Zobrazeno 1 - 7
of 7
pro vyhledávání: '"Chandana Kasireddy"'
Publikováno v:
Physical Chemistry Chemical Physics. 24:19233-19251
New Cδ-H⋯O histidine hydrogen bonding interactions in various proteins are identified by neutron diffraction and computationally characterized. Neutron diffraction data shows several H-bond motifs with the Cδ-H moiety in histidine side chains, in
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::778548acf01e44add12225b23ac20cb3
https://doi.org/10.1039/d2cp02048c
https://doi.org/10.1039/d2cp02048c
Autor:
Jayangika Niroshani Dahanayake, Elaheh Shahryari, Micah E. Heikes, Chandana Kasireddy, Katie R. Mitchell-Koch, Kirsten M. Roberts
Publikováno v:
J Chem Inf Model
The solvation layer surrounding a protein is clearly an intrinsic part of protein structure-dynamics-function, and our understanding of how the hydration dynamics influences protein function is emerging. We have recently reported simulations indicati
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::964f73f860b49db18bc8e2418943419a
https://doi.org/10.1021/acs.jcim.9b00009
https://doi.org/10.1021/acs.jcim.9b00009
Autor:
Joseph P. Karnes, Jonathan M. Ellis, Olivia A. Hull, Jayangika Niroshani Dahanayake, Chandana Kasireddy, Katie R. Mitchell-Koch, Rajni Verma, Ryan M. Steinert, Derek Hildebrandt
Fluorine NMR spectroscopy has diverse applications, including characterization of chemical reaction mechanisms, protein structure–function studies, and solid-state NMR characterization of crystalline, amorphous, and soft materials. Computational me
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::cb9d403d3405c9c52501de124f1e9d68
https://doi.org/10.1016/bs.arnmr.2017.08.002
https://doi.org/10.1016/bs.arnmr.2017.08.002
Publikováno v:
Physical Chemistry Chemical Physics. 17:30606-30612
Fluorine NMR spectroscopy is a powerful tool for studying biomolecular structure, dynamics, and ligand binding, yet the origins of (19)F chemical shifts are not well understood. Herein, we use electronic structure calculations to describe the changes
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0eef8ec46d7236a47e3df59ee94374a0
https://doi.org/10.1039/c5cp05502d
https://doi.org/10.1039/c5cp05502d
Autor:
Joseph P. Karnes, Olivia A. Hull, Jonathan M. Ellis, Derek Hildebrandt, Chandana Kasireddy, Katie R. Mitchell-Koch, Jayangika Niroshani Dahanayake, Dylan Morlan
The ability of electronic structure methods (11 density functionals, HF, and MP2 calculations; two basis sets and two solvation models) to accurately calculate the 19 F chemical shifts of 31 structures of fluorinated amino acids and analogues with kn
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::398f0a27bde8c7a4f2a042bb0687aa69
https://europepmc.org/articles/PMC5638705/
https://europepmc.org/articles/PMC5638705/
Publikováno v:
Scientific Reports
Fluorinated amino acids serve as valuable biological probes, by reporting on local protein structure and dynamics through 19F NMR chemical shifts. 2-fluorohistidine and 4-fluorohistidine, studied here with DFT methods, have even more capabilities for
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ef861c18cbe28de34f1e8bca8bd3f360
http://europepmc.org/articles/PMC5309746
http://europepmc.org/articles/PMC5309746
Ribonuclease A is the oldest model for studying enzymatic mechanisms, yet questions remain about proton transfer within the active site. Seminal work by Jackson et al. (Science, 1994) labeled Ribonuclease A with 4-fluorohistidine, concluding that act
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ac08af7388624b07bc003e437e81357c
https://europepmc.org/articles/PMC5461937/
https://europepmc.org/articles/PMC5461937/