Probing free energy of transmembrane helix-helix association via a novel single-residue based approach

Free energy profiles for each type of interaction can be obtained basedon a given spatial structure of the transmembrane (TM) dimer usingmolecular dynamics (MD) with umbrella sampling and potential of meanforce (PMF) calculation. GlycophorinA (GpA) is one of the well-studiedmembrane proteins. There is a lot of experimental and theoretical dataobtained, but little is known about the role of environment in GpA TMdimer formation. So, the main goal of the present work is to estimatecontributions of all components (protein, lipids, water) in association ofTMhelices for the wild-typeGpA TMdimer and itsmutant form. Also, anew algorithm of residue-based energy decomposition was proposed and tested. © 2013 by Nova Science Publishers, Inc. All rights reserved.

IBCH: 4311
Кол-во цитирований на 10.2023: 0
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