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Affinity, Specificity, and Cooperativity of DNA Binding by Bacterial Gene Regulatory Proteins
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SYSNO ASEP 0553488 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Affinity, Specificity, and Cooperativity of DNA Binding by Bacterial Gene Regulatory Proteins Author(s) Carey, Jannette (MBU-M) ORCID Article number 562 Source Title International Journal of Molecular Sciences. - : MDPI
Roč. 23, č. 1 (2022)Number of pages 16 s. Language eng - English Country CH - Switzerland 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 Subject RIV EE - Microbiology, Virology OECD category Microbiology Method of publishing Open access Institutional support MBU-M - RVO:61388971 UT WOS 000741453200001 EID SCOPUS 85122384956 DOI 10.3390/ijms23010562 Annotation 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. Workplace Institute of Microbiology Contact Eliška Spurná, eliska.spurna@biomed.cas.cz, Tel.: 241 062 231 Year of Publishing 2023 Electronic address https://www.mdpi.com/1422-0067/23/1/562
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