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Identification of Novel Umami Peptides from Yak Bone Collagen and Mechanism Exploration Through <i>In Silico</i> Discovery, Molecular Docking, and Electronic Tongue. [PDF]
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Nature, 1968
A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure,
J, Drenth +4 more
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A three-dimensional X-ray study at a resolution of 2.8 A has revealed that the single polypeptide chain of 211 residues is folded into two distinct parts which are divided by a cleft. The active site, consisting of a cysteine and a histidine, lies at the surface of the cleft. Apart from four short α-helical segments and one short segment of β-structure,
J, Drenth +4 more
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Thiirancarboxamides as Inhibitors of Papain
Archiv der Pharmazie, 2004AbstractDerivatives of the thiirancarboxylic acid building‐block containing a peptide bond were synthesised and screened against the model cysteine protease papain. The most active of the series showed a second‐order rate constant of inactivation comparable to that of the parent compound.
Gemma, Bruno, Tanja, Schirmeister
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1971
Publisher Summary The fruits of the tropical papaya tree have latex that contains several enzymes. This chapter focuses on two different proteolytic enzymes: chymopapain and papain. Both enzymes belong to the group of proteolytic plant enzymes that require a sulfhydryl group for activity.
J, Drenth +3 more
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Publisher Summary The fruits of the tropical papaya tree have latex that contains several enzymes. This chapter focuses on two different proteolytic enzymes: chymopapain and papain. Both enzymes belong to the group of proteolytic plant enzymes that require a sulfhydryl group for activity.
J, Drenth +3 more
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Biochemical and Biophysical Research Communications, 1970
Abstract Papain possesses several regions of internal homology and similar shape. The enzyme probably formed through a series of gene doublings.
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Abstract Papain possesses several regions of internal homology and similar shape. The enzyme probably formed through a series of gene doublings.
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