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Results: 1-12 |
Results: 12
SPECTROSCOPIC, KINETIC, AND ELECTROCHEMICAL CHARACTERIZATION OF HETEROLOGOUSLY EXPRESSED WILD-TYPE AND MUTANT FORMS OF COPPER-CONTAINING NITRITE REDUCTASE FROM RHODOBACTER-SPHAEROIDES-2.4.3
Authors: OLESEN K VESELOV A ZHAO YW WANG YS DANNER B SCHOLES CP SHAPLEIGH JP
Citation: K. Olesen et al., SPECTROSCOPIC, KINETIC, AND ELECTROCHEMICAL CHARACTERIZATION OF HETEROLOGOUSLY EXPRESSED WILD-TYPE AND MUTANT FORMS OF COPPER-CONTAINING NITRITE REDUCTASE FROM RHODOBACTER-SPHAEROIDES-2.4.3, Biochemistry, 37(17), 1998, pp. 6086-6094
ELECTRONIC STRUCTURAL INFORMATION FROM Q-BAND ENDOR ON THE TYPE-1 ANDTYPE-2 COPPER LIGANDING ENVIRONMENT IN WILD-TYPE AND MUTANT FORMS OF COPPER-CONTAINING NITRITE REDUCTASE
Authors: VESELOV A OLESEN K SIENKIEWICZ A SHAPLEIGH JP SCHOLES CP
Citation: A. Veselov et al., ELECTRONIC STRUCTURAL INFORMATION FROM Q-BAND ENDOR ON THE TYPE-1 ANDTYPE-2 COPPER LIGANDING ENVIRONMENT IN WILD-TYPE AND MUTANT FORMS OF COPPER-CONTAINING NITRITE REDUCTASE, Biochemistry, 37(17), 1998, pp. 6095-6105
THE CENTRAL LYSINE IN THE P-LOOP MOTIF OF THE ESCHERICHIA-COLI DNAA PROTEIN IS ESSENTIAL FOR INITIATING DNA-REPLICATION FROM THE CHROMOSOMAL ORIGIN, ORIC, AND THE F-FACTOR ORIGIN, ORIS, BUT IS DISPENSABLE FOR INITIATION FROM THE P1 PLASMID ORIGIN, ORIR
Authors: SKOVGAARD O OLESEN K WRIGHT A
Citation: O. Skovgaard et al., THE CENTRAL LYSINE IN THE P-LOOP MOTIF OF THE ESCHERICHIA-COLI DNAA PROTEIN IS ESSENTIAL FOR INITIATING DNA-REPLICATION FROM THE CHROMOSOMAL ORIGIN, ORIC, AND THE F-FACTOR ORIGIN, ORIS, BUT IS DISPENSABLE FOR INITIATION FROM THE P1 PLASMID ORIGIN, ORIR, Plasmid (Print), 40(2), 1998, pp. 91-99
PEPTIDE-SUBSTRATES DISSOLVED IN DIMETHYLFORMAMIDE MAY BE MODIFIED AT THE EPSILON-AMINO GROUP OF LYSYL RESIDUES, CAUSING ERRONEOUS KINETIC CHARACTERIZATION OF PROTEOLYTIC-ENZYMES
Authors: OLESEN K BREDDAM K
Citation: K. Olesen et K. Breddam, PEPTIDE-SUBSTRATES DISSOLVED IN DIMETHYLFORMAMIDE MAY BE MODIFIED AT THE EPSILON-AMINO GROUP OF LYSYL RESIDUES, CAUSING ERRONEOUS KINETIC CHARACTERIZATION OF PROTEOLYTIC-ENZYMES, Analytical biochemistry (Print), 262(1), 1998, pp. 88-89
SUBSTRATES WITH CHARGED P-1 RESIDUES ARE EFFICIENTLY HYDROLYZED BY SERINE CARBOXYPEPTIDASES WHEN S-3-P-1 INTERACTIONS ARE FACILITATED
Authors: OLESEN K BREDDAM K
Citation: K. Olesen et K. Breddam, SUBSTRATES WITH CHARGED P-1 RESIDUES ARE EFFICIENTLY HYDROLYZED BY SERINE CARBOXYPEPTIDASES WHEN S-3-P-1 INTERACTIONS ARE FACILITATED, Biochemistry, 36(40), 1997, pp. 12235-12241
THE INVOLVEMENT OF THE 2 ACIDIC PATCHES OF SPINACH PLASTOCYANIN IN THE REACTION WITH PHOTOSYSTEM-I
Authors: YOUNG S SIGFRIDSSON K OLESEN K HANSSON O
Citation: S. Young et al., THE INVOLVEMENT OF THE 2 ACIDIC PATCHES OF SPINACH PLASTOCYANIN IN THE REACTION WITH PHOTOSYSTEM-I, Biochimica et biophysica acta. Bioenergetics, 1322(2-3), 1997, pp. 106-114
C-TERMINAL INCORPORATION OF FLUOROGENIC AND AFFINITY LABELS USING WILD-TYPE AND MUTAGENIZED CARBOXYPEPTIDASE-Y
Authors: STENNICKE HR OLESEN K SORENSEN SB BREDDAM K
Citation: Hr. Stennicke et al., C-TERMINAL INCORPORATION OF FLUOROGENIC AND AFFINITY LABELS USING WILD-TYPE AND MUTAGENIZED CARBOXYPEPTIDASE-Y, Analytical biochemistry, 248(1), 1997, pp. 141-148
INCREASE OF THE P-1 LYS LEU SUBSTRATE PREFERENCE OF CARBOXYPEPTIDASE-Y BY RATIONAL DESIGN BASED ON KNOWN PRIMARY AND TERTIARY STRUCTURES OFSERINE CARBOXYPEPTIDASES/
Authors: OLESEN K BREDDAM K
Citation: K. Olesen et K. Breddam, INCREASE OF THE P-1 LYS LEU SUBSTRATE PREFERENCE OF CARBOXYPEPTIDASE-Y BY RATIONAL DESIGN BASED ON KNOWN PRIMARY AND TERTIARY STRUCTURES OFSERINE CARBOXYPEPTIDASES/, Biochemistry, 34(48), 1995, pp. 15689-15699
IMPROVEMENT OF THE APPLICABILITY OF CARBOXYPEPTIDASE-Y IN PEPTIDE-SYNTHESIS BY PROTEIN ENGINEERING
Authors: RAASCHOUNIELSEN M MORTENSEN UH OLESEN K BREDDAM K
Citation: M. Raaschounielsen et al., IMPROVEMENT OF THE APPLICABILITY OF CARBOXYPEPTIDASE-Y IN PEPTIDE-SYNTHESIS BY PROTEIN ENGINEERING, Peptide research, 7(3), 1994, pp. 132-135
CARBOXYPEPTIDASE Y MUTANTS WITH ALTERED SUBSTRATE SPECIFICITIES
Authors: OLESEN K BREDDAM K
Citation: K. Olesen et K. Breddam, CARBOXYPEPTIDASE Y MUTANTS WITH ALTERED SUBSTRATE SPECIFICITIES, Journal of cellular biochemistry, 1994, pp. 138-138
THE ACTIVITY OF CARBOXYPEPTIDASE-Y TOWARD SUBSTRATES WITH BASIC P-1 AMINO-ACID-RESIDUES IS DRASTICALLY INCREASED BY MUTATIONAL REPLACEMENT OF LEUCINE-178
Authors: OLESEN K MORTENSEN UH AASMULOLSEN S KIELLANDBRANDT MC REMINGTON SJ BREDDAM K
Citation: K. Olesen et al., THE ACTIVITY OF CARBOXYPEPTIDASE-Y TOWARD SUBSTRATES WITH BASIC P-1 AMINO-ACID-RESIDUES IS DRASTICALLY INCREASED BY MUTATIONAL REPLACEMENT OF LEUCINE-178, Biochemistry, 33(37), 1994, pp. 11121-11126
ALTERING SUBSTRATE PREFERENCE OF CARBOXYPEPTIDASE-Y BY A NOVEL STRATEGY OF MUTAGENESIS ELIMINATING WILD-TYPE BACKGROUND
Authors: OLESEN K KIELLANDBRANDT MC
Citation: K. Olesen et Mc. Kiellandbrandt, ALTERING SUBSTRATE PREFERENCE OF CARBOXYPEPTIDASE-Y BY A NOVEL STRATEGY OF MUTAGENESIS ELIMINATING WILD-TYPE BACKGROUND, Protein engineering, 6(4), 1993, pp. 409-415
Risultati: 1-12 |