biostudies-literatureHuang CTMinistry of Science and Technology, TaiwanAcademia Sinica375-386https://www.ebi.ac.uk/biostudies/studies/S-EPMC10539794biostudies-literatureUnknown2(1)Trigger factor (TF) is a highly conserved multi-domain molecular chaperone that exerts its chaperone activity at the ribosomal tunnel exit from which newly synthesized nascent chains emerge. TF also displays promiscuous substrate binding for a large number of cytosolic proteins independent of ribosome binding. We asked how TF recognizes a variety of substrates while existing in a monomer-dimer equilibrium. Paramagnetic nuclear magnetic resonance (NMR) and electron spin resonance (ESR) spectroscopy were used to show that dimeric TF displays a high degree of structural polymorphism in solution. A series of peptides has been generated to quantify their TF binding affinities in relation with their sequence compositions. The results confirmed a previous predication that TF preferentially binds Magnetic resonance (Gottingen, Germany)Structural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.PMC10539794102-2113-M-001-017-MY2NA100-2113-M-001-031-MY2Hsu SDLai YCChen SYHuang CTHo MRChiang YWfalseStructural polymorphism and substrate promiscuity of a ribosome-associated molecular chaperone.Trigger factor (TF) is a highly conserved multi-domain molecular chaperone that exerts its chaperone activity at the ribosomal tunnel exit from which newly synthesized nascent chains emerge. TF also displays promiscuous substrate binding for a large number of cytosolic proteins independent of ribosome binding. We asked how TF recognizes a variety of substrates while existing in a monomer-dimer equilibrium. Paramagnetic nuclear magnetic resonance (NMR) and electron spin resonance (ESR) spectroscopy were used to show that dimeric TF displays a high degree of structural polymorphism in solution. A series of peptides has been generated to quantify their TF binding affinities in relation with their sequence compositions. The results confirmed a previous predication that TF preferentially binds 2021-01-01T00:00:00Z20212026-05-28T21:34:36.858Z2025-04-20T01:32:10.578ZS-EPMC105397943790475910.5194/mr-2-375-2021