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image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao https://doi.org/10.1...arrow_drop_down
image/svg+xml Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao Closed Access logo, derived from PLoS Open Access logo. This version with transparent background. http://commons.wikimedia.org/wiki/File:Closed_Access_logo_transparent.svg Jakob Voss, based on art designer at PLoS, modified by Wikipedia users Nina and Beao
https://doi.org/10.1007/978-1-...
Part of book or chapter of book . 2014 . Peer-reviewed
License: Springer Nature TDM
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Fundamentals of Peptide-Materials Interfaces

Authors: Tiffany R. Walsh;

Fundamentals of Peptide-Materials Interfaces

Abstract

The investigation of the binding, dynamics and properties of peptides adsorbed on inorganic surfaces is an inherently multidisciplinary endeavor. This chapter is primarily aimed at new researchers in this field, to introduce the basic concepts that span physical chemistry, surface science, structural biology, computational techniques, and materials science; all of which are necessary for gaining a comprehensive overview of peptide-materials interfaces. What are the key insights that can be determined from these interfaces? Usually, this will comprise a blend of thermodynamics, kinetics and structural characterizations. Typically, we might wish to compare the binding strength of a peptide, and concomitantly, the structure(s) assumed by the peptide upon adsorption. We might also seek to characterize the surface diffusion, and/or aggregation (or assembly) of these surface-adsorbed biomolecules. These observations serve to facilitate connections between the composition and sequence of the peptide, and its behavior and properties at the interface. Such connections could be subsequently exploited in bioinformatics models to enable the prediction of new peptide sequences, with designed, predictable interfacial properties.

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selected citations
These citations are derived from selected sources.
This is an alternative to the "Influence" indicator, which also reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Citations provided by BIP!
popularity
This indicator reflects the "current" impact/attention (the "hype") of an article in the research community at large, based on the underlying citation network.
BIP!Popularity provided by BIP!
influence
This indicator reflects the overall/total impact of an article in the research community at large, based on the underlying citation network (diachronically).
BIP!Influence provided by BIP!
impulse
This indicator reflects the initial momentum of an article directly after its publication, based on the underlying citation network.
BIP!Impulse provided by BIP!
2
Average
Average
Average
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