Search Results - "Rakitina, T V"

Comparative Analysis of the Interfaces between Monomers in the Dimers of Bacterial Histone-Like HU Proteins by the MM-GBSA Method by Agapova, Yu. K., Petrenko, D. E., Timofeev, V. I., Rakitina, T. V.

“…This study aims to perform a comparative analysis of the interfaces between monomers in the dimers of bacterial histone-like DNA-binding proteins (HU proteins)…”
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Prospects of Application of D-amino Acid Transaminase from Aminobacterium colombiense for (R)-selective Amination of α‑Keto Acids by Shilova, S. A., Rakitina, T. V., Popov, V. O., Bezsudnova, E. Yu

“…D-amino acid transaminase from Aminobacterium colombiense was applied for ( R )-selective amination of 2-oxobutyrate, 2-oxovalerate and 2-oxo-4-phenylbutyrate…”
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Preliminary X-ray Diffraction Analysis of the Envelope (E) Protein of Far-Eastern Tick-Borne Encephalitis Virus Subtype (Sofjin Strain) by Dubova, K. M., Vlaskina, A. V., Korzhenevskiy, D. A., Agapova, Yu. K., Rakitina, T. V., Samygina, V. R.

“…The envelope (E) protein of flaviviruses is an attractive target for the development of antiviral agents because this protein plays an important role in the…”
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Improvement of the Diffraction Properties of Thiocyanate Dehydrogenase Crystals by Varfolomeeva, L. A., Polyakov, K. M., Komolov, A. S., Rakitina, T. V., Dergousova, N. I., Dorovatovskii, P. V., Boyko, K. M., Tikhonova, T. V., Popov, V. O.

“…During determination of the thiocyanate dehydrogenase (TcDH) structure difficulties have occurred, related to the fact that enzyme crystals have been either…”
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Molecular Dynamics and Small-Angle X-ray Scattering: Comparison of Computational and Experimental Approaches to Studying Structures of Biological Complexes by Petoukhov, M. V., Rakitina, T. V., Agapova, Yu. K., Petrenko, D. E., Podshivalov, D. D., Timofeev, V. I., Peters, G. S., Gaponov, Yu. A., Bocharov, E. V., Shtykova, E. V.

“…The results of investigation of DNA-protein complexes by two independent structural methods, namely, molecular dynamics (MD) and small-angle X-ray scattering…”
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Comparative Structural Investigation of Histone-Like HU Proteins by Small-Angle X-ray Scattering by Petoukhov, M. V., Rakitina, T. V., Agapova, Yu. K., Petrenko, D. E., Konarev, P. V., Britikov, V. V., Britikova, E. V., Bocharov, E. V., Shtykova, E. V.

“…Nucleoid-associated proteins (NAPs) control the structure and functions of bacterial nucleoid. Histone-like HU proteins are most abundant NAPs in dividing…”
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Study of the Binding Free Energy of Peptide Substrates in the Active Site of Oligopeptidase B from Serratia proteamaculans by the MM-GBSA Method by Petrenko, D. E., Timofeev, V. I., Karlinsky, D. M., Plashchinskaia, D. D., Mikhailova, A. G., Rakitina, T. V.

“…This study is devoted to the modeling and thermodynamic analysis of enzyme–substrate complexes. The complexes consist of wild-type oligopeptidase B (ОрВ) from…”
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Erratum to: Preliminary X-ray Diffraction Analysis of the Envelope (E) Protein of Far-Eastern Tick-Borne Encephalitis Virus Subtype (Sofjin Strain) by Dubova, K. M., Vlaskina, A. V., Korzhenevskiy, D. A., Agapova, Yu. K., Rakitina, T. V., Samygina, V. R.

“…An Erratum to this paper has been published: https://doi.org/10.1134/S1063774522070501…”
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Effect of Disruption of the Interface between Monomers in a Dimer on the Structural and Dynamic Properties of the HU Protein from Spiroplasma Melliferum by Komolov, A. S., Agapova, Yu. K., Timofeev, V. I., Rakitina, T. V.

“…The effect of replacements of amino-acid residues that form the interface between monomers in a dimer of the HU protein from Spiroplasma Melliferum (HUSpm) on…”
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Three-Dimensional Structure of Thermostable D-Amino Acid Transaminase from the Archaeon Methanocaldococcus jannaschii DSM 2661 by Boyko, K. M., Nikolaeva, A. Yu, Bakunova, A. K., Stekhanova, T. N., Rakitina, T. V., Popov, V. O., Bezsudnova, E. Yu

“…Pyridoxal 5′-phosphate (PLP)-dependent transaminases catalyze the stereospecific amino-group transfer from an amino acid or amine to ketone or keto acid…”
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Mobile Loop in the Active Site of Metallocarboxypeptidases as an Underestimated Determinant of Substrate Specificity by Akparov, V. Kh, Timofeev, V. I., Khaliullin, I. G., Konstantinova, E. G., Kuranova, I. P., Rakitina, T. V., Švedas, V. K.

“…It is generally accepted that the primary specificity of metallocarboxypeptidases is mainly determined by the structure of the so–called primary specificity…”
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Virtual Screening Targeting Dimerization Signals of Two Mycoplasma HU Proteins Revealed Different Types of Inhibitors Interacting with Common Binding Determinants by Agapova, Yu. K., Talyzina, A. A., Altukhov, D. A., Lavrentiev, A. L., Timofeev, V. I., Rakitina, T. V.

“…DNA-Binding HU proteins are critical to the maintenance of the nucleoid structure and are promising pharmacological targets for the design of new antibiotics…”
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Three-Dimensional Structure of a Mutant of Carboxypeptidase T from Thermoactinomyces vulgaris Bearing an Implanted S1' Subsite of Pancreatic Carboxypeptidase B Complexed with a Product Analog by Akparov, V. Kh, Timofeev, V. I., Korzhenevskiy, D. A., Kuranova, I. P., Rakitina, T. V.

“…A mutant of bacterial carboxypeptidase T from Thermoactinomyces vulgaris (CPT5) with amino-acid substitutions in the S1' specificity pocket of the active site…”
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Screening of Conditions that Facilitate Crystallization of Oligopeptidase B from Serratia Proteamaculans by Differential Scanning Fluorimetry by Petrenko, D. E., Nikolaeva, A. Yu, Lazarenko, V. A., Dorovatovskii, P. V., Timofeev, V. I., Vlaskina, A. V., Korzhenevskiy, D. A., Mikhailova, A. G., Rakitina, T. V.

“…Oligopeptidases B (OpdBs) are two-domain serine peptidases with trypsin-like substrate specificity belonging to the prolyl oligopeptidase family. These enzymes…”
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Molecular Dynamics Study of Binding of Substrates Bearing Two Positively Charged Residues to Oligopeptidase B from Serratia proteamaculans by Agapova, Yu. K., Talyzina, A. A., Zeifman, Yu. S., Fateeva, T. V., Timofeev, V. I., Mikhailova, A. G., Rakitina, T. V.

“…The behavior of the peptide substrates GlyArgArgGly and GlyLysArgGly, which contain arginine or lysine at the Р2 position, in the active site of oligopeptidase…”
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Proteome of HU-Lacking E. coli Studied by Means of 2D Gel Electrophoresis by Kamashev, D. E., Rakitina, T. V., Matyushkina, D. S., Evsyutina, D. V., Vanyushkina, A. A., Agapova, Yu. K., Anisimova, V. E., Drobyshev, A. L., Butenko, I. O., Pobeguts, O. V., Fisunov, G. Y.

“…Histone-like protein HU is a dimeric nucleoid-associated protein (NAP). HU is the most conserved NAP. It binds nonspecifically to duplex DNA with a preference…”
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Truncated variants of Serratia proteamaculans oligopeptidase B having different activities by Mikhailova, A. G., Nekrasov, A. N., Zinchenko, A. A., Rakitina, T. V., Korzhenevsky, D. A., Lipkin, A. V., Razguljaeva, O. A., Ovchinnikova, M. V., Gorlenko, V. A., Rumsh, L. D.

“…Treatment of native psychrophilic oligopeptidase B from Serratia proteamaculans (PSP, 78 kDa) with chymotrypsin (soluble or immobilized on modified porous…”
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Application of virtual screening and molecular dynamics for the analysis of selectivity of inhibitors of HU proteins targeted to the DNA-recognition site by Talyzina, A. A., Agapova, Yu. K., Podshivalov, D. D., Timofeev, V. I., Sidorov-Biryukov, D. D., Rakitina, T. V.

“…DNA-Binding HU proteins are essential for the maintenance of genomic DNA supercoiling and compaction in prokaryotic cells and are promising pharmacological…”
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Mutation L232H Promotes Chromophore Maturation of EGFP-Based Fluorescent Fusion Proteins by Simanovskaya, A. A., Ivashina, T. V., Zeifman, Y. S., Fateeva, T. V., Krukova, M. V., Popov, A. N., Kachalova, G. S., Rakitina, T. V.

“…The L232H mutant of the enhanced green fluorescent protein (EGFP) was expressed and crystallized. An X-ray diffraction data set was collected from the crystals…”
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Structure of the dodecamer of the aminopeptidase APDkam598 from the archaeon Desulfurococcus kamchatkensis by Petrova, T. E., Slutskaya, E. S., Boyko, K. M., Sokolova, O. S., Rakitina, T. V., Korzhenevskiy, D. A., Gorbacheva, M. A., Bezsudnova, E. Y., Popov, V. O.

“…The crystal structure of the aminopeptidase APDkam589 from the thermophilic crenarchaeon Desulfurococcus kamchatkensis was determined at a resolution of 3.0 Å…”
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