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PMID: 933174 Published · ppublish English Journal Article

Evolutionary processes and evolutionary noise at the molecular level. I. Functional density in proteins.

Journal of molecular evolution ·Vol. 7 ·No. 3 ·1976-04-09 ·Pages 167-83

Zuckerkandl E

Abstract

The distinction between molecular sites that mainly carry out general functions and sites committed to specific functions is analyzed, notably in terms of different evolutionary variabilities. Functional density is defined as the proportion of sites involved in specific functions. Weighted functional density, by representing the relative variability at specific-function sites is to some extent a measure of the specificity of molecular interactions. The relationship between general- and specific-function sites on the one hand the covarions of Fitch on the other is discussed. The functional "degeneracy" of amino acids is described as increasing the interdependence of general functions. It is predicted that proteins tht do not possess general-function sites besides their specific-function sites tend to "freeze" their primary structure, according to an evolutionary process that is an autocatalytic function of the decrease in site variability. This limits the use of weighted functional density as an indicator of the overall degree of interaction specificity of a protein to values that are not close to unity.

MeSH Terms
Amino Acid Sequence Biological Evolution Genetic Variation Origin of Life Protein Conformation Proteins/metabolism
Chemicals
Proteins
Authors & Affiliations
1 authors, click to expand affiliations / ORCID
Zuckerkandl E
References (10)
10 references, click to expand
  1. [Amino acids sequence. Nucleotide sequence and evolution].
    Bull Soc Chim Biol (Paris). 1967;49(6):577-607 PMID: 4861891
  2. Evolution of ribonuclease in relation to polypeptide folding mechanisms.
    Nature. 1972 Dec 15;240(5381):395-8 PMID: 4564316
  3. The biochemistry and function of beta-lactamase (penicillinase).
    Adv Enzymol Relat Areas Mol Biol. 1966;28:237-323 PMID: 5334062
  4. Rate of change of concomitantly variable codons.
    J Mol Evol. 1971;1(1):84-96 PMID: 4377447
  5. An improved method for determining codon variability in a gene and its application to the rate of fixation of mutations in evolution.
    Biochem Genet. 1970 Oct;4(5):579-93 PMID: 5489762
  6. Does the fixation of neutral mutations form a significant part of observed evolution in proteins?
    Brookhaven Symp Biol. 1972;23:186-216 PMID: 4625828
  7. Aspects of molecular evolution.
    Annu Rev Genet. 1973;7:343-80 PMID: 4593308
  8. The appearance of new structures and functions in proteins during evolution.
    J Mol Evol. 1975 Dec 31;7(1):1-57 PMID: 765485
  9. Darwinian evolution in the genealogy of haemoglobin.
    Nature. 1975 Feb 20;253(5493):603-8 PMID: 1089897
  10. Evolutionary variability in hemoglobins.
    Hamatol Bluttransfus. 1972;10:199-215 PMID: 4667990
Article Info
Journal
Journal of molecular evolution
Abbr.
J Mol Evol
ISSN
0022-2844
Published
1976-04-09
Pages
167-83
Language
English
Region
Germany
NLM ID
0360051
Subset
IM
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