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

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

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

Potentiometric determination of ionizations at the active site of papain.

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

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

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.

The pKa value of the active site histidine in photo-oxidised papain.

Resonance Raman evidence for substrate reorginization in the active site of papain.

Stability and unfolding studies on papain.

Site-directed mutagenesis identifies catalytic residues in the active site of Escherichia coli phosphofructokinase.

The tryptophan residues of aspartate transcarbamylase: site-directed mutagenesis and time-resolved fluorescence spectroscopy.

Site-directed alteration of four active-site residues of a pyruvoyl-dependent histidine decarboxylase.

Site-directed mutagenesis of catalytic active-site residues of Taka-amylase A.

Evidence for the involvement of tryptophan 38 in the active site of glutathione S-transferase P.

An essential tryptophan in the active site of phospholipase A2 from the venom of Bitis gabonica.

Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.

Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli.

Effect of active site residues in barnase on activity and stability.

Tryptophan fluorescence studies of ferredoxin:NADP reductase indicate the presence of tryptophan in or near the ferredoxin binding site.

Occurrence of tryptophan in the enzymically active site of diphtheria toxin fragment A.

Functional significance of active site residues in the enzymatic component of the Clostridium difficile binary toxin.

Cloning of the Pseudomonas glumae lipase gene and determination of the active site residues.

Suggest Documents

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

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

Potentiometric determination of ionizations at the active site of papain.

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

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

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.

The pKa value of the active site histidine in photo-oxidised papain.

Resonance Raman evidence for substrate reorginization in the active site of papain.

Stability and unfolding studies on papain.

Site-directed mutagenesis identifies catalytic residues in the active site of Escherichia coli phosphofructokinase.

The tryptophan residues of aspartate transcarbamylase: site-directed mutagenesis and time-resolved fluorescence spectroscopy.

Site-directed alteration of four active-site residues of a pyruvoyl-dependent histidine decarboxylase.

Site-directed mutagenesis of catalytic active-site residues of Taka-amylase A.

Evidence for the involvement of tryptophan 38 in the active site of glutathione S-transferase P.

An essential tryptophan in the active site of phospholipase A2 from the venom of Bitis gabonica.

Active site structure of methylamine dehydrogenase: hydrazines identify C6 as the reactive site of the tryptophan-derived quinone cofactor.

Role of tryptophan 248 in the active site of tryptophanase from Escherichia coli.

Effect of active site residues in barnase on activity and stability.

Tryptophan fluorescence studies of ferredoxin:NADP reductase indicate the presence of tryptophan in or near the ferredoxin binding site.

Occurrence of tryptophan in the enzymically active site of diphtheria toxin fragment A.

Functional significance of active site residues in the enzymatic component of the Clostridium difficile binary toxin.

Cloning of the Pseudomonas glumae lipase gene and determination of the active site residues.

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

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