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Magic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules

TitleMagic-Angle-Spinning NMR Techniques for Measuring Long-Range Distances in Biological Macromolecules
Publication TypeJournal Article
Year of Publication2013
AuthorsHong, M, Schmidt-Rohr, K
JournalAccounts of Chemical Research
Volume46
Pagination2154-2163
Date Published09
Type of ArticleArticle
ISBN Number0001-4842
Accession NumberWOS:000330017600025
Keywordsarginine, cell-penetrating peptide, diffusion nmr, hairpin antimicrobial peptide, interactions, lipid-bilayers, membrane peptide, pore formation, solid-state nmr, Spectroscopy, water-protein
Abstract

ine crystallite thicknesses in biological anocomposites such as bone.The rotational-echo double-resonance (REDOR) technique allows us to detect multispin C-13-P-31 and C-13-H-2 dipolar couplings.Quantitative analysis of these couplings provides information about the structure of peptides bound to phospholipid bilayers and the geometry of ligand-binding sites in proteins. Finally, we also use relayed magnetization transfer, or spin diffusion, to measure long distances. z-Magnetization can diffuse over several nanometers because its long T subset of 1 subset of relaxation times allow it to survive for hundreds of milliseconds. We developed H-1 spin diffusion to probe the depths of protein insertion into the lipid bilayer and protein-water interactions. On the other hand, (19F) spin diffusion of site-specifically fluorinated molecules allowed us to elucidate the oligomeric structures of membrane peptides.

DOI10.1021/ar300294x
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SSNMR

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NIH

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NSF