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of 3
pro vyhledávání: '"Michelle N. Pollock"'
Autor:
Michael W. Capp, Laurel M. Pegram, Record Mt, Hyo Keun Cha, Michelle N. Pollock, Emily J. Guinn
Publikováno v:
Biophysical Journal. 102(3)
Solutes have a broad range of effects on biopolymer processes, forming a spectrum from destabilizers like urea to more stabilizing osmolytes like proline, glycine betaine (GB) and KGlutamate to secondary structure inducers like trifluorethanol. To ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0e7ad7b81b460c938994ebd4a7c65531
To explain the large, opposite effects of urea and glycine betaine (GB) on stability of folded proteins and protein complexes, we quantify and interpret preferential interactions of urea with 45 model compounds displaying protein functional groups an
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::fcc5cf395bc24c661d7496c69c71068b
https://europepmc.org/articles/PMC3193240/
https://europepmc.org/articles/PMC3193240/
Autor:
Dana Bellissimo, Michelle N. Pollock, Laurel M. Pegram, Record Mt, Xiaoyi Qu, Michael W. Capp, Joanne Tsarouha, Emily J. Guinn
Publikováno v:
Biophysical Journal. 100:213a
To develop the use of urea, trifluoroethanol, KGlutamate, proline and other biochemical solutes as probes of interface formation and large scale conformational changes in protein and DNA processes, we are quantifying the thermodynamics of the competi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0bdaa577cd56d6493ffc3bde70d6156a
https://doi.org/10.1016/j.bpj.2010.12.1378
https://doi.org/10.1016/j.bpj.2010.12.1378