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Confinement and crowding effects on tryptophan synthase α 2 β 2 complex
Author(s) -
Pioselli Barbara,
Bettati Stefano,
Mozzarelli Andrea
Publication year - 2005
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/j.febslet.2005.03.011
Subject(s) - tryptophan synthase , nanoporous , chemistry , ficoll , tryptophan , dextran , catalysis , biophysics , macromolecular crowding , atp synthase , molecule , in vivo , stereochemistry , biochemistry , enzyme , in vitro , organic chemistry , biology , amino acid , peripheral blood mononuclear cell , macromolecule , microbiology and biotechnology
Biological molecules experience in vivo a highly crowded environment. The investigation of the functional properties of the tryptophan synthase α 2 β 2 complex either entrapped in wet nanoporous silica gels or in the presence of the crowding agents dextran 70 and ficoll 70 indicates that the rates of the conformational transitions associated to catalysis and regulation are reduced, and an open and less catalytically active conformation is stabilized.