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ribonuclease/τερηδόνα
Ο σύνδεσμος αποθηκεύεται στο πρόχειρο
Σελίδα 1 από 55 Αποτελέσματα
Stabilization of Escherichia coli ribonuclease HI by cavity-filling mutations within a hydrophobic core.
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Σύνδεση εγγραφή
The crystal structure of Escherichia coli ribonuclease HI has a cavity near Val-74 within the protein core. In order to fill the cavity space, we constructed two mutant proteins, V74L and V74I, in which Val-74 was replaced with either Leu or Ile, respectively. The mutant proteins are stabilized, as
Crystallographic structures of ribonuclease S variants with nonpolar substitution at position 13: packing and cavities.
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Σύνδεση εγγραφή
Seven hydrophobic residues ranging in size from glycine to phenylalanine have been substituted for the wild-type methionine residue at position 13 in a 15-residue truncated version (S15) of S-peptide, the small component of ribonuclease S. Complexes of both S-15 and the seven variants with S-protein
Effect of cavity-modulating mutations on the stability of Escherichia coli ribonuclease HI.
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The size of the cavity around Ser68 of Escherichia coli ribonuclease HI was modulated by amino acid substitutions to examine the effects on the stability of the enzyme. Five mutant proteins, Ser68----Gly, Ser68----Ala, Ser68----Thr, Ser68----Val and Ser68----Leu, were constructed. Each of the mutant
The binding of 3'-N-piperidine-4-carboxyl-3'-deoxy-ara-uridine to ribonuclease A in the crystal.
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The binding of a moderate inhibitor, 3'-N-piperidine-4-carboxyl-3'-deoxy-ara-uridine, to ribonuclease A has been studied by X-ray crystallography at 1.7A resolution. Two inhibitor molecules are bound in the central RNA binding cavity of RNase A exploiting interactions with residues from peripheral
Compactness of thermally and chemically denatured ribonuclease A as revealed by volume and compressibility.
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The conformational changes of ribonuclease A due to thermal and guanidine hydrochloride denaturation were monitored by means of precise density and sound velocity measurements. It was found that the apparent molar volume decreased but the adiabatic compressibility increased on thermal denaturation
Action of bull seminal vesicle ribonuclease on mouse leukaemic cells BP-8 and EL-4.
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Bull seminal vesicle ribonuclease, when added in vitro to the suspension of ascitic leukaemic cells EL-4 and BP-8 for 2 hours at 37 degrees C and then transplanted to the abdominal cavities of mice, inhibitied the proliferation of these cells in vivo. When the temperature of the medium was decreased
Structural stability and internal motions of Escherichia coli ribonuclease HI: 15N relaxation and hydrogen-deuterium exchange analyses.
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The relationship between the structural stability and the internal motions of proteins was investigated through measurements of 15N relaxation and hydrogen-deuterium exchange rates of ribonuclease HI from Escherichia coli and its thermostable quintuple mutant (Gly23-->Ala, His62-->Pro, Val74-->Leu,
Mapping the stability clusters in bovine pancreatic ribonuclease A.
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In the present work, we have thermodynamically characterized the thermally induced unfolding of 20 variants of bovine pancreatic ribonuclease A (RNase A) to experimentally describe the residues and the regions that are critical for the stability of the enzyme. The achieved results, complemented with
Structural basis of m(7)GpppG binding to poly(A)-specific ribonuclease.
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Poly(A)-specific ribonuclease (PARN) is a homodimeric, processive, and cap-interacting 3' exoribonuclease that efficiently degrades eukaryotic mRNA poly(A) tails. The crystal structure of a C-terminally truncated PARN in complex with m(7)GpppG reveals that, in one subunit, m(7)GpppG binds to a
Studying salt effects on protein stability using ribonuclease t1 as a model system.
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Salt ions affect protein stability in a variety of ways. In general, these effects have either been interpreted from a charge solvation/charge screening standpoint or they have been considered to be the result of ion-specific interactions with a particular protein. Recent theoretical work suggests
Tri- and tetra-substituted cyclen based lanthanide(III) ion complexes as ribonuclease mimics: a study into the effect of log Ka, hydration and hydrophobicity on phosphodiester hydrolysis of the RNA-model 2-hydroxypropyl-4-nitrophenyl phosphate (HPNP).
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A series of tetra-substituted 'pseudo' dipeptide ligands of cyclen (1,4,7,10,-tetraazacyclododecane) and a tri-substituted 3'-pyridine ligand of cyclen, and the corresponding lanthanide(III) complexes were synthesised and characterised as metallo-ribonuclease mimics. All complexes were shown to
Crystal structure of ribonuclease T1 complexed with adenosine 2'-monophosphate at 1.8-A resolution.
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Ribonuclease T1 was purified from an Escherichia coli overproducing strain and co-crystallized with adenosine 2'-monophosphate (2'-AMP) by microdialysis against 50% (v/v) 2-methyl-2,4-pentanediol in 20 mM sodium acetate, 2 mM calcium acetate, pH 4.2. The crystals have orthorhombic space group
A potential allosteric subsite generated by domain swapping in bovine seminal ribonuclease.
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Bovine seminal ribonuclease (BS-RNase) is a peculiar member of the pancreatic-like ribonuclease superfamily endowed with unique biological functions. It has been shown that native BS-RNase is a mixture of two distinct dimeric forms. The most abundant form is characterised by the swapping of the
The crystal structure of ribonuclease B at 2.5-A resolution.
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The glycosylated form of bovine pancreatic ribonuclease, RNase B, was crystallized from polyethylene glycol 4000 at low ionic strength in space group C2 with unit cell dimensions of a = 101.81 A, b = 33.36 A, c = 73.60 A, and beta = 90.4 degrees. The crystals, which contained two independent
Rapid hydrolytic cleavage of the mRNA model compound HPNP by glycine based macrocyclic lanthanide ribonuclease mimics.
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The lanthanide ion based macrocyclic complexes 1.Ln mimic the hydrophobic nature of ribonucleases, where the lanthanide ions induce the formation of a hydrophobic cavity for 1, giving rise to a large order of magnitude enhancement in the hydrolytic cleavage of HPNP.
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