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Results: 1-7 |
Results: 7
GLUCOAMYLASE MUTANTS IN THE CONSERVED ACTIVE-SITE SEGMENT TRP170-TYR175 LOCATED AT A DISTANCE FROM THE SITE OF CATALYSIS
Authors: STOFFER BB DUPONT C FRANDSEN TP LEHMBECK J SVENSSON B
Citation: Bb. Stoffer et al., GLUCOAMYLASE MUTANTS IN THE CONSERVED ACTIVE-SITE SEGMENT TRP170-TYR175 LOCATED AT A DISTANCE FROM THE SITE OF CATALYSIS, Protein engineering, 10(1), 1997, pp. 81-87
SOME DETAILS OF THE REACTION-MECHANISM OF GLUCOAMYLASE FROM ASPERGILLUS-NIGER - KINETIC AND STRUCTURAL STUDIES ON TRP52-]PHE AND TRP317-]PHE MUTANTS
Authors: CHRISTENSEN T STOFFER BB SVENSSON B CHRISTENSEN U
Citation: T. Christensen et al., SOME DETAILS OF THE REACTION-MECHANISM OF GLUCOAMYLASE FROM ASPERGILLUS-NIGER - KINETIC AND STRUCTURAL STUDIES ON TRP52-]PHE AND TRP317-]PHE MUTANTS, European journal of biochemistry, 250(3), 1997, pp. 638-645
MOLECULAR MODELING OF HUMAN RED-BLOOD-CELL PYRUVATE-KINASE - STRUCTURAL IMPLICATIONS OF A NOVEL G(1091) TO A-MUTATION CAUSING SEVERE NONSPHEROCYTIC HEMOLYTIC-ANEMIA
Authors: VANSOLINGE WW KRAAIJENHAGEN RJ RIJKSEN G VANWIJK R STOFFER BB GAJHEDE M NIELSEN FC
Citation: Ww. Vansolinge et al., MOLECULAR MODELING OF HUMAN RED-BLOOD-CELL PYRUVATE-KINASE - STRUCTURAL IMPLICATIONS OF A NOVEL G(1091) TO A-MUTATION CAUSING SEVERE NONSPHEROCYTIC HEMOLYTIC-ANEMIA, Blood, 90(12), 1997, pp. 4987-4995
STRUCTURE AND ENERGETICS OF THE GLUCOAMYLASE-ISOMALTOSE TRANSITION-STATE COMPLEX PROBED BY USING MODELING AND DEOXYGENATED SUBSTRATES COUPLED WITH SITE-DIRECTED MUTAGENESIS
Authors: FRANDSEN TP STOFFER BB PALCIC MM HOF S SVENSSON B
Citation: Tp. Frandsen et al., STRUCTURE AND ENERGETICS OF THE GLUCOAMYLASE-ISOMALTOSE TRANSITION-STATE COMPLEX PROBED BY USING MODELING AND DEOXYGENATED SUBSTRATES COUPLED WITH SITE-DIRECTED MUTAGENESIS, Journal of Molecular Biology, 263(1), 1996, pp. 79-89
CHEMICAL MAPPING OF THE ACTIVE-SITE OF THE GLUCOAMYLASE OF ASPERGILLUS-NIGER
Authors: LEMIEUX RU SPOHR U BACH M CAMERON DR FRANDSEN TP STOFFER BB SVENSSON B PALCIC MM
Citation: Ru. Lemieux et al., CHEMICAL MAPPING OF THE ACTIVE-SITE OF THE GLUCOAMYLASE OF ASPERGILLUS-NIGER, Canadian journal of chemistry, 74(3), 1996, pp. 319-335
SUBSTRATE-BINDING MECHANISM OF GLU180-]GLN, ASP176-]ASN, AND WILD-TYPE GLUCOAMYLASES FROM ASPERGILLUS-NIGER
Authors: CHRISTENSEN U OLSEN K STOFFER BB SVENSSON B
Citation: U. Christensen et al., SUBSTRATE-BINDING MECHANISM OF GLU180-]GLN, ASP176-]ASN, AND WILD-TYPE GLUCOAMYLASES FROM ASPERGILLUS-NIGER, Biochemistry, 35(47), 1996, pp. 15009-15018
MUTATIONAL MODULATION OF SUBSTRATE BOND-TYPE SPECIFICITY AND THERMOSTABILITY OF GLUCOAMYLASE FROM ASPERGILLUS-AWAMORI BY REPLACEMENT WITH SHORT HOMOLOG ACTIVE-SITE SEQUENCES AND THIOL DISULFIDE ENGINEERING/
Authors: FIEROBE HP STOFFER BB FRANDSEN TP SVENSSON B
Citation: Hp. Fierobe et al., MUTATIONAL MODULATION OF SUBSTRATE BOND-TYPE SPECIFICITY AND THERMOSTABILITY OF GLUCOAMYLASE FROM ASPERGILLUS-AWAMORI BY REPLACEMENT WITH SHORT HOMOLOG ACTIVE-SITE SEQUENCES AND THIOL DISULFIDE ENGINEERING/, Biochemistry, 35(26), 1996, pp. 8696-8704
Risultati: 1-7 |