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Biointerphases

Journal for Biophysical Chemistry

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Directions in peptide interfacial science

Biointerphases volume 1, pages P5–P11 (2006)Cite this article

Abstract

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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Author information

Affiliations

  1. Department of Chemistry, University of California, 94720, Berkeley, California

    Ozzy Mermut, Roger L. York & Diana C. Phillips

  2. Materials Science Division, Lawrence Berkeley National Laboratory, 94720, Berkeley, California

    Ozzy Mermut, Roger L. York, Diana C. Phillips & Gabor A. Somorjai

  3. The Polymer Technology Group, 2810 Seventh Street, 94710, Berkeley, California

    Keith R. McCrea & Robert S. Ward

  4. Department of Chemistry, University of California, 94720, Berkeley, California

    Gabor A. Somorjai

Authors
  1. Ozzy Mermut
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  2. Roger L. York
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  3. Diana C. Phillips
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  4. Keith R. McCrea
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  5. Robert S. Ward
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  6. Gabor A. Somorjai
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Mermut, O., York, R.L., Phillips, D.C. et al. Directions in peptide interfacial science. Biointerphases 1, P5–P11 (2006). https://doi.org/10.1116/1.2194033

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  • DOI: https://doi.org/10.1116/1.2194033