By Victor Muñoz, Stephen Neidle, David M J Lilley, Marius Clore, Simon Campbell, Roderick E Hubbard, Peter Wolynes, Vijay Pande, Andrew Doig, Ben Schuler, Martin Gruebele, Yawen Bai, Luis Moroder, Jose M Sanchez-Ruiz, Andreas Lehmann, Jeff Saven, Luis Serran
This distinct publication covers all of the smooth techniques and the numerous advances skilled within the box over the past 10 years. there's a lot emphasis on computational tools and stories of protein aggregation that have fairly flourished within the final decade. It comprises chapters within the parts that experience witnessed significant advancements and written by way of most sensible specialists together with: machine simulations of folding, speedy folding, unmarried molecule spectroscopy, protein layout, aggregation reviews (both computational and experimental). Readers will receive a different point of view of the issues confronted within the biophysical research of protein conformational habit in aqueous answer and the way those difficulties are being solved with a multidisciplinary method that mixes idea, test and machine simulations.
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Extra info for Protein Folding, Misfolding and Aggregation: Classical Themes and Novel Approaches
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Analyses of the resulting kinetics are not straightforward due to the complexity involved in the measurements and in providing a theoretical description to explain them quantitatively. The i,i + 4 hydrogen bonding pattern in an a-helix implies that the conformation of each residue is aﬀected by at most i,i + 4 (and/or i,i À 4) nearest neighbors. This renders quasione-dimensionality to the a-helix. Unlike proteins where diﬀerent parts of the chain that are far apart in sequence are brought together, the a-helix is primarily stabilized by local interactions.