Protein structure and interactions elucidated with in-cell NMR for different cell cycle phases and in 3D human tissue models.

ABSTRACT: Most of our knowledge of protein structure and function originates from experiments performed with purified proteins resuspended in dilute, buffered solutions. However, most proteins function in crowded intracellular environments with complex compositions. Significant efforts have been made to develop tools to study proteins in their native cellular settings. Among these tools, in-cell NMR spectroscopy has been the sole technique for characterizing proteins in the intracellular space of living cells at atomic resolution and physiological temperature. Nevertheless, due to technological constraints, in-cell NMR studies have been limited to asynchronous single-cell suspensions, precluding obtaining information on protein behavior in different cellular states. In this study, we present a metho

SUBMITTER: Rynes J 

PROVIDER: S-EPMC11806009 | biostudies-literature | 2025 Feb

REPOSITORIES: biostudies-literature