Work

Kinetics of peptide folding in lipid membranes

Year: 2015

Type: review

Abstract: Despite our extensive understanding of water-soluble protein folding kinetics, much less is known about the folding dynamics and mechanisms of membrane proteins. However, recent studies have shown that for relatively simple systems, such as peptides that form a transmembrane α-helix, helical dimer, or helix-turn-helix, it is possible to assess the kinetics of several important steps, including peptide binding to the membrane from aqueous solution, peptide folding on the membrane surface, helix insertion into the membrane, and helix-helix association inside the membrane. Herein, we provide a brief review of these studies and also suggest new initiation and probing methods that could lead to improved temporal and structural resolution in future experiments.

Source: Biopolymers

DOI: 10.1002/bip.22640

Authors: Kwang‐Im Oh, Kathryn B. Smith‐Dupont, Beatrice N. Markiewicz, Feng Gai

Institutions: University of Pennsylvania, Massachusetts Institute of Technology

Language: English

Topic: Lipid Membrane Structure and Behavior

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

Open Access status: green

Funders: National Institutes of Health, National Institute on Aging, National Institute of General Medical Sciences

Awards: Photo-initiated Disassembly of Fibrils: Application to Amyloids and Hydrogels, Spectroscopic Study of Protein Folding Dynamics, G6517606783