Zobrazeno 1 - 7
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pro vyhledávání: '"35"'
Autor:
Yang J; Department of Physics, and Program of Biophysics, The Ohio State University, Columbus, Ohio 43210, USA., Zhang L, Wang L, Zhong D
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2012 Oct 10; Vol. 134 (40), pp. 16460-3. Date of Electronic Publication: 2012 Sep 26.
Autor:
Skalicky JJ; Contribution from the Department of Chemistry, State University of New York at Buffalo, Buffalo, New York 14260, USA., Mills JL, Sharma S, Szyperski T
Publikováno v:
Journal of the American Chemical Society [J Am Chem Soc] 2001 Jan 24; Vol. 123 (3), pp. 388-97.
Autor:
Sung Hyun Yoo, Jérémie Buratto, Arup Roy, Estelle Morvan, Morgane Pasco, Karolina Pulka-Ziach, Caterina M. Lombardo, Frédéric Rosu, Valérie Gabelica, Cameron D. Mackereth, Gavin W. Collie, Gilles Guichard
Publikováno v:
Journal of the American Chemical Society
Journal of the American Chemical Society, 2022, 144 (35), pp.15988-15998. ⟨10.1021/jacs.2c05234⟩
Journal of the American Chemical Society, 2022, 144 (35), pp.15988-15998. ⟨10.1021/jacs.2c05234⟩
International audience; Amphipathic water-soluble helices formed from synthetic peptides or foldamers are promising building blocks for the creation of self-assembled architectures with non-natural shapes and functions. While rationally designed arti
Publikováno v:
Journal of the American Chemical Society, 125(35), 10570-10579. AMER CHEMICAL SOC
The binding of a series of p-alkylbenzamidinium chloride inhibitors to the serine proteinase trypsin over a range of temperatures has been studied using isothermal titration (micro)calorimetry and molecular dynamics simulation techniques. The inhibit
Publikováno v:
Journal of the American Chemical Society. 131(3)
Unlike most ordered molecular systems, globular proteins exhibit a temperature of maximum stability, implying that the structure can be disrupted by cooling. This cold denaturation phenomenon is usually linked to the temperature-dependent hydrophobic
Publikováno v:
Journal of the American Chemical Society. 129(10)
In this paper, we present a series of heteronuclear NMR experiments for the direct observation and characterization of lysine NH3 groups in proteins. In the context of the HoxD9 homeodomain bound specifically to DNA we were able to directly observe t
Publikováno v:
Journal of the American Chemical Society. 123(3)
We have characterized, for the first time, motional modes of a protein dissolved in supercooled water: the flipping kinetics of phenylalanyl and tyrosinyl rings of the 6 kDa protein BPTI have been investigated by NMR at temperatures between -3 and -1