ISSN:
1432-1017
Keywords:
Pike parvalbumin
;
Tritium planigraphy
;
Three-dimensional modelling
Source:
Springer Online Journal Archives 1860-2000
Topics:
Biology
,
Physics
Notes:
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.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/BF00183316
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