Protein folding coupled to binding of a specific ligand is frequently observed in biological processes. In recent years numerous studies have addressed the structural properties of the unfolded proteins in the absence of their ligands. Surprisingly few time-resolved investigations on coupled folding and binding reactions have been published up to date and the dynamics and kinetic mechanisms of these processes are still only poorly understood. Especially, it is still unsolved for most systems which conformation of the protein is recognized by the ligand (conformational selection vs. folding-after-binding) and whether the ligand influences the folding kinetics. Here we review experimental methods, kinetic models and time-resolved experimental studies of coupled folding and binding reactions.
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http://dx.doi.org/10.1016/j.sbi.2011.09.010 | DOI Listing |
Biophys J
January 2025
Department of Chemistry, University of Alabama at Birmingham, Birmingham, Alabama. Electronic address:
The Hsp100 family of protein disaggregases play important roles in maintaining protein homeostasis in cells. E. coli ClpB is an Hsp100 protein that solubilizes protein aggregates.
View Article and Find Full Text PDFInt J Mol Sci
January 2025
Department of Chemistry and Biochemistry, Montana State University, Bozeman, MT 59717, USA.
Dansyl labeling is a widely used approach for enhancing the detection of small molecules by UV spectroscopy and mass spectrometry. It has been successfully applied to identify and quantify a variety of biological and environmental specimens. Despite clear advantages, the dansylation reaction has found very few applications in the study of proteins.
View Article and Find Full Text PDFMicroorganisms
January 2025
Beijing Key Laboratory for Prevention and Control of Infectious Diseases in Livestock and Poultry, In-Stitute of Animal Husbandry and Veterinary Medicine, Beijing Academy of Agriculture and Forestry Sciences, Beijing 100097, China.
Canine Parvovirus (CPV) is a highly contagious virus that causes severe hemorrhagic enteritis and myocarditis, posing a major threat to the life and health of dogs. The molecular mechanism by which VP2, the major capsid protein of CPV, infects host cells and utilizes host cell proteins for self-replication remains poorly understood. In this study, 140 host proteins specifically binding to CPV VP2 protein were identified by immunoprecipitation combined with liquid chromatography-mass spectrometry (LC-MS/MS).
View Article and Find Full Text PDFCancers (Basel)
January 2025
Department of Pathology, Dalhousie University, Halifax, NS B3H 1X5, Canada.
Calreticulin (CRT) is a 46 kDa highly conserved protein initially identified as calregulin, a prominent Ca-binding protein of the endoplasmic reticulum (ER). Subsequent studies have established that CRT functions in the ER's protein folding response and Ca homeostatic mechanisms. An ER retention signal on the carboxyl terminus of CRT suggested that CRT was restricted to the ER.
View Article and Find Full Text PDFInt J Physiol Pathophysiol Pharmacol
December 2024
Gene Expression and Signaling Lab, Department of Zoology, Mahatma Gandhi Central University Motihari Motihari, Bihar 845401, India.
Objective: The Heat Shock Protein 70 (HSP70) family is a highly conserved group of molecular chaperones essential for maintaining cellular homeostasis. These proteins are necessary for protein folding, assembly, and degradation and involve cell recovery from stress conditions. HSP70 proteins are upregulated in response to heat shock, oxidative stress, and pathogenic infections.
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