L Rekha Reddy

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Relatamos algumas moléculas híbridas baseadas na N-(quinolina-3-ilmetileno)benzoidrazida, cuja síntese foi realizada usando-se 2-cloroquinolina-3-carbaldeído e uma variedade de hidrazidas substituídas, em PEG 400. O solvente PEG 400 foi recuperado e reutilizado diversas vezes na presente reação, mostrando-se eficiente em termos de rendimento dos produtos.(More)
Three Hb S variants containing Glu substitutions at Phe-beta85 and/or Leu-beta88 were expressed in yeast in an effort to evaluate the role of hydrophobic amino acids at these sites in stabilizing F helix conformation of Hb S. Helix stability of tetrameric Hb S betaF85E,betaL88E was measured by CD and compared with those of Hb S betaF85E, Hb S betaL88E, Hb(More)
To understand determinants for hemoglobin (Hb) stability and Hb A2 inhibition of Hb S polymerization, three Valdelta6 Hb A2 variants (Hb A2 deltaE6V, Hb A2 deltaE6V,deltaQ87T, and Hb A2 deltaE6V, deltaA22E,deltaQ87T) were expressed in yeast, and stability to mechanical agitation and polymerization properties were assessed. Oxy forms of Hb A2 deltaE6V and Hb(More)
In order to investigate the role of the R (relaxed) to T (tense) structural transition in facilitating polymerization of deoxy-Hb S, we have engineered and expressed two Hb S variants which destabilize either T state (Hb S-Kempsey, alpha 2 beta 2 Val-6,Asn-99) or R state structures (Hb S-Kansas, alpha 2 beta 2 Val-6, Thr-102). Polymerization of deoxy-Hb(More)
Three new Hb S variants containing beta87 Leu, Trp, or Asp instead of Thr were expressed in yeast in order to further define the role of the beta87 position in stability and polymerization of deoxy Hb S. Previous studies showed that hydrophobicity at beta85 Phe and beta88 Leu is critical for stabilization of hemoglobin. Results with the three Hb S beta87(More)
Hemoglobin (Hb) S containing Leu, Ala, Thr, or Trp substitutions at beta 85 were made and expressed in yeast in an effort to evaluate the role of Phe-beta 85 in the acceptor pocket during polymerization of deoxy Hb S. The four Hb S variants have the same electrophoretic mobility as Hb S, and these beta 85 substitutions do not significantly affect(More)
Characterization of the hydrophobic EF acceptor pocket involving Phe-beta 85 and Leu-beta 88 as well as the Val-beta 6 donor site is critical for understanding the polymerization of deoxy Hb S. Glu substitutions at beta 85 or beta 88 in Hb S were made and expressed in yeast in an effort to evaluate the role of hydrophobicity in the acceptor pocket during(More)
The system reliability, performance, cost, and leakage power in deep sub micrometer era have a significant impact by thermal hotspots and temperature gradients. As the system complexity increases, it is very difficult to perform thermal management in a centralized approach due to state explosion and the overhead of monitoring the entire chip. In this work,(More)
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