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pro vyhledávání: '"Gary S. Howarth"'
Autor:
Gary S. Howarth, Ann E. McDermott
Publikováno v:
Biomolecules, Vol 12, Iss 8, p 1122 (2022)
The structure of the transmembrane domain of the pH-activated bacterial potassium channel KcsA has been extensively characterized, yet little information is available on the structure of its cytosolic, functionally critical N- and C-termini. This stu
Externí odkaz:
https://doaj.org/article/fdf9e539d82f4c02a184cdb8aca38661
Publikováno v:
Biochim Biophys Acta Biomembr
The membrane environment, including specific lipid characteristics, plays important roles in the folding, stability, and gating of the prokaryotic potassium channel KcsA. Here we study the effect of membrane composition on the population of various f
Publikováno v:
Biochimica et Biophysica Acta (BBA) - Biomembranes. 1863:183491
The membrane environment, including specific lipid characteristics, plays important roles in the folding, stability, and gating of the prokaryotic potassium channel KcsA. Here we study the effect of membrane composition on the population of various f
Autor:
Alexei V. Demchenko, Gary S. Howarth, Scott J. Hasty, Larry D. Byers, Archana R. Parameswar, Elizabeth Alverson-Banks Avegno
A new, very efficient, class of thioglycoside substrates has been found for β-glucosidase. While thioglycosides are usually resistant to hydrolysis, even in the presence of acids or most glycohydrolases, the β-D-glucopyranosides of 2- mercaptobenzi
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b1cfba81703b2d663dafa8b58dde3b0
https://europepmc.org/articles/PMC3755622/
https://europepmc.org/articles/PMC3755622/