Cracking The Folding Code. Why Do Some Proteins Adopt Partially Folded Conformations, Whereas Other Don't?
Document Type
Article
Publication Date
2002
Digital Object Identifier (DOI)
https://doi.org/10.1016/S0014-5793(02)02359-1
Abstract
Many, but not all, globular proteins have been shown to have compact intermediate state(s) under equilibrium conditions in vitro, giving rise to the question: why do some proteins adopt partially folded conformations, whereas other do not? Here we show that charge to hydrophobicity ratio of a polypeptide chain may represent a key determinant in this respect, as proteins known to form equilibrium partially folded intermediates are specifically localized within a unique region of charge–hydrophobicity space. Thus, the competence of a protein to form equilibrium intermediate(s) may be determined by the bulk content of hydrophobic and charged amino acid residues rather than by the positioning of amino acids within the sequence.
Was this content written or created while at USF?
Yes
Citation / Publisher Attribution
FEBS Letters, v. 514, issue 2-3, p. 181-183
Scholar Commons Citation
Uversky, Vladimir N., "Cracking The Folding Code. Why Do Some Proteins Adopt Partially Folded Conformations, Whereas Other Don't?" (2002). Molecular Medicine Faculty Publications. 687.
https://digitalcommons.usf.edu/mme_facpub/687
