Theory of the influence of oligonucleotide chain conformation on double helix stability

Biopolymers ◽  
1971 ◽  
Vol 10 (10) ◽  
pp. 1809-1827 ◽  
Author(s):  
C. Delisi ◽  
D. M. Crothers
2003 ◽  
Vol 20 (6) ◽  
pp. 801-809 ◽  
Author(s):  
Elena N. Galyuk ◽  
Dmitri Y. Lando ◽  
Valentina P. Egorova ◽  
Hwa Dai ◽  
Yury M. Dosin

Biopolymers ◽  
1981 ◽  
Vol 20 (12) ◽  
pp. 2509-2531 ◽  
Author(s):  
Jeffrey W. Nelson ◽  
Francis H. Martin ◽  
Ignacio Tinoco

1989 ◽  
Vol 111 (11) ◽  
pp. 4123-4125 ◽  
Author(s):  
Carla J. Van Garderen ◽  
Leo P. A. Van Houte ◽  
Hans Van den Elst ◽  
Jacques H. Van Boom ◽  
Jan Reedijk

Author(s):  
D.P. Bazett-Jones ◽  
F.P. Ottensmeyer

Dark field electron microscopy has been used for the study of the structure of individual macromolecules with a resolution to at least the 5Å level. The use of this technique has been extended to the investigation of structure of interacting molecules, particularly the interaction between DNA and fish protamine, a class of basic nuclear proteins of molecular weight 4,000 daltons.Protamine, which is synthesized during spermatogenesis, binds to chromatin, displaces the somatic histones and wraps up the DNA to fit into the small volume of the sperm head. It has been proposed that protamine, existing as an extended polypeptide, winds around the minor groove of the DNA double helix, with protamine's positively-charged arginines lining up with the negatively-charged phosphates of DNA. However, viewing protamine as an extended protein is inconsistent with the results obtained in our laboratory.


Author(s):  
Mark Hannibal ◽  
Jacob Varkey ◽  
Michael Beer

Workman and Langmore have recently proposed a procedure for isolating particular chromatin fragments. The method requires restriction endonuclease cutting of the chromatin and a probe, their digestion with two exonucleases which leave complimentary single strand termini and low temperature hybridization of these. We here report simple electron microscopic monitoring of the four reactions involved.Our test material was ϕX-174 RF DNA which is cut once by restriction endonuclease Xho I. The conversion of circles to linear molecules was followed in Kleinschmidt spreads. Plate I shows a circular and a linear DNA molecule. The rate of cutting is shown in Figure 1.After completion of the endonuclease cutting, one portion of the DNA was treated with exonuclease III, an enzyme known to digest the 3' terminals of double helical DNA. Aliquots when examined in the electron microscope reveal a decreasing length of double helix and increasing bushes at the ends.


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