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Solid-state NMR or proteins at fast magic angle spinning rates
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Perodeau, Jacqueline R.. Solid-state NMR or proteins at fast magic angle spinning rates. Retrieved from https://doi.org/doi:10.7282/t3-nj14-5r15

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TitleSolid-state NMR or proteins at fast magic angle spinning rates
NamePerodeau, Jacqueline R. (author); Nieuwkoop, Andy (chair); Rutgers University; School of Graduate Studies
Date Created2022
Other Date2022-10 (degree)
SubjectChemistry, Nuclear magnetic resonance, Proteins -- Structure, Spectrum analysis
Extent1 online resource (55 pages) : illustrations
DescriptionOver the last 15 years solid-state NMR (ssNMR) has undergone a huge leap forward, particularly as a spectroscopic technique for biomolecules. MAS NMR has become more widespread because of advances in probe technology and development of proton-detected multidimensional experiment. The development of probes which can spin rotors faster and faster allowed the development of experiments which have resolution and acquisition times approaching solution state experiments. ssNMR was used to evaluate three aspects of protein structure. Hydrogen bonding patterns of CDN labeled GB1 were investigated using hNCOH and hNCAH spectra at 105 kHz MAS. PIP3 binding by the kindlin-2 PH domain was investigated with P-N rotationalecho double resonance (REDOR) experiments.
NotePh.D.
NoteIncludes bibliographical references
Genretheses
Persistent URLhttps://doi.org/doi:10.7282/t3-nj14-5r15
LanguageEnglish
CollectionSchool of Graduate Studies Electronic Theses and Dissertations
Organization NameRutgers, The State University of New Jersey
RightsThe author owns the copyright to this work.
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