1H and 15N chemical shift assignments of a carboxy-terminal functional domain of the bacteriophage P22 scaffolding protein

Academic Article

Abstract

  • The 15N-labeled C-terminal functional domain of the bacteriophage P22 scaffolding protein was expressed and purified. The NMR chemical-shift assignments of this functional domain were determined. An analysis of the chemical shift indices for the α-protons indicates that the N-terminal half of this protein is unstructured whereas the C-terminal half is defined by a helix-loop-helix motif. Copyright © 1999 John Wiley & Sons, Ltd.
  • Published In

    Author List

  • Sun Y; Krishna NR
  • Start Page

  • 602
  • End Page

  • 604
  • Volume

  • 37
  • Issue

  • 8