Insights into Cotranslational Nascent Protein Behavior from Computer Simulations.
Regulation of protein stability and function in vivo begins during protein synthesis, when the ribosome translates a messenger RNA into a nascent polypeptide. Cotranslational processes involving a nascent protein include folding, binding to other macromolecules, enzymatic modification, and secretion through membranes. Experiments have shown that the rate at which the ribosome adds amino acids to the elongating nascent chain influences the efficiency of these processes, with alterations to these rates possibly contributing to diseases, including some types of cancer. In this review, we discuss recent insights into cotranslational processes gained from molecular simulations, how different computational approaches have been combined to understand cotranslational processes at multiple scales, and the new scenarios illuminated by these simulations. We conclude by suggesting interesting questions that computational approaches in this research area can address over the next few years.
['Trovato|Fabio|F|', "O'Brien|Edward P|EP|"]
D002462:Cell Membrane D003198:Computer Simulation D056004:Molecular Dynamics Simulation D010452:Peptide Biosynthesis D011485:Protein Binding D014176:Protein Biosynthesis D017510:Protein Folding D017434:Protein Structure, Tertiary D011506:Proteins D012333:RNA, Messenger D012270:Ribosomes D013816:Thermodynamics
nascent protein cotranslational processes molecular simulations biomolecular modeling synonymous mutations translation rate