Bovine zeta-crystallin has the ability to bind with different DNAs. Initially, this protein was named regulatory factor 36 (Kang et al., 1985), but it has been shown to be an ocular lens zeta-crystallin (JΓΆrnvall et al., 1993), which is considered an enzyme-crystallin (Rodakanaki et al., 1989). The
Molecular mechanical studies on left- and right-handed B-DNA
β Scribed by N. Pattabiraman; Shashidhar N. Rao; Kevin Scott; Robert Langridge; Peter A. Kollman
- Publisher
- Wiley (John Wiley & Sons)
- Year
- 1987
- Tongue
- English
- Weight
- 672 KB
- Volume
- 26
- Category
- Article
- ISSN
- 0006-3525
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β¦ Synopsis
Molecular mechanical simulations on base-paired deoxyhexanucleoside phosphates, (dAdT), .
(dAdT),, (dTdA), . (dTdA),, (dGdC), . (dGdC),, and (dCdG), . (dCdG),, have been carried out to assess their energetic stabilities in left-and right-handed forms. These hexamers have also been simulated with alternating sugar-puckering profiles with the combinations (purine : C2'endo-pyrimidine : C3'-endo) and (purine : C3'-e&pyrimidine C2'-endo). The right-handed models have been found to be the energetically most stable structures and the left-handed structures are significantly destabilized. This instability has been rationalized in terms of competition between stabilizing stacking interactions on one hand, and distortions in the bond angles and torsion angles in the sugar-phosphate backbone on the other.
π SIMILAR VOLUMES
The Lifson-Roig and Zimm-Bragg theories of t,he helix-coil transition ill polypeptides are generalized to include both right-and left-handed a-helical states. The partition functions for these more general theories are formulated in terms of the parameters u, V R , V L , W R , and W L for t,he gener
Previous ab initio computations revealed that the conformational building unit of the Ε½ . right-handed helix f y54Π, f y45Π is not an energy minimum on two-Ε½ Γ 4 . dimensional-type Ramachandran potential energy surfaces E s E , . Theoretical investigations were performed on several single-amino-acid