Zobrazeno 1 - 10
of 34
pro vyhledávání: '"Sergei Khrapunov"'
Publikováno v:
Biochemistry
Temperature adaptation is ubiquitous among all living organisms, yet the molecular basis for this process remains poorly understood. It can be assumed that for parasite-host systems, the same enzymes found in both organisms respond to the same select
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::9f8354ac1db092dc74f031156f5e804b
https://europepmc.org/articles/PMC8672703/
https://europepmc.org/articles/PMC8672703/
Publikováno v:
Biochemistry. 56:3587-3595
The thermodynamics of substrate binding and enzymatic activity of a glycolytic enzyme, lactate dehydrogenase (LDH), from both porcine heart, phLDH (Sus scrofa; a mesophile), and mackerel icefish, cgLDH (Chamapsocephalus gunnari; a psychrophile), were
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::909acf5b616fb0ddd1c5316b83f53e5a
https://doi.org/10.1021/acs.biochem.7b00156
https://doi.org/10.1021/acs.biochem.7b00156
Autor:
Sergei Khrapunov
Publikováno v:
Current proteinpeptide science. 19(11)
The thermodynamic analyses of proteins, protein-ligands and protein-nucleic acid complexes involves the entropy-enthalpy (S-H) compensation phenomenon. We have examined the question whether the observed compensation is artificial or reflects anything
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ca7042c64cb9fab6d366fb49d116fe9a
https://pubmed.ncbi.nlm.nih.gov/29779476
https://pubmed.ncbi.nlm.nih.gov/29779476
Autor:
Richard Harris, Mark E. Girvin, Camille Padlan, Yisong Tao, Aristea S. Galanopoulou, Sergei Khrapunov, Michael Brenowitz, John M. Greally, Huiyong Cheng
Publikováno v:
Biochemistry. 55(31)
Methyl-CpG binding protein 2 (MeCP2) is a multifunctional protein that guides neuronal development through its binding to DNA, recognition of sites of methyl-CpG (mCpG) DNA modification, and interaction with other regulatory proteins. Our study explo
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::62c235e9341ec8b1dbbdace872d88737
https://pubmed.ncbi.nlm.nih.gov/27420643
https://pubmed.ncbi.nlm.nih.gov/27420643
Publikováno v:
Biophysical Journal. 112:56a-57a
The thermodynamics of oxamate binding and the temperature stability of the glycolytic enzyme lactate dehydrogenase from porcine heart, phLDH (mesophilic Sus scrofa) and from mackerel icefish, cgLDH (psychrophilic Chamapsocephalus gunnari) have been i
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::8cb59be4d233554d5893df5005b6075c
https://doi.org/10.1016/j.bpj.2016.11.342
https://doi.org/10.1016/j.bpj.2016.11.342
Publikováno v:
Biophysical Journal. 114:50a
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::58d9efa0051873b0d6f691c120607691
https://doi.org/10.1016/j.bpj.2017.11.328
https://doi.org/10.1016/j.bpj.2017.11.328
Publikováno v:
Journal of Biological Chemistry. 283:36290-36299
The pentapeptide repeat is a recently discovered protein fold. Mycobacterium tuberculosis MfpA is a founding member of the pentapeptide repeat protein (PRP) family that confers resistance to the antibiotic fluoroquinolone by binding to DNA gyrase and
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::941f7ca643bed1fb8af47698b2f68461
https://doi.org/10.1074/jbc.m804702200
https://doi.org/10.1074/jbc.m804702200
Autor:
A. K. M. M. Mollah, Sayan Gupta, Sergei Khrapunov, Mark R. Chance, Stephanie Morris, Michael Brenowitz, Huiyong Cheng, Elizabeth Jamison
Publikováno v:
Biochemistry. 46:9886-9898
Recombinant full-length Saccharomyces cerevisiae TATA binding protein (TBP) and its isolated C-terminal conserved core domain (TBPc) were prepared with measured high specific DNA-binding activities. Direct, quantitative comparison of TATA box binding
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::46daecd462586ef1e0a5283343772251
https://doi.org/10.1021/bi7003608
https://doi.org/10.1021/bi7003608
Autor:
Sergei Khrapunov, Michael Brenowitz
Publikováno v:
Biophysical Journal. 86(1):371-383
The formation of sequence-specific complexes of TATA binding protein (TBP) with the minor groove of DNA results in the burial of large nonpolar surfaces and the exclusion of water from these interfaces. The release of water is thus expected to provid
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::02ab0160e8b3116a61fbaccd769674ac
Publikováno v:
Biochemistry. 41:9559-9571
The intrinsic fluorescence of the six tyrosines located within the C-terminal domain of the Saccharomyces cerevisiae TATA binding protein (TBP) and the single tryptophan located in the N-terminal domain has been used to separately probe the structura
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::022279a33fece5f577cae77bd0caed61
https://doi.org/10.1021/bi0255773
https://doi.org/10.1021/bi0255773