Solution structure of a peptide fragment of human alpha-lactalbumin in trifluoroethanol: a model for local structure in the molten globule.

Journal article

BACKGROUND: At low pH, human alpha-lactalbumin forms a partly folded molten globule state that contains a non-native clustering of the side chains of Tyr103, Trp104 and His107. In order to understand the conformation of this region of the protein in the molten globule state, we investigated the structure of a peptide corresponding to residues 101-110 of human alpha-lactalbumin in trifluoroethanol. RESULTS: We determined the structure of the 101-110 peptide from an NMR data set of 145 nuclear ...

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Authors: Smith, L; Alexandrescu, A; Pitkeathly, M; Dobson, C

• Publication status: Published
• Journal: Structure (London, England : 1993)
• Volume: 2
• Issue: 8
• Pages: 703-712
• Publication date: 1994-08-01
• DOI: 10.1016/s0969-2126(00)00071-x
• EISSN: 1878-4186
• ISSN: 0969-2126
• Language: English
• Keywords: Amino Acid Sequence; Molecular Sequence Data; Models, Molecular; Computer Simulation; Magnetic Resonance Spectroscopy; Humans; Protein Folding; Protein Structure, Secondary; Solutions; Peptide Fragments; Trifluoroethanol; Lactalbumin