Modelling protein three-dimensional structure using tritium planigraphy.
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.
N.N. Semenov Institute of Chemical Physics, Academy of Sciences, Moscow, USSR.
A
A
Gedrovich
A
A
Shishkov
V
V
Goldanskii
L
L
Baratova
N
N
Grebenshchikov
A
A
Efimov
D000596:Amino Acids / Q000737:chemistry; D000818:Animals; D002851:Chromatography, High Pressure Liquid; D005399:Fishes / Q000378:metabolism; D006868:Hydrolysis; D008956:Models, Chemical; D010320:Parvalbumins / Q000737:chemistry; D011487:Protein Conformation; D011506:Proteins / Q000737:chemistry*; D012697:Serine Endopeptidases; D014961:X-Ray Diffraction
D000596:Amino Acids; D010320:Parvalbumins; D011506:Proteins; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase