@article{TEXTUAL,
      recid = {13469},
      author = {Murty, Rohan and Bera, Mrinal K. and Walton, Ian M. and  Whetzel, Christina and Prausnitz, Mark R. and Walton,  Krista S.},
      title = {Interrogating Encapsulated Protein Structure within  Metal–Organic Frameworks at Elevated Temperature},
      journal = {Journal of the American Chemical Society},
      address = {2023-03-24},
      number = {TEXTUAL},
      abstract = {Encapsulating biomacromolecules within metal-organic  frameworks (MOFs) can confer thermostability to entrapped  guests. It has been hypothesized that the confinement of  guest molecules within a rigid MOF scaffold results in  heightened stability of the guests, but no direct evidence  of this mechanism has been shown. Here, we present a novel  analytical method using small-angle X-ray scattering (SAXS)  to solve the structure of bovine serum albumin (BSA) while  encapsulated within two zeolitic imidazolate frameworks  (ZIF-67 and ZIF-8). Our approach comprises subtracting the  scaled SAXS spectrum of the ZIF from that of the  biocomposite BSA@ZIF to determine the radius of gyration of  encapsulated BSA through Guinier, Kratky, and pair distance  distribution function analyses. While native BSA exposed to  70 °C became denatured, in situ SAXS analysis showed that  encapsulated BSA retained its size and folded state at 70  °C when encapsulated within a ZIF scaffold, suggesting  that entrapment within MOF cavities inhibited protein  unfolding and thus denaturation. This method of SAXS  analysis not only provides insight into biomolecular  stabilization in MOFs but may also offer a new approach to  study the structure of other conformationally labile  molecules in rigid matrices.},
      url = {http://knowledge.uchicago.edu/record/13469},
}