The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study.

@article{Kraulis1996TheSA,
  title={The serum albumin-binding domain of streptococcal protein G is a three-helical bundle: a heteronuclear NMR study.},
  author={Per J. Kraulis and Per A. Jonasson and Per Ake Nygren and Mathias Uhl{\'e}n and Lena Jendeberg and B. W. Nilsson and Johan K{\"o}rdel},
  journal={FEBS letters},
  year={1996},
  volume={378 2},
  pages={190-4}
}
Streptococcal protein G (SPG) is a cell surface receptor protein with a multiple domain structure containing tandem repeats of serum albumin-binding domains (ABD) and immunoglobulin-binding domains (IgBD). In this paper, we have analysed the fold of ABD. Far-UV circular dichroism analysis of ABD indicates high helical content (56%). Based on an analysis of nuclear magnetic resonance 13C secondary chemical shifts, sequential and short-range NOEs, and a few key nuclear Overhauser effects, we… CONTINUE READING