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Literature DB >> 6547339

Hydropathic anti-complementarity of amino acids based on the genetic code.

Abstract

An interesting pattern in the genetic code has been discovered. Codons for hydrophilic and hydrophobic amino acids on one strand of DNA are complemented by codons for hydrophobic and hydrophilic amino acids on the other DNA strand, respectively. The average tendency of codons for "uncharged" (slightly hydrophilic) amino acids is to be complemented by codons for "uncharged" amino acids.

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Year: 1984 PMID： 6547339 DOI： 10.1016/0006-291x(84)90707-1

Source DB: PubMed Journal: Biochem Biophys Res Commun ISSN： 0006-291X Impact factor: 3.575

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Cited

45 in total

Review 1. Directed molecular evolution.

Authors: L F Harris; M R Sullivan; D L Hatfield
Journal: Orig Life Evol Biosph Date: 1999-08 Impact factor: 1.950

2. Anti-platelet autoantibodies from ITP patients recognize an epitope in GPIIb/IIIa deduced by complementary hydropathy.

Authors: S J De Souza; J Sabbaga; E D'Amico; R Pasqualini; R Brentani
Journal: Immunology Date: 1992-01 Impact factor: 7.397

3. Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

Authors: J J Calvete; K Mann; M V Alvarez; M M López; J González-Rodríguez
Journal: Biochem J Date: 1992-03-01 Impact factor: 3.857

4. Affinity capture of [Arg8]vasopressin-receptor complex using immobilized antisense peptide.

Authors: F X Lu; N Aiyar; I Chaiken
Journal: Proc Natl Acad Sci U S A Date: 1991-05-01 Impact factor: 11.205

5. Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Localization of monoclonal antibody epitopes and the putative fibrinogen-binding sites.

Authors: J J Calvete; J Arias; M V Alvarez; M M Lopez; A Henschen; J González-Rodríguez
Journal: Biochem J Date: 1991-03-01 Impact factor: 3.857

Hydropathic anti-complementarity of amino acids based on the genetic code.

Review 1. Directed molecular evolution.

2. Anti-platelet autoantibodies from ITP patients recognize an epitope in GPIIb/IIIa deduced by complementary hydropathy.

3. Proteolytic dissection of the isolated platelet fibrinogen receptor, integrin GPIIb/IIIa. Localization of GPIIb and GPIIIa sequences putatively involved in the subunit interface and in intrasubunit and intrachain contacts.

4. Affinity capture of [Arg8]vasopressin-receptor complex using immobilized antisense peptide.

5. Further studies on the topography of the N-terminal region of human platelet glycoprotein IIIa. Localization of monoclonal antibody epitopes and the putative fibrinogen-binding sites.

6. Molecular Recognition Theory of the complementary (antisense) peptide interactions.

7. Binding of peptides that are specified by complementary RNAs.

8. ANCA patients have T cells responsive to complementary PR-3 antigen.

9. Structural study of binding of flagellin by Toll-like receptor 5.

10. Open reading frames in the antisense strands of genes coding for glycolytic enzymes in Saccharomyces cerevisiae.