Adsorption of polypeptides on the solid surface. II. Effect of secondary chain structure and helix–coil transition

✍ Scribed by E. B. Zhulina; T. M. Birshtein; A. M. Skvortsov

• Publisher: Wiley (John Wiley & Sons)
• Year: 1980
• Tongue: English
• Weight: 837 KB
• Volume: 19
• Category: Article
• ISSN: 0006-3525
• DOI: 10.1002/bip.1980.360190407

✦ Synopsis

Abstract

The theory of adsorption of semistiff chains on a planar surface developed by the authors previously has been used to consider the helix–coil transition in single‐stranded macromolecule interacting with an adsorbent plane. The cases of nonselective interaction when the adsorption energy is independent of the unit conformation (a) and selective interaction with only helical (b) or coiled (c) sequences active in adsorption were investigated. In case (b) the existence of secondary structure favors chain bonding to the surface. This leads to the increase in the stability of the helical state and complete polypeptide chain spiralization. The profile of the conformational helix–coil transition acquires an asymmetrical shape inherent to the second‐order phase transition.

In case (c) the bonding of a partially helical chain to the surface is similar to the adsorption of Gaussian coils and is accompanied by the destruction of secondary structure, this destruction being appreciable even if the helical state in space was favorable.