By Ariel Fernández Stigliano
The e-book makes a speciality of the aqueous interface of biomolecules, an important but missed zone of biophysical learn. such a lot organic phenomena can't be absolutely understood on the molecular point with no contemplating interfacial behavior.
The writer provides conceptual advances in molecular biophysics that bring in the appearance of a brand new self-discipline, epistructural biology, headquartered at the interactions of water and bio molecular constructions around the interface. the writer introduces strong theoretical and computational assets that allows you to tackle primary subject matters equivalent to protein folding, the physico-chemical foundation of enzyme catalysis and protein institutions. at the foundation of this data, a multi-disciplinary technique is used to engineer healing medicinal drugs and to permit important advances in specified molecular medication. This booklet should be of curiosity to scientists, scholars and practitioners within the fields of chemistry, biophysics and biomedical engineering.
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Additional info for Biomolecular Interfaces: Interactions, Functions and Drug Design
The net gain in Coulomb energy associated with wrapping a dehydron has been 18 1 The Aqueous Interface of a Soluble Protein … experimentally determined to be *4 kJ/mol . 8 pN, a magnitude comparable to the hydrophobic attraction between two nonpolar moieties that frame unfavorable interfaces with water. This study was motivated by the earlier observations that dehydrons play a pivotal role in driving protein associations, as such associations contribute intermolecularly to the wrapping of preformed structure [27, 29], as discussed in the previous section.
Scalley-Kim M, Baker D (2004) Characterization of the folding energy landscapes of computer generated proteins suggests high folding free energy barriers and cooperativity may be consequences of natural selection. J Mol Biol 338:573–583 21. Fernández A, Colubri A, Berry RS (2002) Three-body correlations in protein folding: the origin of cooperativity. Phys A 307:235–259 22. Fernández A, Kostov K, Berry RS (1999) From residue matching patterns to protein folding topographies: general model and bovine pancreatic trypsin inhibitor.
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.