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Biophysical Journal 35: 23-29 (1981)
© 1981 the Biophysical Society
ABSTRACT
Absorption and fluorescence changes were used to monitor the thermally induced folding-unfolding transition of beta-trypsin. These parameters reflect changes in the microenvironment of different subsets of the four tryptophanyl residues of this protein. The thermal transition was found to be sequential.
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