Navigating the complexities of multi-domain protein folding
Nandakumar Rajasekaran, Christian Kaiser
Abstract
Proteome complexity has expanded tremendously over evolutionary time, enabling biological diversification. Much of this complexity is achieved by combining a limited set of structural units into long polypeptides. This widely used evolutionary strategy poses challenges for folding of the resulting multi-domain proteins. As a consequence, their folding differs from that of small single-domain proteins, which generally fold quickly and reversibly. Co-translational processes and chaperone interactions are important aspects of multi-domain protein folding. In this review, we discuss some of the recent experimental progress toward understanding these processes.
Topics & Concepts
Protein foldingComputational biologyProteomeFolding (DSP implementation)Chaperone (clinical)Domain (mathematical analysis)Diversification (marketing strategy)WW domainProtein domainComputer scienceHuman proteome projectChemistryBiologyBioinformaticsCell biologyProteomicsBiochemistryEngineeringMathematicsBusinessGeneMedicineMarketingMathematical analysisElectrical engineeringPathologyProtein Structure and DynamicsRNA and protein synthesis mechanismsEnzyme Structure and Function