Applications of DNP and solid-state NMR for protein structure determination
Name
655808064-MIT.pdf
Description
Full printable version
Size
4.41 MB
Format
Adobe PDF
Checksum (MD5)
b8a27d5595dae949b30bd37eec3550fd
Author(s)
Mayrhofer, Rebecca Maria
Advisor(s)
Robert G. Griffin.
Alternative Title
Applications of dynamic nuclear polarization and solid-state nuclear magnetic resonance for protein structure determination
Applications of DNP and SSNMR for protein structure determination
Date Issued
2010
Publisher
Massachusetts Institute of Technology
Abstract
Magic Angle Spinning (MAS) solid state nuclear magnetic resonance (SSNMR) is a developing method for determining the structures and studying the dynamics and functions of biological molecules. This method is particularly important for systems, such as amyloidogenic fibrous proteins, that do not crystallize or dissolve well and are therefore not amendable to X-ray or solution NMR techniques. However, due to inherently low sensitivity, NMR experiments may require weeks to obtain spectra with sufficient signal-to-noise ratio. This issue is further exacerbated for biological systems of interest due to their large size and limited mass availability. The sensitivity can be increased by two orders of magnitude by combining MAS NMR with dynamic nuclear polarization (DNP). The application of SSNMR-DNP to protein structure determination is explored using malonic acid and a model peptide system, WT-TTR105-115. A custom built MAS-SSNMR probe is modified for the purpose of MAS-SSNMR DNP experiments.
Description
Thesis (S.M.)--Massachusetts Institute of Technology, Dept. of Chemistry, 2010.
Vita. Cataloged from PDF version of thesis.
Includes bibliographical references.
Subjects
Chemistry.
MIT Department
Massachusetts Institute of Technology. Department of Chemistry
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