Investigation of protein folding

Uneven distribution of point mutations along polypeptide chains

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

The distribution of point mutations accepted by natural selection in the amino acid sequences of 16 cytochrome-C, 7 lysozyme, 15 myoglobin, 10 ribonuclease, 12 short neurotoxin, 16 plant ferredoxin and 6 bacterial ferredoxin molecules have been investigated. The number of point mutations shows an increasing tendency from the NH2-terminus towards the COON-terminus of these proteins or at least within their structural domains. Our results suggest that the continuous folding of polypeptide chain during biosynthesis may play an important role in the formation of globular protein structure.

Original languageEnglish
Pages (from-to)247-258
Number of pages12
JournalJournal of Theoretical Biology
Volume81
Issue number2
DOIs
Publication statusPublished - Nov 21 1979

Fingerprint

Protein folding
Ferredoxins
ferredoxins
Protein Folding
protein folding
Polypeptides
point mutation
Point Mutation
polypeptides
Mutation
Proteins
Peptides
Natural Selection
neurotoxins
ribonucleases
myoglobin
Myoglobin
Genetic Selection
Biosynthesis
Neurotoxins

ASJC Scopus subject areas

  • Agricultural and Biological Sciences(all)

Cite this

Investigation of protein folding : Uneven distribution of point mutations along polypeptide chains. / Simon, I.

In: Journal of Theoretical Biology, Vol. 81, No. 2, 21.11.1979, p. 247-258.

Research output: Contribution to journalArticle

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