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Modelling protein three-dimensional structure using tritium planigraphy.

A Gedrovich·A Shishkov·V Goldanskii·L Baratova·N Grebenshchikov·A Efimov
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Abstract

We propose the use of data on the topography of the label-accessible surface of a protein molecule obtained by the method of tritium planigraphy as a criterion for choosing the optimal intermediate arrangements of alpha-helices in globular proteins so as to model their three-dimensional structures. This approach has been used for modelling the three-dimensional structure of parvalbumin III from pike. The proposed model has been compared with high-resolution X-ray structural data for a related protein, paryvalbumin from carp. The possibilities and limitations of this approach are discussed.

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Amino AcidsAnimalsChromatography, High Pressure LiquidFishesHydrolysisModels, ChemicalParvalbuminsProtein ConformationProteinsSerine EndopeptidasesX-Ray DiffractionJournal Article

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A Gedrovich, A Shishkov, V Goldanskii, L Baratova, N Grebenshchikov, A Efimov. 1991. Modelling protein three-dimensional structure using tritium planigraphy.. https://doi.org/10.1007/bf00183316

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