Zobrazeno 1 - 10
of 22
pro vyhledávání: '"V Kh, Akparov"'
Publikováno v:
Crystallography Reports. 66:476-478
Crystals of mutant carboxypeptidase T from Thermoactinomyces vulgaris (CPT11QG)with amino acid substitutions L211Q, T262S, L254S, and A251S were grown by the hanging-drop vapor-diffusion method. The crystals belong to sp. gr. P6(3)22. The X-ray-diffr
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9988502b970179860218a1c2a36749c4
https://doi.org/10.1134/s1063774521030020
https://doi.org/10.1134/s1063774521030020
Autor:
Ilyas G. Khaliullin, Galina E. Konstantinova, Vladimir I. Timofeev, Inna P. Kuranova, V. Kh. Akparov
Publikováno v:
Crystallography Reports. 65:900-902
Crystals of mutant carboxypeptidase T from Thermoactinomyces vulgaris (CPT11QG) with amino-acid substitutions G215S, Q249G, A251G, T257A, D260G, T262D, and L254I and with the insertion ins253T were grown in microgravity by the capillary counter-diffu
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8c6cf2a1a8b248b92de62ef7e41a9522
https://doi.org/10.1134/s106377452006005x
https://doi.org/10.1134/s106377452006005x
Autor:
Vladimir I. Timofeev, D.A. Korzhenevskiy, V. Kh. Akparov, Inna P. Kuranova, Tatiana V. Rakitina
Publikováno v:
Crystallography Reports. 64:750-757
A mutant of bacterial carboxypeptidase T from Thermoactinomyces vulgaris (CPT5) with amino-acid substitutions in the S1' specificity pocket of the active site for the residues corresponding to the S1' region of pancreatic carboxypeptidase B (Gly215Se
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::829c0b9c21bdac75c3739d035c08e5ff
https://doi.org/10.1134/s1063774519040035
https://doi.org/10.1134/s1063774519040035
Autor:
Ilyas G. Khaliullin, Inna P. Kuranova, Tatiana V. Rakitina, Vladimir I. Timofeev, E. G. Konstantinova, V. Kh. Akparov, Vytas K. Švedas
Publikováno v:
Biochemistry (Moscow). 83:1594-1602
It is generally accepted that the primary specificity of metallocarboxypeptidases is mainly determined by the structure of the so-called primary specificity pocket. However, the G215S/A251G/T257A/D260G/T262D mutant of carboxypeptidase T from Thermoac
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aea6357da63604bc16e2adba5b5e9d87
https://doi.org/10.1134/s0006297918120167
https://doi.org/10.1134/s0006297918120167
Publikováno v:
Crystallography Reports. 62:249-253
Crystals of porcine pancreatic carboxypeptidase B (CPB) were grown by the capillary counter-diffusion method in the presence of polyethylene glycol and zinc acetate. The three-dimensional structure of CPB was determined at 1.40 A resolution using the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::9a3e1cd7d60039b7adaa45f9ccf394fe
https://doi.org/10.1134/s106377451702002x
https://doi.org/10.1134/s106377451702002x
Publikováno v:
Crystallography Reports. 60:367-369
Crystals of porcine pancreatic carboxypeptidase B have been grown in microgravity by the capillary counter-diffusion method through a gel layer. The X-ray diffraction study showed that the crystals belong to sp. gr. P41212 and have the following unit
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::6ce63884dc4161d4b1d3ff8eed5c5788
https://doi.org/10.1134/s1063774515030025
https://doi.org/10.1134/s1063774515030025
Autor:
E. A. Smirnova, Mikhail V. Kovalchuk, Vladimir I. Timofeev, Inna P. Kuranova, Yu. A. Abramchik, Roman S. Esipov, V. Kh. Akparov, L. A. Chupova
Publikováno v:
Crystallography Reports. 56:884-891
Crystals of phosphopantetheine adenylyltransferase from Mycobacterium tuberculosis, thymidine phosphorylase from Escherichia coli, carboxypeptidase T from Thermoactinomyces vulgaris and its mutant forms, and crystals of complexes of these proteins wi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::87f5329bf70accc5d82ed69da4ebe7f9
https://doi.org/10.1134/s1063774511050154
https://doi.org/10.1134/s1063774511050154
Publikováno v:
Crystallography Reports. 56:596-602
Crystals of recombinant carboxypeptidase T (CPT) from Thermoactinomyces vulgaris were grown in a capillary by the counterdiffusion method in the absence of calcium ions. The three-dimensional structure of CPT was solved at 1.69-A resolution using the
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::698e9adb00ebd6a9c0cc96a1868fdfbc
https://doi.org/10.1134/s106377451104002x
https://doi.org/10.1134/s106377451104002x
Publikováno v:
Crystallography Reports. 55:802-805
Recombinant G215S, A251G, T257A, D260G, T262D mutant carboxypeptidase T from Thermoactinomyces vulgaris containing mutations in the primary specificity pocket was prepared and crystallized. Single crystals with a size of up to 0.3 mm were grown and i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::fa50992d74a6c0fc4a9e7bfcb96dffc8
https://doi.org/10.1134/s1063774510050147
https://doi.org/10.1134/s1063774510050147
Autor:
V. P. Lezina, A. A. Morozova, Galina A. Korshunova, Natalia V. Sumbatyan, T. A. Gudasheva, V. Kh. Akparov
Publikováno v:
Russian Journal of Bioorganic Chemistry. 34:550-562
Cyclic peptides cyclo(-Gly-Asp-Glu-Lys-), cyclo(-Gly-Gly-Asp-Glu-Lys-) and cyclo(-Gly-Gly-Gly-Asp-Glu-Lys-) were synthesized as models of theβ-turn of nerve growth factor loop 4. The corresponding protected linear precursors were obtained in 52–83
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::4a52713667df368aadce6d05b4c669e3
https://doi.org/10.1134/s106816200805004x
https://doi.org/10.1134/s106816200805004x