Studies on the active site of papain. VI. Chemical modification of tryptophan residues by N-bromosuccinimide.

Studies on the active site of papain. VII. Photooxidation of tryptophan residues.

Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.

Studies on the active site of papain. V. Photooxidation of histidine residues.

Identification of active site residues of Fenugreek β-amylase: chemical modification and in silico approach.

Identification of the active-site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin.

Potentiometric determination of ionizations at the active site of papain.

Chemical modification studies of the active centre of Candida albicans chitinase and its inhibition by allosamidin.

Denaturation studies of active-site labeled papain using electron paramagnetic resonance and fluorescence spectroscopy.

Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase.

Evaluation of the role of electrostatic residues in human epidermal growth factor by site-directed mutagenesis and chemical modification.

Chemical modification of the tryptophan residue in adrenocorticotropin.

Chemical modification of serine at the active site of penicillin acylase from Kluyvera citrophila.

Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification.

Chemical modification locates guanidinyl and carboxylate groups within the active site of prolidase.

Site-specific chemical modification of peptide and protein by thiazolidinediones.

Selective photochemical modification by trichloroethanol of tryptophan residues in proteins with a high tyrosine-to-tryptophan ratio.

Chemical modification of histidine residues of rabbit hemopexin.

Cysteine residues in the active site of Corynebacterium sarcosine oxidase.

Functional residues at the active site of aminopeptidase N.

Spectroscopic studies on the active site of Sepioteuthis lessoniana hemocyanin.

Chemical modification of arginine residues in alpha-bungarotoxin.

The chemical modification of papain with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide.

Modulation of the affinity of aspartic proteases by the mutated residues in active site models.

On the role of histidine residues in cyclodextrin glycosyltransferase: chemical modification with diethyl pyrocarbonate.

Suggest Documents

Studies on the active site of papain. VII. Photooxidation of tryptophan residues.

Chemical modification of xylanases: evidence for essential tryptophan and cysteine residues at the active site.

Studies on the active site of papain. V. Photooxidation of histidine residues.

Identification of active site residues of Fenugreek β-amylase: chemical modification and in silico approach.

Identification of the active-site serine in human pancreatic lipase by chemical modification with tetrahydrolipstatin.

Potentiometric determination of ionizations at the active site of papain.

Chemical modification studies of the active centre of Candida albicans chitinase and its inhibition by allosamidin.

Denaturation studies of active-site labeled papain using electron paramagnetic resonance and fluorescence spectroscopy.

Chemical modification of arginine at the active site of the bovine erythrocyte superoxide dismutase.

Evaluation of the role of electrostatic residues in human epidermal growth factor by site-directed mutagenesis and chemical modification.

Chemical modification of the tryptophan residue in adrenocorticotropin.

Chemical modification of serine at the active site of penicillin acylase from Kluyvera citrophila.

Role of cysteine residues in ribonuclease H from Escherichia coli. Site-directed mutagenesis and chemical modification.

Chemical modification locates guanidinyl and carboxylate groups within the active site of prolidase.

Site-specific chemical modification of peptide and protein by thiazolidinediones.

Selective photochemical modification by trichloroethanol of tryptophan residues in proteins with a high tyrosine-to-tryptophan ratio.

Chemical modification of histidine residues of rabbit hemopexin.

Cysteine residues in the active site of Corynebacterium sarcosine oxidase.

Functional residues at the active site of aminopeptidase N.

Spectroscopic studies on the active site of Sepioteuthis lessoniana hemocyanin.

Chemical modification of arginine residues in alpha-bungarotoxin.

The chemical modification of papain with 1-ethyl-3-(3-dimethylaminopropyl)carbodiimide.

Modulation of the affinity of aspartic proteases by the mutated residues in active site models.

On the role of histidine residues in cyclodextrin glycosyltransferase: chemical modification with diethyl pyrocarbonate.

Studies on the active site of papain. VI. Chemical modification of tryptophan residues by N-bromosuccinimide.

Recommend Documents

Follow Us