By Ariel Fernández Stigliano
The e-book makes a speciality of the aqueous interface of biomolecules, a necessary but ignored quarter of biophysical examine. 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 usher in the appearance of a brand new self-discipline, epistructural biology, established at the interactions of water and bio molecular constructions around the interface. the writer introduces strong theoretical and computational assets for you to tackle basic subject matters reminiscent of protein folding, the physico-chemical foundation of enzyme catalysis and protein institutions. at the foundation of this data, a multi-disciplinary process is used to engineer healing medicinal drugs and to permit substantive advances in specified molecular drugs. This ebook may be of curiosity to scientists, scholars and practitioners within the fields of chemistry, biophysics and biomedical engineering.
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Additional resources for Biomolecular Interfaces: Interactions, Functions and Drug Design
Nature 437:640–647 19. Jewett A, Pande VS, Plaxco KW (2003) Cooperativity, smooth energy landscapes and the origins of topology-dependent protein folding rates. J Mol Biol 326:247–253 32 1 The Aqueous Interface of a Soluble Protein … 20. 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.
The mean Y-value and standard deviation were computed for each n-group and the results are shown in Fig. 8a. 96) results and is further corroborated by the raw X-Y-trendline generated by linear regression on all (X, Y) data points (Fig. 8b). Taken together, the results from Fig. 8 unambiguously reveal a simple balance relation Y = 5X + 20. This statistical relation introduces a 1:5 ratio to buttress vulnerable proteins and allows for a 20 %-baseline in structural deﬁciency. To illustrate the role of this relation in deﬁning protein structure we focus on speciﬁc examples of proteins with widely diverse levels of structural deﬁciency.
This ﬁeld is given by xÀ1 U R (ω = volume of test hydrophobe). 5 Dehydron Stickiness: Epistructural View of Biomolecular Interfaces 19 where integration extends over the closed surface of the dehydration domain of the hydrogen bond (cf. Fig. 4) and drð~ RÞ is the differential surface area vector. To fully understand dehydron stickiness, it is useful at this stage to switch back to the solvent-centric view of the protein-water interface. The object we need to focus on is the 4 Å-radius solvation shell of the atom closest to the center of a backbone hydrogen bond and containing at least one water oxygen in the shell.
Biomolecular Interfaces: Interactions, Functions and Drug Design by Ariel Fernández Stigliano