Allostery without Conformational Change: A Native Mass Spectrometry Perspective.

ABSTRACT: Native electrospray ionization-mass spectrometry (nESI-MS) enables studies of intact proteins, protein complexes, and protein-ligand complexes. Variable temperature (vT)-nESI-MS, where the temperature of the solution contained in the ESI emitter can be varied from 2 to 100 °C, adds new capabilities for dissecting the thermodynamics for protein-ligand binding. Here, vT-nESI-MS and ion mobility spectrometry (IMS) are used to compare the effects of temperature and nESI buffers on nucleotide (ADP) binding for the GroEL single ring mutant (SR1). Temperature-dependent shifts for average charge states (Z_avg) and rotationally averaged collision cross sections (CCS) for both apo- and nucleotide-bound SR1 complexes (SR1-ADP_n, n = 1-7) indicate that nESI buf

SUBMITTER: Sun HM 

PROVIDER: S-EPMC12400411 | biostudies-literature | 2025 Aug

REPOSITORIES: biostudies-literature