Journal of Biomolecular NMR

, Volume 18, Issue 3, pp 207–216 | Cite as

Pressure alters electronic orbital overlap in hydrogen bonds

  • Hua Li
  • Hiroaki Yamada
  • Kazuyuki Akasaka
  • Angela M. Gronenborn


Pressure-induced changes in 3hJNC′ scalar couplings through hydrogen bonds were investigated in the immunoglobulin binding domain of streptococcal protein G. 1H, 15N and 13C triple-resonance NMR spectroscopy coupled with the on-line high pressure cell technique was used to monitor 3hJNC′ scalar couplings at 30 and 2000 bar in uniformly labeled 15N and 13C protein isotopes. Both increased and decreased 3hJNC′ scalar couplings were observed at high pressure. No correlation with secondary structure was apparent. The difference in coupling constants as well as pressure-induced chemical shift data suggests a compaction of the helix ends and an increase of the helix pitch at its center in response to pressure. Our data provides the first direct evidence that the electronic orbital overlap in protein backbone hydrogen bonds is altered by pressure.

GB1 H-bonds J coupling pressure proteins 


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Copyright information

© Kluwer Academic Publishers 2000

Authors and Affiliations

  • Hua Li
    • 1
  • Hiroaki Yamada
    • 2
  • Kazuyuki Akasaka
    • 3
    • 2
  • Angela M. Gronenborn
    • 4
  1. 1.Graduate School of Science and TechnologyKobe UniversityJapan
  2. 2.Faculty of ScienceKobe UniversityJapan
  3. 3.Graduate School of Science and TechnologyJapan
  4. 4.Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney DiseasesNational Institutes of HealthBethesdaU.S.A.

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