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An examination of the effect of B-domain deletion on the folding of thrombin and plasma kallikrein is reported. The fluorescence yield of the intrinsic tryptophan of thrombin and plasma kallikrein is increased by the solvent, acetonitrile, indicating exposure of the tryptophan in the native state. The increase in fluorescence yield is due to the formation of an unstable intermediate that is converted to the native state on dilution of the denaturant. The unfolding of thrombin and plasma kallikrein involves an intermediate and a final collapse to the native state. Deletion of the B-domain of thrombin eliminates the intermediate and results in a final collapse to the native state. Similar deletions in both the thrombin and plasma kallikrein B-domains, however, disrupt the intermediate and prevent formation of the native state. The intermediate formed from both proteins appears to be a short-lived species, as indicated by its rapid conversion to the native state. These data indicate that formation of the intermediate requires unfolding of the B-domain, in which case the increased exposure of tryptophan in the partially unfolded structure of the B-domain would be due to solvent.\pm$
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