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PMID: 6265870 Published · ppublish English Journal Article

Temperature mediated variation of DNA secondary structure in (A.T) clusters; evidence by use of the oligopeptide netropsin as a structural probe.

Nucleic acids research ·Vol. 9 ·No. 10 ·1981-05-25 ·Pages 2335-49

Reinert KE, Geller D, Stutter E

Abstract

The titration viscometric investigation of the multi-mode interaction of netropsin (Nt) with (A.T) clusters of NaDNA12 and NH4DNA10 has been extended to different temperatures. The position of two boundaries on the r-scale (r= [Nt]bound/[DNA-P]) with increasing temperature steadily (rI/II) or more abruptly (rO/I) shifts to lower values. For the most (A.T) rich Nt-binding sites of modes (O), (I) and (II) this observation suggests the existence of an equilibrium between different DNA secondary structures with a different translation per base pair. The mode specific changes delta L1Nt of DNA contour length as induced by one Nt molecule proved to be almost independent of temperature. Concomitant stiffening effects increase with decreasing temperature, contrary to initial expectation. Conformational variability of (A.T) clusters may represent an essential feature in specific or selective DNA-protein interaction.

MeSH Terms
Chemical Phenomena Chemistry Clostridium perfringens DNA DNA, Bacterial Guanidines Netropsin Nucleic Acid Conformation Temperature Viscosity
Chemicals
DNA, Bacterial Guanidines Netropsin DNA
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Reinert K E
Geller D
Stutter E
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66 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/9.10.2335
Published
1981-05-25
Pages
2335-49
Language
English
Region
England
NLM ID
0411011
PMCID
PMC326849
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/9.10.2335 PMC Full Text View journal details
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