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Updated: Jul 7, 2026

Detection of Protein S-Acylation using Acyl-Resin Assisted Capture
Published on: April 10, 2020
A hydrophobic loop in acyl-CoA binding protein is functionally important for binding to palmitoyl-coenzyme A: a
Diego F G Vallejo1, J Raúl Grigera, Marcelo D Costabel
1Instituto de Física de Líquidos y Sistemas Biológicos (IFLYSIB), UNLP-CONICET-CIC, Argentina.
Abstract:
Acyl-CoA binding protein (ACBP) plays a key role in lipid metabolism, interacting via a partly unknown mechanism with high affinity with long chain fatty acyl-CoAs (LCFA-CoAs). At present there is no study of the microscopic way ligand binding is accomplished. We analyzed this process by molecular dynamics (MDs) simulations. We proposed a computational model of ligand, able to reproduce some evidence from nuclear magnetic resonance (NMR) data, quantitative time resolved fluorometry and X-ray crystallography. We found that a hydrophobic loop, not in the active site, is important for function. Besides, multiple sequence alignment shows hydrophobicity (and not the residues itselves) conservation.
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