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chymotrypsin/dental caries
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Effect of cavity-creating mutations in the hydrophobic core of chymotrypsin inhibitor 2.
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Hydrophobic residues in the core of a truncated form of chymotrypsin inhibitor 2 (CI2) have been mutated in order to measure their contribution to the stability of the protein. The free energy of unfolding of wild-type and mutants was measured by both guanidinium chloride-induced denaturation and
Nonspecific protein-DNA interactions: complexation of alpha-chymotrypsin with a genomic DNA.
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In this contribution, we report studies on nonspecific protein-DNA interactions of an enzyme protein bovine pancreatic alpha-chymotrypsin (CHT) with genomic DNA (from salmon testes) using two biologically common fluorescent probes: 1-anilinonaphthalene-8-sulfonate (ANS) and
Location and volume of the active site of chymotrypsin.
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The active site of chymotrypsin molecule (approximated by a sphere with radius of 20 A) was taken as the largest cavity on the enzyme surface. The volume inside the approximating sphere is sufficient for placement of 95% of non-hydrogen atoms of the enzyme. The active site cavity is localized in a
Chymotrypsin Adsorption on Montmorillonite: Enzymatic Activity and Kinetic FTIR Structural Analysis.
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Soils have a large solid surface area and high adsorptive capacities. To determine if structural and solvation changes induced by adsorption on clays are related to changes in enzyme activity, alpha-chymotrypsin adsorbed on a phyllosilicate with an electronegative surface (montmorillonite) has been
[The mobility of the side chains of His57 and other amino acid residues in the active center of chymotrypsin].
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Using the "hard-sphere" atom-atom approximation with consideration of the available X-ray data, the possibility of free rotation of the side chain of His57 residue in the active center of chymotrypsin was studied. It was shown that there is a significant rotational freedom of the imidazole ring on
High-pressure stabilization of alpha-chymotrypsin entrapped in reversed micelles of aerosol OT in octane against thermal inactivation.
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alpha-Chymotrypsin (CT) solubilized in reversed micelles of sodium bis-(2-ethylhexyl)-sulfosuccinate (AOT) undergoes thermal inactivation and the enzyme stability decreases significantly when temperature increases (25-40 degrees C). The half-life of CT in micelles shows a bell-shaped dependence on
[Trypsin and chymotrypsin distribution between the fractions of the duodenal contents and the parietal mucosal deposits].
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An attempt has been made to assay the distribution of the typical representatives of pancreatic enzymes such as trypsin and chymotrypsin between dense and liquid fractions of the duodenal contents on an empty stomach and parietal mucous overlaps. The mass of the dense fraction being formed and
Binding of amino acid side chains to preformed cavities: interaction of serine proteinases with turkey ovomucoid third domains with coded and noncoded P1 residues.
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In the association of serine proteinases with their cognate substrates and inhibitors an important interaction is the fitting of the P1 side chain of the substrate or inhibitor into a preformed cavity of the enzyme called the S1 pocket. In turkey ovomucoid third domain, which is a canonical protein
[Interconnection between activity and conformational mobility of alpha-chymotrypsin in reverse micelle systems].
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A comparative study of the catalytic activity of alpha-chymotrypsin and the spin label rotation frequency in the alpha-chymotrypsin active center of reverse micellar systems solvated by H2O-organic mixtures was carried out. It was found that the decrease in the label rotation frequency resulting
[Activity of alpha-chymotrypsin immobilized in nanocapsules of poly(N,N-didodecyl-N,N-diallylammonium bromide)].
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Biocatalytic nanocapsule systems containing alpha-chymotrypsin in the inner aqueous cavity were synthesized. These systems can function in both organic solvents and aqueous media. To this end, the reversed hydrated micelles of N,N-diallyl-N,N-didodecylammonium bromide (DDAB) in cyclohexane (w0 = 22)
Structure and function of aspartate transcarbamoylase studied using chymotrypsin as a probe.
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Aspartate transcarbamoylase from Escherichia coli is composed of six catalytic (c) and six regulatory (r) polypeptides. We have studied the structure and function of this enzyme using chymotrypsin as a probe. The protease inactivates the isolated catalytic subunit (c3) but has not effects on the
Protein recognition of hetero-/homoleptic ruthenium(II) tris(bipyridine)s for α-chymotrypsin and cytochrome c.
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We examined the relationship between the structures of hetero-/homoleptic ruthenium(II) tris(bipyridine) metal complexes (Ru(II)(bpy)(3)) and their binding properties for α-chymotrypsin (ChT) and cytochrome c (cyt c). Heteroleptic compound 1a binds to both ChT and cyt c in 1:1 ratio, whereas
Designing of substrates and inhibitors of bovine alpha-chymotrypsin with synthetic phenylalanine analogues in position P(1).
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The primary specificity residue of a substrate or an inhibitor, called the P(1) residue, is responsible for the proper recognition by the cognate enzyme. This residue enters the S(1) pocket of the enzyme and establishes contacts (up to 50%) inside the proteinase substrate cavity, strongly affecting
The three-dimensional structure of the human alpha 2-macroglobulin dimer reveals its structural organization in the tetrameric native and chymotrypsin alpha 2-macroglobulin complexes.
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Three-dimensional electron microscopy reconstructions of the human alpha(2)-macroglobulin (alpha(2)M) dimer and chymotrypsin-transformed alpha(2)M reveal the structural arrangement of the two dimers that comprise native and proteinase-transformed molecules. They consist of two side-by-side extended
Binding of amino acid side-chains to S1 cavities of serine proteinases.
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The P1 or primary specificity residue of standard mechanism canonical protein inhibitors of serine proteinases, inserts into the S1 primary specificity cavity of the cognate enzyme upon enzyme-inhibitor complex formation. Both natural evolution and protein engineering often change the P1 residue to
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