Affiliations: Oxford Centre for Molecular Sciences, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QH, UK | Center for Molecular and Structural Biology, LNLS, CP 6192, 13084‐971, Campinas, Brazil | LNLS and Department of Biochemistry, University of Campinas, Campinas, Brazil
Note: [] Corresponding author: Dr. L.J. Smith, Central Chemistry Laboratory, University of Oxford, South Parks Road, Oxford, OX1 3QH, UK. Tel.: +44 1865 275961; Fax: +44 1865 275905; E‐mail: [email protected].
Abstract: Peptide fragments taken from residues 18–54 of short consensus repeat 3 (SCR3) from the human complement receptor CR1 have been found in aqueous solution to slowly aggregate and form fibrils. NMR studies of the monomeric form of these peptides show that they are essentially unfolded in aqueous solution and that they all have an increased helicity in TFE solutions. The behaviour of residues 28–31 from SCR3 is particularly interesting. These residues have a high β‐sheet propensity in the native protein and a seven peptide containing their sequence is found to form fibrils despite its short length. However, NMR studies show that these residues adopt a well‐defined α‐helix in 80% TFE and under these conditions fibril formation has not been observed. These data demonstrate the strong dependence of conformational propensities on environment.
Journal: Spectroscopy, vol. 18, no. 1, pp. 1-11, 2004
