Dielectric study of the interaction between DNA and an oligopeptide (lysine-tyrosinelysine).

Rix-Montel, M.A.; Grassi, H.; Vasilescu, D.

doi:10.1093/nar/3.4.1001

Cited by 5 publications

(2 citation statements)

References 13 publications

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“…(c) Ion release can be considered to be the thermodynamic driving force that shifts the reaction equilibrium toward complex formation as the electrolyte concentration is reduced. In the interaction of the tripeptide lys-tyr-lys with double-stranded DNA, Rix-Montel, Grassi & Vasilescu (1976) demonstrated the occurrence of counterion release directly by conductivity measurements. There are parallels, as noted in sections 1 and 2 of this review, between the role of water release in driving the interactions of non-polar regions of biopolymers and the role of ion release in driving the interactions of highly charged biopolyelectrolytes.…”

Section: Protein-nucleic Acid Interactionsmentioning

confidence: 99%

Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity

1978

Quart. Rev. Biophys.

1,653

1,047

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The purpose of this review is to examine the various effects of low- molecular-weight electrolytes on the associations and interactions of proteins and nucleic acids. Our primary interest is in general electrostatic effects, rather than chemical effects (specific interactions) of particular ions (e.g. transition metals, protons). We consider those interactions in which a variation in salt concentration has a significant effect on the macromolecular equilibrium, and analyse the effects of salt in these situations in terms of (i) direct participation of ions in the biopolymer reaction, (ii) Debye—Hückel screening by salt ions of the charge interactions on the biopolymers, and (iii) the reduction in water activity brought about at high salt concentrations.

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Section: Protein-nucleic Acid Interactionsmentioning

confidence: 99%

Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity

1978

Quart. Rev. Biophys.

1,653

1,047

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“…However, the thermodynamics of such systems are complex (Overman et al, 1988;Overman, L. B., and Lohman, T. M., manuscript in preparation), and interpretations of such studies can often be facilitated by comparative studies of simpler model systems. The study of small oligopeptides and their interactions with ss and duplex nucleic acids has proven useful for such purposes ( (Latt & Sober, 1967a,b;Helene & Dimicoli, 1972;Brun et al, 1975;Lohman et al, 1980;Helene & Maurizot, 1981;Helene & Lancelot, 1982;Rix-Montel et al, 1976; Montenay-Garestier et al, 1982). Although there have been systematic thermodynamic studies of the nonspecific binding of positively charged peptides to duplex RNA and DNA (Latt & Sober, 1967a,b;Lohman et al, 1980), such studies with ss nucleic acids have been lacking.…”

mentioning

confidence: 99%

Thermodynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition

Mascotti¹,

Lohman²

1993

Biochemistry

102

121

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We have examined the thermodynamics of binding of a series of oligolysines (net charge z = +2 to +10) containing one, two, or three tryptophans to several single-stranded (ss) homo-polynucleotides [poly(A), poly(C), poly(I), poly(dU), poly(dT)] and duplex (ds) DNA in order to investigate the effects of peptide charge, tryptophan content, and polynucleotide base and sugar type. Equilibrium association constants, Kobs, were measured as a function of monovalent salt concentration (KCH3CO2) and temperature by monitoring the quenching of the peptide tryptophan fluorescence upon interaction with the polynucleotides, from which the dependence of delta G(o)obs, delta H(o)obs, and delta S(o)obs on [KCH3CO2] was obtained. As observed previously with poly(U) [Mascotti, D.P., & Lohman, T.M. (1992) Biochemistry 31, 8932], the dependence of delta G(o)obs on [K+] for peptide binding to each polynucleotide is entirely entropic in origin (i.e., delta H(o)obs is independent of [K+]), consistent with the conclusion that Kobs increases with decreasing salt concentration due to the favorable increase in entropy resulting from the displacement of bound cations (K+) from the nucleic acid upon formation of the complex. For each ss polynucleotide, we find that significantly less than one potassium ion is released thermodynamically per net positive peptide charge, as determined from the value of delta log Kobs/delta log [K+]. Interestingly, (-delta log Kobs/delta log [K+])/z decreases with increasing peptide charge for poly(A), poly(C), and poly(dT), contrary to the behavior observed with poly(U) and ds-DNA, which may reflect a significant release of bound water upon formation of peptide complexes with these ss homo-polynucleotides or an increased binding of K+ to the ss polynucleotide with increasing [K+]. Alternatively, there may be conformational differences between the bound states of oligolysines of low charge, relative to oligolysines of higher charge. However, in all cases, peptides with z < +4 display different thermodynamics of binding than peptides with z > +4. The presence of tryptophan (Trp) within these peptides does not influence the salt dependence of Kobs for binding to poly(A), poly(C), or poly(dT). However, the Trp content of the peptide does contribute significantly to the thermodynamics of these interactions: Trp interactions result in a favorable contribution to delta H(o)obs, but an unfavorable contribution to delta S(o)obs, with little effect on delta G(o)obs due to entropy-enthalpy compensations. Oligolysines containing Trp also display a small, but significant, dependence of Kobs on base composition, with Kobs decreasing in the order poly(I) >> poly(dT) approximately poly(U) approximately poly(A) >> poly(C).

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A study of the interaction tyrosine and DNA using voltammetry and spectroscopy methods

Fotouhi

Tabatabaee

2014

Spectrochimica Acta Part A: Molecular and Biomolecular Spectros

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Dielectric study of the interaction between DNA and an oligopeptide (lysine-tyrosinelysine).

Cited by 5 publications

References 13 publications

Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity

Thermodynamic analysis of ion effects on the binding and conformational equilibria of proteins and nucleic acids: the roles of ion association or release, screening, and ion effects on water activity

Thermodynamics of single-stranded RNA and DNA interactions with oligolysines containing tryptophan. Effects of base composition

A study of the interaction tyrosine and DNA using voltammetry and spectroscopy methods

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