This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


1d81

From Proteopedia

(Difference between revisions)
Jump to: navigation, search

OCA (Talk | contribs)
(New page: 200px<br /><applet load="1d81" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d81, resolution 2.500&Aring;" /> '''THE CONFORMATIONAL ...)
Next diff →

Revision as of 00:35, 25 November 2007


1d81, resolution 2.500Å

Drag the structure with the mouse to rotate

THE CONFORMATIONAL VARIABILITY OF AN ADENOSINE. INOSINE BASE-PAIR IN A SYNTHETIC DNA DODECAMER

Overview

A crystal structure analysis of the synthetic deoxydodecamer, d(CGCAAATTIGCG) which contains two adenosine.inosine (A.I) mispairs has, revealed that, in this sequence, the A.I base-pairs adopt a A(anti).I(syn), configuration. The refinement converged at R = 0.158 for 2004 reflections, with F greater than or equal to 2 sigma(F) in the range 7.0-2.5A for a, model consisting of the DNA duplex and 71 water molecules. A notable, feature of the structure is the presence of an almost complete spine of, hydration spanning the minor groove of the whole of the (AAATTI)2 core, region of the duplex. pH-dependent ultraviolet melting studies have, suggested that the base-pair observed in the crystal structure is, in, fact, a protonated AH+ (anti).I(syn) species and that the A.I base-pairs, in the sequence studied display the same conformational variability as A.G, mispairs in the sequence d(CGCAAATTGGCG). The AH+(anti).I(syn) base-pair, predominates below pH 6.5 and an A(anti).I(anti) mispair is the major, species present between pH 6.5 and 8.0. The protonated base-pairs are held, together by two hydrogen bonds one between N6(A) and O6(I) and the other, between N1(A) and N7(I). This second hydrogen bond is a direct result of, the protonation of the N1 of adenosine. The ultraviolet melting studies, indicate that the A(anti).I(anti) base-pair is more stable than the, A(anti).G(anti) base-pair but that the AH+(anti).I(syn) base pair is less, stable than its AH+(anti).G(syn) analogue. Possible reasons for this, observation are discussed.

About this Structure

1D81 is a Protein complex structure of sequences from [1]. Full crystallographic information is available from OCA.

Reference

The conformational variability of an adenosine.inosine base-pair in a synthetic DNA dodecamer., Leonard GA, Booth ED, Hunter WN, Brown T, Nucleic Acids Res. 1992 Sep 25;20(18):4753-9. PMID:1408788

Page seeded by OCA on Sun Nov 25 02:42:35 2007

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools