Simulation of the shape of chaperonins using the small-angle x-ray scattering curves and torus form factor

Journal Article · Mon Aug 15 00:00:00 EDT 2011 · Journal of Experimental and Theoretical Physics

DOI:https://doi.org/10.1134/S1063776111060112· OSTI ID:22028033

Naletova, I N ^[1]; Kurochkina, L P ^[2]

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1. Moscow State University, Belozerskii Institute of Molecular Biology and Bioorganic Chemistry (Russian Federation)
2. Russian Academy of Sciences, Shemyakin-Ovchinnikov Institute of Bioorganic Chemistry (Russian Federation)

The inverse scattering problem has been solved for protein complexes whose surfaces can be described by a set of the simplest doubly connected surfaces in the uniform approximation (a scattering potential inside the molecule is a constant). Solutions of two proteins-well-known GroEL bacterial chaperonin and poor-studied bacteriophage chaperonin, which is a product of 146 gene (gp146)-were taken for the experiment. The shapes of protein complexes have been efficiently reconstructed from the experimental scattering curves. The shell method, the method of the rotation of amino acid sequences with the use of the form factor of an amino acid, and the method of seeking the model parameters of a protein complex with the preliminarily obtained form factor of the model have been used to reconstruct the shape of these particles.

• OSTI ID: 22028033
• Journal Information: Journal of Experimental and Theoretical Physics, Vol. 113, Issue 2; Other Information: Copyright (c) 2011 Pleiades Publishing, Ltd.; Country of input: International Atomic Energy Agency (IAEA); ISSN 1063-7761
• Country of Publication: United States
• Language: English

Related Subjects

75 CONDENSED MATTER PHYSICS
SUPERCONDUCTIVITY AND SUPERFLUIDITY
60 APPLIED LIFE SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
APPROXIMATIONS
BACTERIOPHAGES
COMPUTERIZED SIMULATION
FORM FACTORS
GENES
HEAT-SHOCK PROTEINS
INVERSE SCATTERING PROBLEM
MATHEMATICAL SOLUTIONS
MOLECULES
POTENTIALS
ROTATION
SMALL ANGLE SCATTERING
SURFACES
X-RAY DIFFRACTION