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Autor:
Christopher M. Lauderback, David Allan Butterfield, Jaroslaw Kanski, Marina V. Aksenova, Sridhar Varadarajan
Publikováno v:
Journal of the American Chemical Society. 123(24)
Oxidative stress induced by amyloid beta-peptide (A beta) has been implicated in the neurodegeneration observed in Alzheimer's disease (AD) brain. However, the mechanism by which the predominant form of A beta found in AD brains, A beta(1--42), cause
Publikováno v:
Journal of the American Chemical Society, vol 137, iss 35
Optical modulation of proteins provides superior spatiotemporal resolution for understanding biological processes, and photoswitches built on light-sensitive proteins have been significantly advancing neuronal and cellular studies. Small molecule pho
Autor:
Michal Avital-Shmilovici, Kalyaneswar Mandal, Nelson B. Phillips, Michael A. Weiss, Zachary P. Gates, Stephen B. H. Kent
Publikováno v:
Journal of the American Chemical Society. 135:3173-3185
Efficient total synthesis of insulin is important to enable the application of medicinal chemistry to the optimization of the properties of this important protein molecule. Recently we described "ester insulin"--a novel form of insulin in which the f
Autor:
Ann E. McDermott, Justin L. Lorieau
Publikováno v:
Journal of the American Chemical Society. 128:11505-11512
The majority of protein structures are determined in the crystalline state, yet few methods exist for the characterization of dynamics for crystalline biomolecules. Solid-state NMR can be used to probe detailed dynamic information in crystalline biom
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(22)
NMR-based drug screening methods provide the most reliable characterization of binding propensities of ligands to their target proteins. Unique to NMR is its capability to detect weak microM-mM bindings. NMR assays are, however, one of the least effe
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
Publikováno v:
Journal of the American Chemical Society. 130:2428-2429
Hydrogen bonds play critical roles in protein structure, stability, and function. Conventionally, hydrogen bonds are mainly determined by X-ray crystallography and NOE-based NMR spectroscopy in indirect manners. In recent years, it was demonstrated t