Structural determinants of mini-protein stability

Fabio Polticelli, Gabriella Raybaudi-Massilia, Paolo Ascenzi

Research output: Contribution to journalArticle

5 Citations (Scopus)

Abstract

Mini-proteins can be defined as polypeptides shorter than 40-50 residues which nevertheless exhibit a well defined tertiary structure. Mini-proteins represent simple and useful model systems to study the structural determinants of protein folding and stability and to illustrate such principles within biochemistry and molecular biology educational context. Here, strategies adopted by different classes of mini-proteins to attain family-characteristic, well-ordered, three-dimensional structures are reviewed.

Original languageEnglish
Pages (from-to)16-20
Number of pages5
JournalBiochemistry and Molecular Biology Education
Volume29
Issue number1
DOIs
Publication statusPublished - 2001

Fingerprint

Protein Stability
Protein folding
Biochemistry
Proteins
Molecular biology
Protein Folding
Molecular Biology
Peptides

Keywords

  • Mini-proteins
  • Protein redesign
  • Protein stability

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology

Cite this

Structural determinants of mini-protein stability. / Polticelli, Fabio; Raybaudi-Massilia, Gabriella; Ascenzi, Paolo.

In: Biochemistry and Molecular Biology Education, Vol. 29, No. 1, 2001, p. 16-20.

Research output: Contribution to journalArticle

Polticelli, Fabio ; Raybaudi-Massilia, Gabriella ; Ascenzi, Paolo. / Structural determinants of mini-protein stability. In: Biochemistry and Molecular Biology Education. 2001 ; Vol. 29, No. 1. pp. 16-20.
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