitorBiochemistry, 1980
- Picosecond dynamics of tyrosine side chains in proteinsBiochemistry, 1979
- Near-ultraviolet tyrosyl circular dichroism of pig insulin monomers, dimers, and hexamers. Dipole-dipole coupling calculations in the monopole approximationBiochemistry, 1976