Macrochelate formation in monomeric metal ion complexes of nucleoside 5'-triphosphates and the promotion of stacking by metal ions. Comparison of the self-association of purine and pyrimidine 5'-triphosphates using proton nuclear magnetic resonance

1981 ◽  
Vol 103 (2) ◽  
pp. 247-260 ◽  
Author(s):  
Kurt H. Scheller ◽  
Fritz Hofstetter ◽  
Paul R. Mitchell ◽  
Bernhard Prijs ◽  
Helmut Sigel
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Ions ◽  
Metal Ion ◽  
The Self ◽  
Proton Nuclear Magnetic Resonance ◽  
Metal Ion Complexes ◽  
Self Association ◽  
Nuclear Magnetic

scholarly journals Visible absorption and proton nuclear magnetic resonance studies on the self-association of doxorubicin in aqueous solution.

1991 ◽  
Vol 39 (4) ◽  
pp. 1009-1012 ◽  
Author(s):  
Eiji HAYAKAWA ◽  
Kunitoshi FURUYA ◽  
Hideo UENO ◽  
Tokuyuki KURODA ◽  
Masuo MORIYAMA ◽  
...  
Keyword(s):  
Aqueous Solution ◽  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
The Self ◽  
Proton Nuclear Magnetic Resonance ◽  
Visible Absorption ◽  
Magnetic Resonance Studies ◽  
Self Association ◽  
Nuclear Magnetic

Phosphorus nuclear magnetic resonance studies of phosphoglucomutase and its metal ion complexes

1977 ◽  
Vol 184 (2) ◽  
pp. 453-463 ◽  
Author(s):  
W.J. Ray ◽  
A.S. Mildvan ◽  
John B. Grutzner
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Ion ◽  
Metal Ion Complexes ◽  
Magnetic Resonance Studies ◽  
Nuclear Magnetic

A cooperative conformational change in duplex DNA induced by Zn2+ and other divalent metal ions

1993 ◽  
Vol 71 (3-4) ◽  
pp. 162-168 ◽  
Author(s):  
Jeremy S. Lee ◽  
Laura J. P. Latimer ◽  
R. Stephen Reid
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Ions ◽  
Conformational Change ◽  
Divalent Metal ◽  
Proton Nuclear Magnetic Resonance ◽  
Duplex Dna ◽  
Divalent Metal Ions ◽  
Base Pairs ◽  
Nuclear Magnetic

Zn2+ and some other divalent metal ions bind to duplex DNA at pHs above 8 and cause a conformational change. This new structure does not bind ethidium, allowing the development of a rapid fluorescence assay. All duplex DNAs, regardless of sequence or G∙C content, can form this structure. The rate of formation shows a strong dependence on temperature, pH, and Zn2+ concentration; at 20 °C, 1 mM Zn2+, and pH 8.6 the dismutation is half complete in 30 min. Addition of EDTA causes rapid reversion to 'B' DNA, showing that the new conformation retains two strands that are antiparallel. Unlike the ultraviolet or circular dichroism spectra, the nuclear magnetic resonance spectrum was informative since the imino protons of both A∙T and G∙C base pairs are lost upon addition of a stoichiometric amount of Zn2+. The pitch of the helix was estimated from gel electrophoresis of circular DNAs in the presence of Zn2+ and it contains at least 5% fewer base pairs per turn than 'B' DNA. The transformation is cooperative and shows hysteresis, suggesting that this is a distinct structure and not simply a minor variant of 'B' DNA. It is proposed to call this new structure 'M' DNA because of the intimate involvement of metal ions.Key words: DNA conformation, cooperative transition, ethidium binding, divalent metal ions, proton nuclear magnetic resonance.

Hydrophobic Interactions in Solution: A Nuclear Magnetic Resonance Approach

2000 ◽  
Vol 214 (7) ◽  
Author(s):  
A. Sacco
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Hydrophobic Interactions ◽  
The Self ◽  
Aqueous Mixtures ◽  
Organic Components ◽  
Self Association ◽  
Small Hydrophobic ◽  
Nuclear Magnetic

The self-association behaviour of relatively small hydrophobic organic components in aqueous mixtures has been investigated by the application of an NMR technique. The association A

NMR spectroscopic studies of I = 1/2 metal ions in biological systems

1998 ◽  
Vol 76 (2-3) ◽  
pp. 223-234 ◽  
Author(s):  
Gülin Öz ◽  
Dean L Pountney ◽  
Ian M Armitage
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Ions ◽  
Metal Binding ◽  
Metal Ion ◽  
Structural Features ◽  
Spectroscopic Studies ◽  
Mercury Resistance ◽  
New Information ◽  
Nuclear Magnetic

This article reviews the use of nuclear magnetic resonance methods of spin 1/2 metal nuclei to probe the metal binding site(s) in a variety of metalloproteins. The majority of the studies have involved native Zn(II) and Ca(II) metalloproteins where there has been isostructural substitution of these metal ions with the I = 1/2 111/113Cd(II) ion. Also included are recent studies that have utilized the 109Ag(I) ion to probe Cu(I) sites in yeast metallothionein and 199Hg(II) as a probe of the metal binding sites in mercury resistance proteins. Pertinent aspects for the optimal execution of these experiments along with the procedures for the metal substitution reactions are discussed together with the presentation of a 113Cd chemical shift correlation map with ligand type and coordination number. Specific examples of protein systems studied using the 111/113Cd and 109Ag nuclei include the metallothionein superfamily of Zn(II)- and Cu(I)-binding proteins from mammalian, invertebrate, and yeast systems. In addition to the structural features revealed by these metal ion nuclear magnetic resonance studies, important new information is frequently provided about the dynamics at the active-site metal ion. In an effort for completeness, other less frequently used spin 1/2 metal nuclei are mentioned.Key words: metallothionein, 111/113Cd, 199Hg, 109Ag, 57Fe, 205Tl, 195Pt, 207Pb, 119Sn, nuclear magnetic resonance.

Metal ion and drug binding to proteolytic fragments of calmodulin: proteolytic cadmium-113 and proton nuclear magnetic resonance studies

Biochemistry ◽  
1984 ◽  
Vol 23 (8) ◽  
pp. 1862-1870 ◽  
Author(s):  
Eva Thulin ◽  
Anita Andersson ◽  
Torbjoern Drakenberg ◽  
Sture Forsen ◽  
Hans J. Vogel
Keyword(s):  
Nuclear Magnetic Resonance ◽  
Magnetic Resonance ◽  
Metal Ion ◽  
Drug Binding ◽  
Proton Nuclear Magnetic Resonance ◽  
Magnetic Resonance Studies ◽  
Nuclear Magnetic
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