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Results: 4
MUTATIONAL ANALYSIS OF DISULFIDE BONDS IN THE TRYPSIN-REACTIVE SUBDOMAIN OF A BOWMAN-BIRK-TYPE INHIBITOR OF TRYPSIN AND CHYMOTRYPSIN - COOPERATIVE VERSUS AUTONOMOUS REFOLDING OF SUBDOMAINS
Authors: PHILLIP S KIM YM DURR I WENZL G VOGT M FLECKER P
Citation: S. Phillip et al., MUTATIONAL ANALYSIS OF DISULFIDE BONDS IN THE TRYPSIN-REACTIVE SUBDOMAIN OF A BOWMAN-BIRK-TYPE INHIBITOR OF TRYPSIN AND CHYMOTRYPSIN - COOPERATIVE VERSUS AUTONOMOUS REFOLDING OF SUBDOMAINS, European journal of biochemistry, 251(3), 1998, pp. 854-862
PROTEOLYTIC CLEAVAGE OF SOYBEAN BOWMAN-BIRK INHIBITOR MONITORED BY MEANS OF HIGH-PERFORMANCE CAPILLARY ELECTROPHORESIS - IMPLICATIONS FOR THE MECHANISM OF PROTEINASE-INHIBITORS
Authors: JENSEN B UNGER KK UEBE J GEY M KIM YM FLECKER P
Citation: B. Jensen et al., PROTEOLYTIC CLEAVAGE OF SOYBEAN BOWMAN-BIRK INHIBITOR MONITORED BY MEANS OF HIGH-PERFORMANCE CAPILLARY ELECTROPHORESIS - IMPLICATIONS FOR THE MECHANISM OF PROTEINASE-INHIBITORS, Journal of biochemical and biophysical methods, 33(3), 1996, pp. 171-185
CRYSTAL-STRUCTURE OF THE BIFUNCTIONAL SOYBEAN BOWMAN-BIRK INHIBITOR AT 0.28-NM RESOLUTION - STRUCTURAL PECULIARITIES IN A FOLDED PROTEIN CONFORMATION
Authors: VOSS RH ERMLER U ESSEN LO WENZL G KIM YM FLECKER P
Citation: Rh. Voss et al., CRYSTAL-STRUCTURE OF THE BIFUNCTIONAL SOYBEAN BOWMAN-BIRK INHIBITOR AT 0.28-NM RESOLUTION - STRUCTURAL PECULIARITIES IN A FOLDED PROTEIN CONFORMATION, European journal of biochemistry, 242(1), 1996, pp. 122-131
TEMPLATE-DIRECTED PROTEIN-FOLDING INTO A METASTABLE STATE OF INCREASED ACTIVITY
Authors: FLECKER P
Citation: P. Flecker, TEMPLATE-DIRECTED PROTEIN-FOLDING INTO A METASTABLE STATE OF INCREASED ACTIVITY, European journal of biochemistry, 232(2), 1995, pp. 528-535
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