Folding minimal sequences

The lower bound for sequence complexity of globular proteins

Pedro Romero, Zoran Obradovic, A. Dunker

Research output: Contribution to journalArticle

64 Citations (Scopus)

Abstract

Alphabet size and informational entropy, two formal measures of sequence complexity, are herein applied to two prior studies on the folding of minimal proteins. These measures show a designed four-helix bundle to be unlike its natural counterparts but rather more like a coiled-coil dimer. Segments from a simplified sarc homology 3 domain and more than 2 000 000 segments from globular proteins both have lower bounds for alphabet size of 10 and for entropy near 2.9. These values are therefore suggested to be necessary and sufficient for folding into globular proteins having both rigid side chain packing and biological function. Copyright (C) 1999 Federation of European Biochemical Societies.

Original languageEnglish (US)
Pages (from-to)363-367
Number of pages5
JournalFEBS Letters
Volume462
Issue number3
DOIs
StatePublished - Dec 3 1999
Externally publishedYes

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Protein Folding
Entropy
Proteins
Dimers

Keywords

  • Alphabet size
  • Complexity
  • Entropy
  • Minimal sequence
  • Protein folding

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Folding minimal sequences : The lower bound for sequence complexity of globular proteins. / Romero, Pedro; Obradovic, Zoran; Dunker, A.

In: FEBS Letters, Vol. 462, No. 3, 03.12.1999, p. 363-367.

Research output: Contribution to journalArticle

Romero, Pedro ; Obradovic, Zoran ; Dunker, A. / Folding minimal sequences : The lower bound for sequence complexity of globular proteins. In: FEBS Letters. 1999 ; Vol. 462, No. 3. pp. 363-367.
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