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Unusual conformational transitions of leucine-containing basic polytripeptides

✍ Scribed by ŠTěPánka Šokrová; Miloslav Bohdanecký; Blahoslav Sedlá Ček; Karel Bláha; Jaroslav Šponar

Book ID
102765940
Publisher
Wiley (John Wiley & Sons)
Year
1986
Tongue
English
Weight
948 KB
Volume
25
Category
Article
ISSN
0006-3525

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✦ Synopsis

The conformational transitions of synthetic basic polytripeptides (Lys-Leu-Gly)., (A,bu-Leu-Gly),, (Lys-Leu-Ala),, and (A,bu-Leu-Ala), induced by high salt concentrations and elevated pH were investigated by CD, ir, and 'H-nmr spectroscopy, sedimentation analysis, viscometry, and light scattering. Sheet aggregates of chains in a conformation similar to the polyglycine I1 (polyproline 11) helix, bound together by hydrogen bonds, are the most probable form of (Lys-Leu-Gly), and also, partly, of (Azbu-Leu-Gly), in a high-pH or high-salt solutions. The conformation (Lys-Leu-Ala),, in a low-salt concentration, is an a-helix. Since (A,bu-Leu-Ala). is disordered under similar conditions, it appears that this a-helix is stabilized by hydrophobic interactions between Lys and Leu side chains. In a high concentration of water structure-making ions, CD data for (Lys-Leu-Ala), indicate distortion of the a-helix, with a parallel increase in the average molecular weight corresponding to trimer formation. Hydrodynamic data are consistent with a model of bundles of three closely touching spherocylinders. (A,bu-Leu-Ala), shows a limited tendency to a-helix formation.

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