Literature DB >> 1449603

Correlation between the compact regions predicted by the average distance map (ADM) and the biologically active sites in atrial natriuretic peptide.

T Kikuchi1.   

Abstract

The prediction of the short-range compact regions of human atrial natriuretic peptide (alpha-hANP), one of the biologically active peptides, has been made by means of the Average Distance Map(ADM). We found out that the location of the predicted short-range compact regions is consistent with the structural units determined by the NMR analysis (Kobayashi et al., 1988). Furthermore, the short-range compact regions correspond well to the biologically active areas of atriopeptin (103-125)-amide (which is homologous peptide to alpha-hANP), detected by the glycine substitution technique (Konishi et al., 1987). The results suggest that a predicted short-range compact region can be regarded as a possible active site in a biologically active peptide.

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Year:  1992        PMID: 1449603     DOI: 10.1007/bf01025036

Source DB:  PubMed          Journal:  J Protein Chem        ISSN: 0277-8033


  4 in total

1.  Prediction of probable pathways of folding in globular proteins.

Authors:  T Kikuchi; G Némethy; H A Scheraga
Journal:  J Protein Chem       Date:  1988-08

2.  Purification and complete amino acid sequence of alpha-human atrial natriuretic polypeptide (alpha-hANP).

Authors:  K Kangawa; H Matsuo
Journal:  Biochem Biophys Res Commun       Date:  1984-01-13       Impact factor: 3.575

3.  The differences in conformation between alpha-human atrial natriuretic polypeptide, alpha-hANP, and its derivative, Met(O)-alpha-hANP, in solution.

Authors:  S Koyama; Y Kobayashi; T Ohkubo; Y Kyogoku; A Sato; M Kobayashi; N Go
Journal:  Protein Eng       Date:  1990-04

4.  The conformation of alpha-human atrial natriuretic polypeptide in solution.

Authors:  Y Kobayashi; T Ohkubo; Y Kyogoku; S Koyama; M Kobayashi; N Go
Journal:  J Biochem       Date:  1988-09       Impact factor: 3.387

  4 in total
  1 in total

1.  Prediction of location of active sites in biologically active peptides.

Authors:  T Kikuchi
Journal:  J Protein Chem       Date:  1996-08
  1 in total

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