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Folding kinetics of mammalian ribonucleases
Author(s) -
Lang Kurt,
Wrba Alex,
Krebs Herbert,
Schmid Franz X.,
Beintema Jaap J.
Publication year - 1986
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 - 10.1016/0014-5793(86)81401-6
Subject(s) - kinetics , chemistry , folding (dsp implementation) , protein folding , biophysics , computational biology , biochemistry , biology , physics , engineering , quantum mechanics , electrical engineering
The folding kinetics of seven different pancreatic ribonucleases are compared both under native conditions and within the unfolding transition. In general, the folding kinetics of these proteins are similar despite numerous amino acid substitutions. Ribonucleases with 4–6 proline residues show 80% slow‐folding species. For three ribonucleases with 7 prolines this number increases to 90%. Porcine ribonuclease with a unique Pro 114‐Pro 115 sequence folds significantly slower than other ribonucleases which do not show this sequence.