Solid state NMR studies of molecular recognition at protein-mineral interfaces

Gil Goobes, Patrick S. Stayton, Gary P. Drobny

Research output: Contribution to journalReview articlepeer-review

48 Scopus citations


The use of nuclear magnetic resonance (NMR) to analyze the structure and crystal recognition mechanisms of an salivary protein model system is described. NMR dipolar coupling measurements are used to obtain high resolution structures for proteins in microcrystalline form, for proteins oriented in lipid bilayers and lipid vesicles and for proteins in fibrillar form. NMR pulse techniques are also capable of reporting the structures of surface-adsorbed proteins and protein-crystal interactions in molecular detail. The investigations of protein mineral interactions are frequently conducted with techniques that characterize the macroscopic behavior of proteins in the presence of mineral crystals. Equilibrium properties are derived via adsorption isotherm measurements, where data are usually analyzed by assuming a simple Langmuir model of protein adsorption onto the crystal faces.

Original languageEnglish
Pages (from-to)71-85
Number of pages15
JournalProgress in Nuclear Magnetic Resonance Spectroscopy
Issue number2-3
StatePublished - 30 May 2007
Externally publishedYes

Bibliographical note

Funding Information:
This work was supported by the NSF (Grants EEC 9529161 and DMR 0110505) and the National Dental Institute (Grant DE-12554). In addition, many people contributed to the statherin NMR/structural modelling project. NMR studies of the structure of the N-terminus of statherin as well as studies of the structures of peptides derived from the N-terminus were conducted by J.R. Long and W.J. Shaw. NMR studies of statherin side chain interactions with HAP were conducted by V. Raghunathan, J.M. Gibson, and J.M. Popham. Samples of multiply labelled statherin were provided by R. Goobes. NMR experiments on multiply labelled statherin samples were performed by G. Goobes. The ROSETTA program was developed in the laboratory of D. Baker. O. Schueler-Furman produced ROSETTA-based models of statherin. We thank Nicholas Breen for proof-reading the manuscript and for helpful discussions.


  • Adsorbed protein
  • Biomineralization
  • Magic angle spinning
  • Recoupling
  • Structure determination


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