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Structural determinants of mini‐protein stability
Author(s) -
Polticelli Fabio,
RaybaudiMassilia Gabriella,
Ascenzi Paolo
Publication year - 2001
Publication title -
biochemistry and molecular biology education
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.34
H-Index - 39
eISSN - 1539-3429
pISSN - 1470-8175
DOI - 10.1111/j.1539-3429.2001.tb00057.x
Subject(s) - context (archaeology) , protein folding , folding (dsp implementation) , computational biology , protein stability , protein tertiary structure , structural biology , protein structure , chemistry , biology , biochemistry , engineering , paleontology , electrical engineering
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. © 2001 IUBMB. Published by Elsevier Science Ltd. All rights reserved.