Read e-book online Biomolecular Interfaces: Interactions, Functions and Drug PDF

By Ariel Fernández Stigliano

ISBN-10: 3319168495

ISBN-13: 9783319168494

ISBN-10: 3319168509

ISBN-13: 9783319168500

The publication specializes in the aqueous interface of biomolecules, an essential but ignored sector of biophysical learn. so much organic phenomena can't be totally understood on the molecular point with out contemplating interfacial behavior.

The writer offers conceptual advances in molecular biophysics that usher in the arrival of a brand new self-discipline, epistructural biology, based at the interactions of water and bio molecular buildings around the interface. the writer introduces robust theoretical and computational assets so one can deal with primary subject matters comparable to protein folding, the physico-chemical foundation of enzyme catalysis and protein institutions. at the foundation of this data, a multi-disciplinary strategy is used to engineer healing medicines and to permit great advances in specific molecular drugs. This e-book may be of curiosity to scientists, scholars and practitioners within the fields of chemistry, biophysics and biomedical engineering.

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Phys Rev Lett 93:228104 42. Demetri G (2002) Efficacy and safety of imatinib mesyalte in advanced gastrointestinal stromal tumors. N Engl J Med 347:472–480 43. Fernández A, Sanguino A, Peng Z, Ozturk E, Chen J, Crespo A, Wulf S, Shavrin A, Qin C, Ma J, Trent J, Lin Y, Han HD, Mangala LS, Bankson JA, Gelovani J, Samarel A, Bornmann References 44. 45. 46. 47. 48. 49. 50. 33 W, Sood AK, Lopez-Berestein G (2007) An anticancer c-Kit kinase inhibitor is reengineered to make it more active and less cardiotoxic.

Chap. 1). These packing defects expose the backbone polar groups amide (>N–H) and carbonyl (>C=O) to structure-disruptive effects of backbone hydration with the net effect of steering water dipoles into orientations that are not collinear with ~ E. The confined water molecules relinquish some of their hydrogen-bonding possibilities in order to form hydrogen bonds with the backbone polar groups. This reduction in coordination represents a departure from the bulk water structure embodied in the tetrahedral lattice and the resulting water polarization becomes statistically independent of the internal field ~ E.

Thus, protein adsorption is commensurate with photon loss resulting from the extent of local refraction or “evanescent field”. Hence adsorption uptake can be determined by the loss of photons due to refractive photon leakage from the total reflection pattern. For proteins with comparable surface hydrophobicity, the adsorption uptake correlates strongly with the extent of protein under-wrapping [34]. As an adequate control, only proteins with the same extent of surface hydrophobicity or solventexposed nonpolar area were included in the comparative analysis.

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Biomolecular Interfaces: Interactions, Functions and Drug Design by Ariel Fernández Stigliano


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