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Directions in peptide interfacial science
Author(s) -
Ozzy Mermut,
Roger L. York,
Diana Phillips,
Keith R. McCrea,
Robert S. Ward,
Gábor A. Somorjai
Publication year - 2006
Publication title -
biointerphases
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.633
H-Index - 45
eISSN - 1934-8630
pISSN - 1559-4106
DOI - 10.1116/1.2194033
Subject(s) - biomolecule , chemical physics , adsorption , chemistry , biomolecular structure , molecular dynamics , nanotechnology , nanoscopic scale , surface finish , ion , aqueous solution , surface roughness , materials science , computational chemistry , protein structure , organic chemistry , biochemistry , composite material
The evolution of biological surface science can be credited to the development of traditional surface-chemistry tools and techniques to investigate molecular and atomic-scale bonding, structure, conformation, physical properties (e.g., chemical, electronic, mechanical), and dynamics of adsorbates at various interfaces:1 Both classical measurements of surface behavior and features (i.e., adsorption isotherms, surface areas, roughness, thickness, and topography) and modern spectroscopic-based techniques that provide information on elemental composition, oxidation state, depth profiling, and distribution of chemical species have shown applicability to the study of biomolecular interactions.1 However, experiments that probe with electrons, atoms or ions require ultrahigh vacuum (UHV) or reduced pressures at the interface, and are thus intrinsically limited with regards to interfacial explorations in an aqueous environment, i.e., the study of at biomolecules the solid/water interface.1

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