Structure of Poly(dA)·Poly(dT) is not Identical to the AT Rich Regions of the Single Crystal Structure of CGCGAATTBrCGCG. The Consequence of this to Netropsin Binding to Poly(dA)·Poly(dT)
Author:
Publisher
Informa UK Limited
Subject
Molecular Biology,General Medicine,Structural Biology
Link
http://www.tandfonline.com/doi/pdf/10.1080/10256018808623883
Reference15 articles.
1. Nuclear Overhauser Data and Stereochemical Considerations Suggest that Netropsin Binds Symmetrically Within the Minor Groove of Poly(dA)·Poly(dT), Forming Hydrogen Bonds with Both Strands of the Double Helix
2. Netropsin Specifically Recognizes One of the Two Conformationally Equivalent Strands of Poly (dA)·Poly (dT). One Dimensional NMR Study at 500 MHz Involving NOE Transfer Between Netropsin and DNA Protons
3. Reversible bending and helix geometry in a B-DNA dodecamer: CGCGAATTBrCGCG.
4. Untenability of the Heteronomous DNA Model for Poly(dA) · Poly(dT) in Solution. This DNA Adopts a Right-Handed B-DNA Duplex in Which the Two Strands are Conformationally Equivalent. A 500 MHz NMR Study Using One Dimensional NOE
5. Quantitation of mRNAs during mouse spermatogenesis: protamine-like histone and phosphoglycerate kinase-2 mRNAs increase after meiosis.
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4. Molecular Mechanisms of Specificity in DNA–Antitumour Drug Interactions;Advances in Drug Research;1989
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