Loop structure in human serum albumin from Raman optical activity

Teraoka, J., Bell, A. F., Hecht, L. and Barron, L. D. (1998) Loop structure in human serum albumin from Raman optical activity. Journal of Raman Spectroscopy, 29(1), pp. 67-71. (doi: 10.1002/(SICI)1097-4555(199801)29:1<67::AID-JRS207>3.0.CO;2-U)

Full text not currently available from Enlighten.


Vibrational Raman optical activity (ROA) measurements on human serum albumin are reported and discussed. At neutral pH, the ROA spectrum in the normal state N is dominated by bands assigned to α-helix together with a strong positive ROA band at ca. 1340 cm-1 assigned to a loop structure with local order possibly that of a 310-helix. On reducing the pH to 3.4, which generates the molten globule-like F state, only small decreases in the α-helix ROA bands occur, but the ca. 1340 cm-1 band decreases by ca. 40%, reflecting a loss of rigidity of part of the loop structure, possibly involving residues 292–315 since these connect the two halves of the molecule thought to be dissociated in the F state. These results suggest that the long loops comprising residues 106–119, 292–315 and 492–511 which connect subdomains A and B within each of the three domains I, II and III and previously described from x-ray studies simply as extended polypeptide might in fact have local order of a 310-helix.

Item Type:Articles
Additional Information:We thank the Biotechnology and Biological Sciences Research Council for a Research Grant and the Engineering and Physical Sciences Research Council for a Senior Fellowship for L.D.B.
Glasgow Author(s) Enlighten ID:Hecht, Dr Lutz and Barron, Professor Laurence
Authors: Teraoka, J., Bell, A. F., Hecht, L., and Barron, L. D.
College/School:College of Science and Engineering > School of Chemistry
Journal Name:Journal of Raman Spectroscopy
ISSN (Online):1097-4555
Published Online:04 December 1998

University Staff: Request a correction | Enlighten Editors: Update this record