Angewandte Chemie International Edition · 2012 · 33 citations · 17 references
Life SciencesBiochemistryBiophysicsProtein BiochemistryStructural BiochemistryStructural BiologyAmino Acid ChemistryMacromolecular AssemblyPeptide AnalysisPeptide ChemistryProtein StructureSecondary Structure FormationAmino Acid AnaloguesHigh-resolution SpectrometryPeptide InteractionsPeptide Secondary StructurePeptide Stability AnalysisPeptide Structure AnalysisTransient InteractionsTransient Protein-protein Interactions
Photochemical cross-linking was applied to trap intramolecular interactions in peptides. The incorporation of diazirine-labeled amino acid analogues in combination with high-resolution mass spectrometry made it possible to catch reverse-turn conformations within peptides, exactly map their self-interacting surfaces, and discriminate between stable and transient interactions. Detailed facts of importance to specialist readers are published as ”Supporting Information”. Such documents are peer-reviewed, but not copy-edited or typeset. They are made available as submitted by the authors. Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article.
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Allister J. Maynard, Gary J. Sharman, Mark S. Searle · Journal of the American Chemical Society · 1998 · 240 citations
Andrew L. MacKinnon, Jennifer L. Garrison, Ramanujan S. Hegde et al. · Journal of the American Chemical Society · 2007 · 136 citations · Full text