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The role of proline in the prevention of aggregation during protein folding in vitro
Author(s) -
Kumat T. K. S.,
Samuel D.,
Jayaraman G.,
Srimathi T.,
Yu C.
Publication year - 1998
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216549800204032
Subject(s) - in vitro , chemistry , proline , biophysics , folding (dsp implementation) , protein folding , protein aggregation , biochemistry , biology , amino acid , engineering , electrical engineering
Proline effectively inhibits protein aggregation during the refolding of bovine carbonic anhydrase. Other osmolytes used such as glyeine and ethylene glycol fail to exhibit the ‘aggregation‐blockade’ role shown by proline. Results of viscosity and ANS fluorescence (1‐anilino‐8‐naphthalene sulphonic acid) experiments suggest that proline at high concentrations forms an ordered supramolecular assembly. Based on these results, it is proposed that proline behaves as a protein folding chaperone due to the formation of an ordered, amphipathic supramolecular assembly. To our knowledge, this is the first report wherein proline is proposed as a protein folding aid.