Location and Conformation of the LKα14 Peptide in Water/Ethanol Mixtures.

ABSTRACT: It is widely recognized that solvation is one of the major factors determining structure and functionality of proteins and long peptides, however it is a formidable challenge to address it both experimentally and computationally. For this reason, simple peptides are used to study fundamental aspects of solvation. It is well established that alcohols can change the peptide conformation and tuning of the alcohol content in solution can dramatically affect folding and, as a consequence, the function of the peptide. In this work, we focus on the leucine and lysine based LKα14 peptide designed to adopt an α-helical conformation at an apolar-polar interface. We investigate LKα14 peptide's bulk and interfacial behavior in water/ethanol mixtures combining a suite of experimental techniques (namely

SUBMITTER: Maltseva D 

PROVIDER: S-EPMC7871320 | biostudies-literature | 2021 Jan

REPOSITORIES: biostudies-literature