Zobrazeno 1 - 10
of 48
pro vyhledávání: '"Kathryn A, Thomasson"'
Autor:
Eric N. Njabon, Issofa Patouossa, Kristine L. Carlson, Stephen L. Lowe, Neville Y. Forlemu, Kathryn A. Thomasson
Publikováno v:
Scientific African, Vol 9, Iss , Pp e00510- (2020)
Glycolytic enzymes may compartment in cells by binding to cytoskeletal structures. One potentially important step in compartmentation is the binding of the cytoskeletal protein F-actin by lactate dehydrogenase (LDH). Brownian dynamics (BD) simulation
Externí odkaz:
https://doaj.org/article/f5c397bd29fb4955a6f0b9981545cbe0
Autor:
Igor V. Uporov, Neville Y. Forlemu, Rahul Nori, Tsvetan Aleksandrov, Boris A. Sango, Yvonne E. Bongfen Mbote, Sandeep Pothuganti, Kathryn A. Thomasson
Publikováno v:
International Journal of Molecular Sciences, Vol 16, Iss 9, Pp 21237-21276 (2015)
The dipole interaction model is a classical electromagnetic theory for calculating circular dichroism (CD) resulting from the π-π* transitions of amides. The theoretical model, pioneered by J. Applequist, is assembled into a package, DInaMo, writte
Externí odkaz:
https://doaj.org/article/96e2c945b66c4b6ea6f7d7be6863add2
Publikováno v:
Chemical Papers. 75:1937-1948
Experimental studies have shown that many glycolytic enzymes bind cytoskeletal proteins reversibly including lactate dehydrogenase (LDH) and that the interaction may be electrostatic in nature. LDH is particularly interesting because different isofor
Autor:
Neville Y. Forlemu, Kristine L. Carlson, Kathryn A. Thomasson, Issofa Patouossa, Eric N. Njabon, Stephen L. Lowe
Publikováno v:
Scientific African, Vol 9, Iss, Pp e00510-(2020)
Glycolytic enzymes may compartment in cells by binding to cytoskeletal structures. One potentially important step in compartmentation is the binding of the cytoskeletal protein F-actin by lactate dehydrogenase (LDH). Brownian dynamics (BD) simulation
Autor:
Ethan R. Austhof, Kathryn A. Thomasson, I. V. Uporov, Akongnwi C. Jungong, Rahul Nori, Emily Holt, Felix N. Ngassa
Publikováno v:
Biophysical Journal. 110(3)
The dipole interaction model, an implementation of classical electromagnetic theory, is assembled in a computer package: DInaMo/CDCALC. This package is very successful in predicting the far-UV CD π-π∗ transition of proteins, replicating the peak
Autor:
Victor F. Waingeh, Kristine L. Carlson, Elizabeth Spanbauer Schmidt, Eric N. Njabon, Kathryn A. Thomasson, Neville Y. Forlemu
Publikováno v:
Proteins: Structure, Function, and Bioinformatics. 79:2813-2827
The association of glycolytic enzymes with F-actin is proposed to be one mechanism by which these enzymes are compartmentalized, and, as a result, may possibly play important roles for: regulation of the glycolytic pathway, potential substrate channe
Publikováno v:
International Journal of Peptide and Protein Research. 47:447-459
Semi-empirical energy calculations were performed for published conformations of cyclo (Gly-Pro-Gly)2 using different force fields (DISCOVER cvff and cff91, AMBER, and CHARMM). The resulting potential energies were then used to create Boltzmann weigh
Autor:
G. Kie-Adams, R.R. Pandey, Mark R. Hoffmann, Kathryn A. Thomasson, Ken S. Pierce, Stephen L. Lowe, J. Czlapinski
Publikováno v:
The Journal of Peptide Research. 61:189-201
Cyclo(l-Pro)3 (CP3) is a synthetic peptide created to model cis and torsionally strained peptide bonds that also exhibits a strong distinctive UV circular dichroic (CD) spectrum. Circular dichroic spectra were computed for the amide pi-pi* transition
Autor:
Tsvetan Aleksandrov, Akongnwi C. Jungong, Rahul Nori, Emma Miller, I. V. Uporov, Jenna Soukup, Kathryn A. Thomasson
Publikováno v:
Biophysical Journal. 108(2)
The dipole interaction model (assembled into the computer package DInaMo) uses a classical electromagnetic theory for calculating the far UV circular dichroism (CD) of peptides and proteins. DInaMo reduces all amide chromophores to a single point wit