ArticleProceedings of the National Academy of Sciences of the United States of America2010
Sum frequency generation and solid-state NMR study of the structure, orientation, and dynamics of polystyrene-adsorbed peptides.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.
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Who cites it
48 citing papers in PubMed.
- Ligand-induced conformational changes in protein molecules detected by sum-frequency generation.Biophysical journal · 2024Article
- Developments and Ongoing Challenges for Analysis of Surface-Bound Proteins.Annual review of analytical chemistry (Palo Alto, Calif.) · 2021Article
- Role of Water in CaCOJournal of the American Chemical Society · 2021Article
- Location and Conformation of the LKα14 Peptide in Water/Ethanol Mixtures.Langmuir : the ACS journal of surfaces and colloids · 2021Article
- Mirror-image antiparallel β-sheets organize water molecules into superstructures of opposite chirality.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Surface analysis tools for characterizing biological materials.Chemical Society reviews · 2020Review
- Chiral Inversion of Amino Acids in Antiparallel β-Sheets at Interfaces Probed by Vibrational Sum Frequency Generation Spectroscopy.The journal of physical chemistry. B · 2019Article
- Solid-State NMR and MD Study of the Structure of the Statherin Mutant SNa15 on Mineral Surfaces.Journal of the American Chemical Society · 2019Article
- Surface Analysis: From Single Crystals to Biomaterials.Surface and interface analysis : SIA · 2018Article
- Engineering Proteins at Interfaces: From Complementary Characterization to Material Surfaces with Designed Functions.Angewandte Chemie (International ed. in English) · 2018Review
- Basic experiments inMethods (San Diego, Calif.) · 2018Review
- Nonlinear Optical Methods for Characterization of Molecular Structure and Surface Chemistry.Topics in catalysis · 2018Article
- Electric fields control the orientation of peptides irreversibly immobilized on radical-functionalized surfaces.Nature communications · 2018Article
- Static solid-stateProgress in nuclear magnetic resonance spectroscopy · 2017Review
- Solid state deuterium NMR study of LKα14 peptide aggregation in biosilica.Biointerphases · 2017Article
- Interplay between adsorbed peptide structure, trapped water, and surface hydrophobicity.Biointerphases · 2017Article
- Comparative Dynamics of Methionine Side-Chain in FMOC-Methionine and in Amyloid Fibrils.Chemical physics letters · 2017Article
- Predicting the orientation of protein G B1 on hydrophobic surfaces using Monte Carlo simulations.Biointerphases · 2016Article
- Flexibility and Solvation of Amyloid-β Hydrophobic Core.The Journal of biological chemistry · 2016Article
- Effect of Lipid Composition on the Membrane Orientation of the G Protein-Coupled Receptor Kinase 2-Gβ1γ2 Complex.Biochemistry · 2016Article
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5 authors.
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Abstract
The power of combining sum frequency generation (SFG) vibrational spectroscopy and solid-state nuclear magnetic resonance (ssNMR) spectroscopy to quantify, with site specificity and atomic resolution, the orientation and dynamics of side chains in synthetic model peptides adsorbed onto polystyrene (PS) surfaces is demonstrated in this study. Although isotopic labeling has long been used in ssNMR studies to site-specifically probe the structure and dynamics of biomolecules, the potential of SFG to probe side chain orientation in isotopically labeled surface-adsorbed peptides and proteins remains largely unexplored. The 14 amino acid leucine-lysine peptide studied in this work is known to form an alpha-helical secondary structure at liquid-solid interfaces. Selective, individual deuteration of the isopropyl group in each leucine residue was used to probe the orientation and dynamics of each individual leucine side chain of LKalpha14 adsorbed onto PS. The selective isotopic labeling methods allowed SFG analysis to determine the orientations of individual side chains in adsorbed peptides. Side chain dynamics were obtained by fitting the deuterium ssNMR line shape to specific motional models. Through the combined use of SFG and ssNMR, the dynamic trends observed for individual side chains by ssNMR have been correlated with side chain orientation relative to the PS surface as determined by SFG. This combination provides a more complete and quantitative picture of the structure, orientation, and dynamics of these surface-adsorbed peptides than could be obtained if either technique were used separately.
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