FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W1983727572> ?p ?o ?g. }

• W1983727572 abstract "Introduction Life rests on a web of molecular recognition;1,2 the folding of proteins, the hybridization of nucleic acids, the recognition of signaling molecules by receptors, and the interaction of enzymes with substrates and cofactors all require molecular recognition. Molecular recognition is based on shape-sensitive, noncovalent interactions between molecules or fragments of molecules.3-6 The energetics of molecular recognition can reflect van der Waals, hydrophobic, hydrogen bonding, and electrostatic interactions; all include both enthalpic and entropic contributions. The role of van der Waals interactions in molecular recognition in aqueous ionic solutions is well understood; they contribute to molecular recognition primarily through unfavorable steric interactions that exclude ligands with noncomplementary shapes from the recognition site of the protein. Hydrophobic interactions, although still a challenge to describe theoretically, can be estimated empirically from the observed partitioning of model compounds between aqueous and hydrocarbon solvents.7 Hydrogen bonds are best thought of as a specific type of localized electrostatic interaction;8 they are also well understood qualitatively. Although much theoretical and experimental work has gone into understanding the electrostatic properties and interactions that are central to biomolecular recognition events9-11(for a review, see ref 12), it has been difficult to measure and evaluate these interactions quantitatively. One of the central electrostatic properties of proteins is their charge, which is determined, in principle, by the sequence and structure of the protein and the properties of the solvent. Although one can measure the isoelectric point of proteins (the value of pH at which the charge of the protein is zero), there has been no general way of measuring the charge of a protein at other values of pH or as a function of the properties of the solution. Previous attempts to estimate the effects of electrostatic interactions on the affinities of proteins for ligands have focused on the use of site-directed mutagenesis.10,13-15 This technique, although powerful, is labor intensive, and the number of mutated sites that can be explored practically is limited. In this Account we describe the use of protein charge ladders in combination with capillary electrophoresis (CE) as a new biophysical tool with which to measure the electrostatic properties and interactions that are central to biomolecular recognition events involving proteins. The partial acetylation of amino groups on a protein changes the charge of the protein and generates a protein charge ladder, that is, a series of derivatives of a protein differing in values of charge but having similar coefficients of friction. The distribution of protein derivatives group, in terms of their values of electrophoretic mobility, into the “rungs” of a charge ladder, which appear in CE as a set of peaks; each successive peak in the charge ladder differs incrementally in the number of acetylated amino groups (Scheme 1). Charge ladders in combination with CE have been used to estimate the charge of the unmodified protein16 and the values of pKa of individual ionizable groups.17,18 Charge ladders in combination with affinity capillary electrophoresis (ACE) make it possible to quantify the contributions of electrostatics to the free energies of binding of charged ligands to proteins.19 Although we have developed this approach primarily using charge ladders of bovine carbonic anhydrase II (BCA II, EC 4.2.1.1.) as a model system (Figure 1),16,19 we have demonstrated the formation of charge ladders with a range of other proteins and biological molecules.17,18,20-23" @default.
• W1983727572 created "2016-06-24" @default.
• W1983727572 creator A5007785866 @default.
• W1983727572 creator A5023517707 @default.
• W1983727572 creator A5074428718 @default.
• W1983727572 creator A5078636171 @default.
• W1983727572 date "2010-06-20" @default.
• W1983727572 modified "2023-09-25" @default.
• W1983727572 title "ChemInform Abstract: Protein Charge Ladders, Capillary Electrophoresis, and the Role of Electrostatics in Biomolecular Recognition" @default.
• W1983727572 cites W2950689153 @default.
• W1983727572 doi "https://doi.org/10.1002/chin.199834329" @default.
• W1983727572 hasPublicationYear "2010" @default.
• W1983727572 type Work @default.
• W1983727572 sameAs 1983727572 @default.
• W1983727572 citedByCount "0" @default.
• W1983727572 crossrefType "journal-article" @default.
• W1983727572 hasAuthorship W1983727572A5007785866 @default.
• W1983727572 hasAuthorship W1983727572A5023517707 @default.
• W1983727572 hasAuthorship W1983727572A5074428718 @default.
• W1983727572 hasAuthorship W1983727572A5078636171 @default.
• W1983727572 hasConcept C112887158 @default.
• W1983727572 hasConcept C117626034 @default.
• W1983727572 hasConcept C119599485 @default.
• W1983727572 hasConcept C126061179 @default.
• W1983727572 hasConcept C127413603 @default.
• W1983727572 hasConcept C137277065 @default.
• W1983727572 hasConcept C145148216 @default.
• W1983727572 hasConcept C147597530 @default.
• W1983727572 hasConcept C147789679 @default.
• W1983727572 hasConcept C148093993 @default.
• W1983727572 hasConcept C159467904 @default.
• W1983727572 hasConcept C178790620 @default.
• W1983727572 hasConcept C179303850 @default.
• W1983727572 hasConcept C185592680 @default.
• W1983727572 hasConcept C201194858 @default.
• W1983727572 hasConcept C2182769 @default.
• W1983727572 hasConcept C32909587 @default.
• W1983727572 hasConcept C71240020 @default.
• W1983727572 hasConcept C87716614 @default.
• W1983727572 hasConcept C90260826 @default.
• W1983727572 hasConceptScore W1983727572C112887158 @default.
• W1983727572 hasConceptScore W1983727572C117626034 @default.
• W1983727572 hasConceptScore W1983727572C119599485 @default.
• W1983727572 hasConceptScore W1983727572C126061179 @default.
• W1983727572 hasConceptScore W1983727572C127413603 @default.
• W1983727572 hasConceptScore W1983727572C137277065 @default.
• W1983727572 hasConceptScore W1983727572C145148216 @default.
• W1983727572 hasConceptScore W1983727572C147597530 @default.
• W1983727572 hasConceptScore W1983727572C147789679 @default.
• W1983727572 hasConceptScore W1983727572C148093993 @default.
• W1983727572 hasConceptScore W1983727572C159467904 @default.
• W1983727572 hasConceptScore W1983727572C178790620 @default.
• W1983727572 hasConceptScore W1983727572C179303850 @default.
• W1983727572 hasConceptScore W1983727572C185592680 @default.
• W1983727572 hasConceptScore W1983727572C201194858 @default.
• W1983727572 hasConceptScore W1983727572C2182769 @default.
• W1983727572 hasConceptScore W1983727572C32909587 @default.
• W1983727572 hasConceptScore W1983727572C71240020 @default.
• W1983727572 hasConceptScore W1983727572C87716614 @default.
• W1983727572 hasConceptScore W1983727572C90260826 @default.
• W1983727572 hasLocation W19837275721 @default.
• W1983727572 hasOpenAccess W1983727572 @default.
• W1983727572 hasPrimaryLocation W19837275721 @default.
• W1983727572 hasRelatedWork W1486433989 @default.
• W1983727572 hasRelatedWork W1541258411 @default.
• W1983727572 hasRelatedWork W1581338119 @default.
• W1983727572 hasRelatedWork W1903660448 @default.
• W1983727572 hasRelatedWork W1925045229 @default.
• W1983727572 hasRelatedWork W1964337480 @default.
• W1983727572 hasRelatedWork W1991665852 @default.
• W1983727572 hasRelatedWork W2030732279 @default.
• W1983727572 hasRelatedWork W2078159738 @default.
• W1983727572 hasRelatedWork W2103977803 @default.
• W1983727572 hasRelatedWork W2106334513 @default.
• W1983727572 hasRelatedWork W2108765440 @default.
• W1983727572 hasRelatedWork W2140230121 @default.
• W1983727572 hasRelatedWork W2541680013 @default.
• W1983727572 hasRelatedWork W2766682498 @default.
• W1983727572 hasRelatedWork W2950689153 @default.
• W1983727572 hasRelatedWork W2998189912 @default.
• W1983727572 hasRelatedWork W3119734745 @default.
• W1983727572 hasRelatedWork W3129011282 @default.
• W1983727572 hasRelatedWork W3208438050 @default.
• W1983727572 isParatext "false" @default.
• W1983727572 isRetracted "false" @default.
• W1983727572 magId "1983727572" @default.
• W1983727572 workType "article" @default.