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- M K Pirtskhalava, V V Poroĭkov, V G Tumanian
- Bioorganicheskaia khimiia
- 1983

Conformational analysis of immunoglobulin G3 (IgG3) hinge region repeating part was performed. In approximation of backbone regular conformations for the case of C2 symmetry (the symmetry axis is perpendicular to S-S bridges and passes through their midpoint) on the basis of total analysis of ring geometry possibilities and estimation of steric conditions,… (More)

- V. G. Tumanyan, Yu. A. Neyfack, M. K. Pirtskhalava, J. H. Männik
- Journal of Biosciences
- 2007

On the basis of complete scanning through conformational space of dihedral angles, twelve structural genera were obtained. Subsequent energy minimization within these genera yielded a limited set of duplexes with stacking: right-handed B-form (Wilkins type), B2-form (Watson and Crick type) and left-handed Ll-form (Sasisekharan type) and the new L2-form. In… (More)

- M K Pirtskhalava, V V Poroĭkov, V G Tumanian
- Molekuliarnaia biologiia
- 1985

The method of possible conformations calculations for cyclic structures, formed by two (or more) identical parallel polypeptide chains, closed by cross bridges has been elaborated. The algorithm is necessary for rigorous conformational analysis of cyclic regions in immunoglobulin, fibronectin and myosin.

- B M Vishnepol'skiĭ, M K Pirtskhalava
- Molekuliarnaia biologiia
- 1997

- B M Vishnepol'skiĭ, M K Pirtskhalava
- Molekuliarnaia biologiia
- 1990

The realization of two models for Zn-finger structure--DNA-binding domain was estimated by taking into account the geometric and energetic requirements of polypeptide chain folding. The following structures were taken as models: antiparallel beta-structure and helix-turn-helix motif. The latter hasn't been considered earlier as the possible structure for… (More)

- M K Pirtskhalava, N G Esipova, V G Tumanian, M M Zaalishvili
- Biofizika
- 1991

Local conformational states of fibrous fragments of myosin molecules from striated muscle have been studied. Analysis of the amino acid sequences of the rat embryonic skeletal muscle myosin heavy chain and the nematode myosin heavy chain have been performed with the aim to estimate the influence of electrostatic interactions on secondary structure stability… (More)

- B M Vishnepol'skiĭ, M K Pirtskhalava
- Molekuliarnaia biologiia
- 1993

Distribution of nonpolar residues in the hydrophobic core (a and d positions) of fibrillar proteins in the form of alpha-helical coiled-coil has been studied. It was shown that concentration of large nonpolar residues (Phe, Trp) in a and d positions would not stabilize this structure; amino acids with smaller nonpolar side chains (Leu, Ala, Val, Ile, Met)… (More)

- M K Pirtskhalava, M M Zaalishvili
- Biofizika
- 1998

The investigations of the molecular bases of muscle contraction posed the following question: in which part of the myosin cross-bridge, the head or the fibrillar part, the conformational changes occur that lead to the generation of force. The paper deals with experimental and theoretical data that are in some way related to the solution of this question.… (More)

- B M Vishnepol'skiĭ, M K Pirtskhalava
- Molekuliarnaia biologiia
- 1993

To estimate the role of nonbonded interactions in the folding of the hydrophobic core of a two-stranded parallel alpha-helical coiled-coil, a conformational analysis was carried out for the model fragment: [formula: see text] with a 2-fold symmetry axis running between the parallel helices, where X denotes nonpolar residues Ala, Leu, Val, Ile, Met, Phe,… (More)

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