Protein folding: From physico-chemical rules and cellular machineries of protein quality control to AI solutions
Year: 2024
Type: article
Abstract: Practically every biological process in our cells relies on the function of proteins, acting either as single molecules or parts of larger assemblies.Proteins (from the Greek prōteios, of the first order) are the most diverse group of macromolecules.Following their synthesis on ribosomes as amino acid polymer chains, typically hundreds of residues in length, most proteins must fold into well-defined three-dimensional structures in order to become biologically active.While the threedimensional (3D) structures of proteins are of remarkable complexity (Fig. 1), the intramolecular interactions that drive the folding process are mainly dependent on a multiplicity of noncovalent, energetically weak interactions.Therefore, how the amino acid sequence, encoded in the genetic information, determines the folded state of a protein (1) remains a fundamental problem in biology, driven by the long-standing desire to predict the fold from the amino acid sequence.
Authors: Ulyana Shimanovich, F. Ulrich Hartl
Language: English
Subfield: Molecular Biology
Domain: Life Sciences
Open Access status: hybrid
OpenAlex ID: W4401506332