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NMR Characterization of Amphipathic Helical Peptides

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Antibacterial Peptide Protocols

Part of the book series: Methods In Molecular Biology™ ((MIMB,volume 78))

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Abstract

The remarkable advances and improvements in nuclear magnetic resonance (NMR) technology and methodology in recent years have made significant impact on the investigation of biological macromolecules, including amphipathic helical peptides. Through NMR studies, the three-dimensional structures of such peptides can now be obtained in solution at resolution levels comparable to those of single-crystal X-ray structures. NMR spectroscopy can provide a wealth of additional information about peptides in solution. For example, oligomerization, peptide-lipid interactions, and dynamics of the peptide can be investigated. The diversity of information obtainable from NMR data as well as the ability to study the peptides under conditions analogous to those found in vivo makes NMR spectroscopy increasingly attractive for the investigation of biological macromolecules.

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Authors and Affiliations

  1. Department of Biochemistry, Louisiana State University, Baton Rouge, LA

    Xiaotang Wang & Kathleen M. Morden

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  1. Xiaotang Wang
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  2. Kathleen M. Morden
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Editors and Affiliations

  1. Emory University School of Medicine, Atlanta, GA

    William M. Shafer

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© 1997 Humana Press Inc.

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Wang, X., Morden, K.M. (1997). NMR Characterization of Amphipathic Helical Peptides. In: Shafer, W.M. (eds) Antibacterial Peptide Protocols. Methods In Molecular Biology™, vol 78. Humana Press. https://doi.org/10.1385/0-89603-408-9:85

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  • DOI: https://doi.org/10.1385/0-89603-408-9:85

  • Publisher Name: Humana Press

  • Print ISBN: 978-0-89603-408-2

  • Online ISBN: 978-1-59259-564-8

  • eBook Packages: Springer Protocols

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