Loop structure in human serum albumin from Raman optical activity
✍ Scribed by Junji Teraoka; Alasdair F. Bell; Lutz Hecht; Laurence D. Barron
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 250 KB
- Volume
- 29
- Category
- Article
- ISSN
- 0377-0486
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✦ Synopsis
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 a-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 On reducing the pH to 3.4, which generates the molten globule-like F state, only small decreases in the 3 10 -helix. a-helix ROA bands occur, but the ca. 1340 cm-1 band decreases by ca. 40%, reÑecting 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 1998 John 3 10 -helix. (