Literature DB >> 1807631

Patterns in protein primary sequences: classification, display and analysis.

P N Saurugger1, B A Metfessel.   

Abstract

The protein folding code, which is contained in the amino acid chain of a protein, has so far eluded elucidation. However, patterns of hydrophobic residues have previously been identified which show a specificity towards certain secondary structural elements. We are developing an analysis toolkit to find, visualize, and analyze patterns in primary sequences. Preliminary results show that there exist patterns in primary sequences which are useful for predicting the structural class of amino acid chains, performing especially well for the all-alpha helix and all-beta sheet classes.

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Year:  1991        PMID: 1807631      PMCID: PMC2247562     

Source DB:  PubMed          Journal:  Proc Annu Symp Comput Appl Med Care        ISSN: 0195-4210


  13 in total

1.  Some factors in the interpretation of protein denaturation.

Authors:  W KAUZMANN
Journal:  Adv Protein Chem       Date:  1959

2.  Improved sensitivity of biological sequence database searches.

Authors:  D L Brutlag; J P Dautricourt; S Maulik; J Relph
Journal:  Comput Appl Biosci       Date:  1990-07

3.  Predicting the secondary structure of globular proteins using neural network models.

Authors:  N Qian; T J Sejnowski
Journal:  J Mol Biol       Date:  1988-08-20       Impact factor: 5.469

4.  The use of various properties of amino acids in color and monochrome dot-matrix analyses for protein homologies.

Authors:  A H Reisner; C A Bucholtz
Journal:  Comput Appl Biosci       Date:  1988-08

5.  Hydrophobic cluster analysis: an efficient new way to compare and analyse amino acid sequences.

Authors:  C Gaboriaud; V Bissery; T Benchetrit; J P Mornon
Journal:  FEBS Lett       Date:  1987-11-16       Impact factor: 4.124

6.  Structural principles of the globular organization of protein chains. A stereochemical theory of globular protein secondary structure.

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

7.  The folding type of a protein is relevant to the amino acid composition.

Authors:  H Nakashima; K Nishikawa; T Ooi
Journal:  J Biochem       Date:  1986-01       Impact factor: 3.387

8.  An analysis of incorrectly folded protein models. Implications for structure predictions.

Authors:  J Novotný; R Bruccoleri; M Karplus
Journal:  J Mol Biol       Date:  1984-08-25       Impact factor: 5.469

9.  How good are predictions of protein secondary structure?

Authors:  W Kabsch; C Sander
Journal:  FEBS Lett       Date:  1983-05-08       Impact factor: 4.124

10.  Polypeptide chain folding through a highly helical intermediate as a general principle of globular protein structure formation.

Authors:  V I Lim
Journal:  FEBS Lett       Date:  1978-05-01       Impact factor: 4.124

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