DNA nanomechanics: How proteins deform the double helix

Journal of Chemical Physics

Volumn 130, Issue 13, 2009, Pages

  Becker, Nils B ^a   Everaers, Ralf ^a  

^a Laboratoire de Physique UMR CNRS ENSL   (France)

Author keywords

[No Author keywords available]

Indexed keywords

BIOCHEMISTRY; CONFORMATIONS; PROTEINS;

COMPLEX STRUCTURE; DNA CONFORMATIONS; ELASTIC POTENTIAL; ELASTIC PROPERTIES; EXTERNAL FORCE; FORCES AND TORQUES; HIGH RESOLUTION; NANOMECHANICAL;

DNA;

DEOXYRIBONUCLEASE; DNA; I PPO ENDONUCLEASE; I-PPO ENDONUCLEASE; NANOMATERIAL; TATA BINDING PROTEIN;

ARTICLE; CHEMICAL STRUCTURE; CHEMISTRY; COMPUTER SIMULATION; CONFORMATION; GENETICS; METABOLISM; PROTEIN CONFORMATION; X RAY CRYSTALLOGRAPHY;

COMPUTER SIMULATION; CRYSTALLOGRAPHY, X-RAY; DNA; ENDODEOXYRIBONUCLEASES; MODELS, MOLECULAR; NANOSTRUCTURES; NUCLEIC ACID CONFORMATION; PROTEIN CONFORMATION; TATA-BOX BINDING PROTEIN;

EID: 64549094624     PISSN: 00219606     EISSN: None     Source Type: Journal    
DOI: 10.1063/1.3082157     Document Type: Article

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45. See EPAPS Document No. E-JCPSA6-130-027909 for the supplementary figures and text, and for three-dimensional VRML models of the presented force and torque. For more information on EPAPS, see http://www.aip.org/pubservs/epaps. html
46. By "forces" we always mean "mean forces" in the following.
47. Equation is the equivalent of the standard relation " force=div stress " of continuum elasticity in the present context of a discrete, linear chain.
48. This requirement precludes the use of Euler angles for the orientation Rk.