Interfacial nano-structuring of designed peptides regulated by solution pH.

Journal article

The in-situ conformations of peptide layers formed from the adsorption of two different synthetic 15-mer peptides at the hydrophilic silicon oxide/aqueous solution interface have been determined using neutron reflectivity (NR). The first peptide is based on the native sequence of a protein-binding domain within a heteromeric transcriptional activator, HAP2, identified from yeast Saccharomyces cerevisiae, with tyrosine (Y) present at the 1st, 8th and 15th amino acid positions, hence we denote ...

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Authors: Lu, JR; Perumal, S; Hopkinson, I; Webster, JR; Penfold, J

• Publication status: Published
• Journal: Journal of the American Chemical Society
• Volume: 126
• Issue: 29
• Pages: 8940-8947
• Publication date: 2004-07-01
• DOI: 10.1021/ja049477r
• EISSN: 1520-5126
• ISSN: 0002-7863
• Language: English
• Keywords: Models, Molecular; Tryptophan; Neutrons; Solutions; Protein Structure, Secondary; Peptide Fragments; Tyrosine; Nanotechnology; Molecular Sequence Data; Scattering, Radiation; Fungal Proteins; CCAAT-Binding Factor; Amino Acid Sequence; Hydrogen-Ion Concentration