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

By Ariel Fernández Stigliano

The booklet specializes in the aqueous interface of biomolecules, an essential but neglected quarter of biophysical examine. such a lot 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 bring in the arrival of a brand new self-discipline, epistructural biology, headquartered at the interactions of water and bio molecular buildings around the interface. the writer introduces robust theoretical and computational assets as a way to tackle basic subject matters comparable to protein folding, the physico-chemical foundation of enzyme catalysis and protein institutions. at the foundation of this knowledge, a multi-disciplinary process is used to engineer healing medications and to permit substantial advances in particular molecular drugs. This booklet could be of curiosity to scientists, scholars and practitioners within the fields of chemistry, biophysics and biomedical engineering.

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Sample text

Thus, the thermal denaturation free energy change, ΔG, under reducing conditions and comparable temperatures [47, 48] was obtained for monomeric uncomplexed PDB-reported proteins with disulfide bonds and lacking prosthetic groups or ion coordination. 72, Fig. 10) between the deviation from the balance equation, measured as Y – (5X + 20), and the thermal denaturation free energy (ΔG). This tight anticorrelation provides a thermodynamic validation of the balance equation. 92 1RHB 1K5A a SCOP structural classification of proteins (Murzin et al.

Fernández A (2003) What caliber pore is like a pipe? Nanotubes as modulators of ion gradients. J Chem Phys 119:5315–5319 41. Despa F, Fernández A, Berry RS (2004) Dielectric modulation of biological water. 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.

Pietrosemoli N, Crespo A, Fernández A (2007) Dehydration propensity of order-disorder intermediate regions in soluble proteins. J Proteome Res 6:3519–3526 29. Fernández A, Scott R (2003) Dehydron: a structure-encoded signal for protein interactions. Biophys J 85:1914–1928 30. Avbelj F, Baldwin RL (2003) Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi. Proc Natl Acad Sci USA 100:5742–5747 31. Krantz BA, Moran LB, Kentsis A, Sosnick TR (2000) D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding.

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