Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Aditya Natarajan"'
Autor:
Filip Yabukarski, Todd J. Martínez, Ruibin Liang, Tzanko Doukov, Margaux M. Pinney, Daniel Herschlag, Aditya Natarajan, Fang Liu, David M. Sanchez, Jason P. Schwans
Publikováno v:
Journal of the American Chemical Society. 140:9827-9843
Hydrogen bonds are fundamental to biological systems and are regularly found in networks implicated in folding, molecular recognition, catalysis, and allostery. Given their ubiquity, we asked the fundamental questions of whether, and to what extent,
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7e6ee3ca33e9d0cea6206798ec53bbd5
https://doi.org/10.1021/jacs.8b01596
https://doi.org/10.1021/jacs.8b01596
Publikováno v:
Journal of the American Chemical Society
Hydrogen bonds are ubiquitous in enzyme active sites, providing binding interactions and stabilizing charge rearrangements on substrate groups over the course of a reaction. But understanding the origin and magnitude of their catalytic contributions
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7df641b204a4add9a4acee5158c4a4a3
http://europepmc.org/articles/PMC4046884
http://europepmc.org/articles/PMC4046884
Autor:
Ido Braslavsky, Christopher P. Garnham, Adam J. Middleton, Aditya Natarajan, Peter L. Davies, Mike Kuiper
Publikováno v:
Biochemistry. 49:9063-9071
By binding to the surface of ice crystals, type III antifreeze protein (AFP) can depress the freezing point of fish blood to below that of freezing seawater. This 7-kDa globular protein is encoded by a multigene family that produces two major isoform
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::d7bd7af8575faf13417b18176402eb2c
https://doi.org/10.1021/bi100516e
https://doi.org/10.1021/bi100516e
Autor:
Daniel Herschlag, Aditya Natarajan
Publikováno v:
Biochemistry. 52(12)
Enzymes are remarkable catalysts that lie at the heart of biology, accelerating chemical reactions to an astounding extent with extraordinary specificity. Enormous progress in understanding the chemical basis of enzymatic transformations and the basi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::42655e40082aa597aacce27a9f5fc647
https://pubmed.ncbi.nlm.nih.gov/23488725
https://pubmed.ncbi.nlm.nih.gov/23488725
Ground state destabilization from a positioned general base in the ketosteroid isomerase active site
Autor:
Aditya Natarajan, Matthew Sonnett, Daniel Herschlag, Jason P. Schwans, Eliza A. Ruben, Ana Gonzalez, Yingssu Tsai
Publikováno v:
Biochemistry. 52(6)
We compared the binding affinities of ground state analogues for bacterial ketosteroid isomerase (KSI) with a wild-type anionic Asp general base and with uncharged Asn and Ala in the general base position to provide a measure of potential ground stat
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::5deb8406e37e7a8a48ae5870003ea801
https://pubmed.ncbi.nlm.nih.gov/23311398
https://pubmed.ncbi.nlm.nih.gov/23311398
Autor:
Jason P. Schwans, Daniel Herschlag, Aditya Natarajan, Fanny Sunden, Filip Yabukarski, Vandana Lamba
Publikováno v:
Science. 349:936-936
Fried et al . (Reports, 19 December 2014, p. 1510) demonstrated a strong correlation between reaction rate and the carbonyl stretching frequency of a product analog bound to ketosteroid isomerase oxyanion hole mutants and concluded that the active-si
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::82ac21996bbd16b57800d792ba29b936
https://doi.org/10.1126/science.aab1584
https://doi.org/10.1126/science.aab1584