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Cracking the folding code. Why do some proteins adopt partially folded conformations, whereas other don't?
Author(s) -
Uversky Vladimir N
Publication year - 2002
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(02)02359-1
Subject(s) - globular protein , protein folding , chemistry , amino acid , lattice protein , folding (dsp implementation) , crystallography , polypeptide chain , biophysics , peptide sequence , protein structure , sequence (biology) , biochemistry , biology , gene , electrical engineering , engineering
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.