Literature DB >> 1915152

Modelling protein three-dimensional structure using tritium planigraphy.

A Gedrovich1, A Shishkov, V Goldanskii, L Baratova, N Grebenshchikov, A Efimov.   

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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Year:  1991        PMID： 1915152     DOI： 10.1007/bf00183316

Source DB:  PubMed          Journal:  Eur Biophys J        ISSN： 0175-7571            Impact factor:   1.733


  18 in total

1.  A model of myoglobin self-organization.

Authors:  O B Ptitsyn; A A Rashin
Journal:  Biophys Chem       Date:  1975-02       Impact factor: 2.352

2.  The primary structure of the parvalbumin II of pike (Esox lucius).

Authors:  C Gerday
Journal:  Eur J Biochem       Date:  1976-11-01

3.  Refinement of the structure of carp muscle calcium-binding parvalbumin by model building and difference Fourier analysis.

Authors:  P C Moews; R H Kretsinger
Journal:  J Mol Biol       Date:  1975-01-15       Impact factor: 5.469

Review 4.  Empirical predictions of protein conformation.

Authors:  P Y Chou; G D Fasman
Journal:  Annu Rev Biochem       Date:  1978       Impact factor: 23.643

5.  Algorithms for prediction of alpha-helical and beta-structural regions in globular proteins.

Authors:  V I Lim
Journal:  J Mol Biol       Date:  1974-10-05       Impact factor: 5.469

6.  Carp muscle calcium-binding protein. II. Structure determination and general description.

Authors:  R H Kretsinger; C E Nockolds
Journal:  J Biol Chem       Date:  1973-05-10       Impact factor: 5.157

7.  Are there proteins between the ribosomal subunits? Hot tritium bombardment experiments.

Authors:  M M Yusupov; A S Spirin
Journal:  FEBS Lett       Date:  1986-03-03       Impact factor: 4.124

8.  [Study of the three-dimensional structure of proteins by means of tritium labeling. II. Intramolecular distribution of tritium in the N-terminal part of myoglobin and the tertiary structure of protein].

Authors:  V I Gol'danskiĭ; Iu M Rumiantsev; A V Shishkov; L A Baratova; L P Belianova
Journal:  Mol Biol (Mosk)       Date:  1982 May-Jun

9.  The use of thermally activated tritium atoms for structural-biological investigations: the topography of the TMV protein-accessible surface of the virus.

Authors:  V I Goldanskii; I A Kashirin; A V Shishkov; L A Baratova; N I Grebenshchikov
Journal:  J Mol Biol       Date:  1988-06-05       Impact factor: 5.469

10.  The relation between the divergence of sequence and structure in proteins.

Authors:  C Chothia; A M Lesk
Journal:  EMBO J       Date:  1986-04       Impact factor: 11.598
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  2 in total

1.  Flavin-dependent alcohol oxidase from the yeast Pichia pinus. Spatial localization of the coenzyme FAD in the protein structure: hot-tritium bombardment and ESR experiments.

Authors:  A Z Averbakh; N D Pekel; V I Seredenko; A V Kulikov; R I Gvozdev; I P Rudakova
Journal:  Biochem J       Date:  1995-09-01       Impact factor: 3.857

2.  Tritium planigraphy: from the accessible surface to the spatial structure of a protein.

Authors:  E N Bogacheva; V I Gol'danskii; A V Shishkov; A V Galkin; L A Baratova
Journal:  Proc Natl Acad Sci U S A       Date:  1998-03-17       Impact factor: 11.205
  2 in total

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