Literature DB >> 4463965

Analysis of code relating sequences to conformation in globular prtoeins. Theory and application of expected information.

B Robson.   

Abstract

1. An information theory analysis of the folding of a globular protein is proposed. 2. The folding is seen as a transfer of information between two messages, the primary sequence and the biologically active conformation. 3. It is shown how the information transferred was estimated by inspection of proteins of known primary sequence and conformation. 4. In this estimation, concerted use of subjective (Bayesian) probabilities leads to a more robust approach which can be employed whether the number of proteins of known sequence and conformation is large or small. 5. Further, it is demonstrated that the problem then becomes a very simple algebraic formulation for information estimates. 6. Finally, it is shown how this process of information theory analysis can be reversed to predict the conformation of a protein by using its primary sequence and the above information estimates obtained from other proteins. 7. The present paper provides the theoretical basis for the derivation and application of a stereochemical alphabet (Robson & Pain, 1974a,c), and for an investigation of the effects of residues on the conformations of their neighbours (Robson & Pain, 1974b).

Entities:  

Mesh:

Year:  1974        PMID: 4463965      PMCID: PMC1168191          DOI: 10.1042/bj1410853

Source DB:  PubMed          Journal:  Biochem J        ISSN: 0264-6021            Impact factor:   3.857


  12 in total

1.  The tertiary structure of ribonuclease.

Authors:  C B ANFINSEN
Journal:  Brookhaven Symp Biol       Date:  1962-12

2.  Nucleation, rapid folding, and globular intrachain regions in proteins.

Authors:  D B Wetlaufer
Journal:  Proc Natl Acad Sci U S A       Date:  1973-03       Impact factor: 11.205

3.  Analysis of the code relating sequence to conformation in globular proteins. Development of a stereochemical alphabet on the basis of intra-residue information.

Authors:  B Robson; R H Pain
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

4.  Directional information transfer in protein helices.

Authors:  B Robson; R H Pain
Journal:  Nat New Biol       Date:  1972-07-26

5.  Logical analysis of the mechanism of protein folding. I. Predictions of helices, loops and beta-structures from primary structure.

Authors:  K Nagano
Journal:  J Mol Biol       Date:  1973-04-05       Impact factor: 5.469

Review 6.  Protein denaturation.

Authors:  C Tanford
Journal:  Adv Protein Chem       Date:  1968

Review 7.  The formation of the tertiary structure of proteins.

Authors:  C B Anfinsen
Journal:  Harvey Lect       Date:  1967

8.  Analysis of the code relating sequence to secondary structure in proteins.

Authors:  R H Pain; B Robson
Journal:  Nature       Date:  1970-07-04       Impact factor: 49.962

9.  Statistical analysis of the distribution of amino acid residues among helical and non-helical regions in globular proteins.

Authors:  O B Ptitsyn
Journal:  J Mol Biol       Date:  1969-06-28       Impact factor: 5.469

10.  The influence of short-range interactions on protein conformation. 3. Dipeptide distributions in proteins of known sequence and structure.

Authors:  D Kotelchuck; M Dygert; H A Scheraga
Journal:  Proc Natl Acad Sci U S A       Date:  1969-07       Impact factor: 11.205

View more
  9 in total

1.  A reexamination of correlations of amino acids with particular secondary structures.

Authors:  Sasa N Malkov; Miodrag V Zivković; Milos V Beljanski; Srdan D Stojanović; Snezana D Zarić
Journal:  Protein J       Date:  2009-02       Impact factor: 2.371

2.  A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure.

Authors:  Sasa N Malkov; Miodrag V Zivković; Milos V Beljanski; Michael B Hall; Snezana D Zarić
Journal:  J Mol Model       Date:  2008-05-27       Impact factor: 1.810

3.  Drug discovery using very large numbers of patents: general strategy with extensive use of match and edit operations.

Authors:  Barry Robson; Jin Li; Richard Dettinger; Amanda Peters; Stephen K Boyer
Journal:  J Comput Aided Mol Des       Date:  2011-05-03       Impact factor: 3.686

4.  Predicting protein secondary structure with probabilistic schemata of evolutionarily derived information.

Authors:  M J Thompson; R A Goldstein
Journal:  Protein Sci       Date:  1997-09       Impact factor: 6.725

5.  Analysis of the code relating sequence to conformation in globular proteins. Development of a stereochemical alphabet on the basis of intra-residue information.

Authors:  B Robson; R H Pain
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

6.  Analysis of the code relating sequence to conformation in globular proteins. An informational analysis of the role of the residue in determining the conformation of its neighbours in the primary sequence.

Authors:  B Robson; R H Pain
Journal:  Biochem J       Date:  1974-09       Impact factor: 3.857

7.  A program for prediction of protein secondary structure from nucleotide sequence data: application to histocompatibility antigens.

Authors:  J Novotný; C Auffray
Journal:  Nucleic Acids Res       Date:  1984-01-11       Impact factor: 16.971

8.  Direct demonstration of critical amino acid residues required for cytotoxic T-lymphocyte allorecognition of H-2 class I antigens.

Authors:  E McLaughlin-Taylor; C G Miyada; M McMillan; R B Wallace
Journal:  Proc Natl Acad Sci U S A       Date:  1988-05       Impact factor: 11.205

9.  Refined 1.2 A crystal structure of the complex formed between subtilisin Carlsberg and the inhibitor eglin c. Molecular structure of eglin and its detailed interaction with subtilisin.

Authors:  W Bode; E Papamokos; D Musil; U Seemueller; H Fritz
Journal:  EMBO J       Date:  1986-04       Impact factor: 11.598

  9 in total

北京卡尤迪生物科技股份有限公司 © 2022-2023.