Affinity, Specificity, and Cooperativity of DNA Binding by Bacterial Gene Regulatory Proteins

0553488 - MBÚ 2023 RIV CH eng J - Journal Article
Carey, Jannette
Affinity, Specificity, and Cooperativity of DNA Binding by Bacterial Gene Regulatory Proteins.
International Journal of Molecular Sciences. Roč. 23, č. 1 (2022), č. článku 562. E-ISSN 1422-0067
Institutional support: RVO:61388971
Keywords : escherichia-coli * ligand-binding * trp-repressor * thermodynamics * conformations * constraints * mutants * domain * biological constraints * host-guest chemistry * pre-organization * cryptic thermodynamic factors * protein folding coupled to ligand binding * gestalt properties of proteins * drug design
OECD category: Microbiology
Impact factor: 5.6, year: 2022
Method of publishing: Open access
https://www.mdpi.com/1422-0067/23/1/562

Nearly all of biology depends on interactions between molecules: proteins with small molecules, proteins with other proteins, nucleic acids with small molecules, and nucleic acids with proteins that regulate gene expression, our concern in this Special Issue. All those kinds of interactions, and others, constitute the vast majority of biology at the molecular level. An understanding of those interactions requires that we quantify them to learn how they interact: How strongly? With which partners? How-and how well-are different partners distinguished? This review addresses the evolution of our current understanding of the molecular origins of affinity and specificity in regulatory protein-DNA interactions, and suggests that both these properties can be modulated by cooperativity.
Permanent Link: http://hdl.handle.net/11104/0331807