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

Journal Article · · Solid State Nuclear Magnetic Resonance
 [1]
  1. Pacific Northwest National Lab. (PNNL), Richland, WA (United States)

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.

Research Organization:
Pacific Northwest National Laboratory (PNNL), Richland, WA (United States)
Sponsoring Organization:
USDOE Office of Science (SC), Biological and Environmental Research (BER)
Grant/Contract Number:
AC05-76RL01830; DE-015347
OSTI ID:
1222894
Alternate ID(s):
OSTI ID: 1250248
Report Number(s):
PNNL-SA-104618; 400412000
Journal Information:
Solid State Nuclear Magnetic Resonance, Vol. 70, Issue C; ISSN 0926-2040
Publisher:
ElsevierCopyright Statement
Country of Publication:
United States
Language:
English
Citation Metrics:
Cited by: 20 works
Citation information provided by
Web of Science

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