ISSN:
0006-3525
Keywords:
Chemistry
;
Polymer and Materials Science
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Chemistry and Pharmacology
Notes:
The conformation of two fragments of rabbit uteroglobin is described. The peptides are PRFAHVIENLL and PQTTRENIMKLTEKIVK, corresponding to helices I and IV in the crystal structure. CD shows that both peptides interact with sodium dodecyl sulfate (SDS) micelles and change their conformation to an α-helix. The helical content estimated from the CD band at 222 nm is about 40% in each peptide. Surface tension measurements show that both peptides lower the critical micellar concentration (cmc) of SDS, with a more dramatic effect in the case of helix I. This peptide by itself acts as a surfactant, and is able to interact with SDS even below the observed cmc, forming β aggregates. Proton magnetic resonance (1H-nmr) suggests that flexible helices are present. The longest helical stretches compatible with 1H-nmr data extend from Phe6 to Leu14 for helix I and from Arg53 to Ile63 for helix IV. © 1993 John Wiley & Sons, Inc.
Additional Material:
14 Ill.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1002/bip.360331213
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