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Title: Solid-state NMR studies of proteins immobilized on inorganic surfaces

Solid state NMR is the primary tool for studying the quantitative, site-specific structure, orientation, and dynamics of biomineralization proteins under biologically relevant conditions. Two calcium phosphate proteins, statherin and leucine rich amelogenin protein (LRAP), have been studied in depth and have different features, challenging our ability to extract design principles. More recent studies of the significantly larger full-length amelogenin represent a challenging but necessary step to ultimately investigate the full diversity of biomineralization proteins. Interactions of amino acids and silaffin peptide with silica are also being studied, along with qualitative studies of proteins interacting with calcium carbonate. Dipolar recoupling techniques have formed the core of the quantitative studies, yet, the need for isolated spin pairs makes this approach costly and time intensive. The use of multi-dimensional techniques is advancing, methodology which, despite its challenges with these difficult-to-study proteins, will continue to drive future advancements in this area.
  1. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Publication Date:
Report Number(s):
Journal ID: ISSN 0926-2040; 400412000
Grant/Contract Number:
AC05-76RL01830; DE-015347
Accepted Manuscript
Journal Name:
Solid State Nuclear Magnetic Resonance
Additional Journal Information:
Journal Volume: 70; Journal Issue: C; Journal ID: ISSN 0926-2040
Research Org:
Pacific Northwest National Lab. (PNNL), Richland, WA (United States)
Sponsoring Org:
USDOE Office of Science (SC), Biological and Environmental Research (BER) (SC-23)
Country of Publication:
United States
59 BASIC BIOLOGICAL SCIENCES; 37 INORGANIC, ORGANIC, PHYSICAL, AND ANALYTICAL CHEMISTRY; Biomineralization; Immobilized proteins; Dipolar recoupling; Protein structure; Protein dynamics; Protein orientation; Multi-dimensional solid state NMR; Amelogenin; Statherin; Silaffin
OSTI Identifier:
Alternate Identifier(s):
OSTI ID: 1250248