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Draws Implementation


EMSL Project ID
12696

Abstract

Naturally occurring biominerals possess an impressive array of strength, order and nanostructure. These properties are the direct result of protein controlled nucleation and templated mineral growth. To develop engineered implants, materials and coatings that mimic the strength, order and specificity of those found in nature, the protein-surface interface must be understood. Few techniques exist that investigate the protein-surface interface on a molecular level. Solid state NMR (SSNMR) has recently been demonstrated to be a valuable tool in providing quantitative, site specific structure and orientation information for surface immobilized proteins under various conditions (e.g. hydrated and pH controlled). Dipolar recoupling sequences are particularly useful in characterizing protein structure. One pulse sequence, DRAWS, is uniquely suited to determining protein structure, but its hardware requirements exceed typical "off the shelf" SSNMR probes and the "windowless" nature of the pulse sequence requires special care for proper implementation. We propose to build a probe capable of performing the DRAWS experiment and execute the DRAWS pulse sequence on our spectrometers. Once enabled, we have two biomaterials systems we will investigate with DRAWS. The first is a peptide that can exist in a -sheet and an -helix conformation and will be studied on two or more surfaces to investigate the ability of the surface to induce secondary structure. The second system focuses on an antimicrobial cationic peptide. Its mechanism of action is not known but interactions with negatively charged membranes are believed to be crucial for its activity. Better understanding this mechanism of action could lead to the development of "universal drugs" and the natural prevention of infections. These membrane-interacting peptides are also useful models for large membrane proteins.

Project Details

Project type
Capability Research
Start Date
2005-04-11
End Date
2007-10-01
Status
Closed

Team

Principal Investigator

Wendy Shaw
Institution
Pacific Northwest National Laboratory

Team Members

Joseph Ford
Institution
Pacific Northwest National Laboratory

Sarah Burton
Institution
Environmental Molecular Sciences Laboratory

Jesse Sears
Institution
Environmental Molecular Sciences Laboratory