19 F NMR Chemical Shifts Induced by a Helical Peptide
Author:
Affiliation:
1. Department of Chemistry, Fairfield University, 1073 North Benson Road, Fairfield, CT 06824, USA, Fax: (+1) 203‐254‐4034
Publisher
Wiley
Subject
Organic Chemistry,Molecular Biology,Molecular Medicine,Biochemistry
Link
https://onlinelibrary.wiley.com/doi/pdf/10.1002/cbic.200500541
Reference36 articles.
1. The Preparation of 19F-Labeled Proteins for NMR Studies
2. NMR Studies of 4-19F-Phenylalanine-Labeled Intestinal Fatty Acid Binding Protein: Evidence for Conformational Heterogeneity in the Native State
3. Folding and Domain−Domain Interactions of the Chaperone PapD Measured by 19F NMR
4. Real-time and equilibrium 19F-NMR studies reveal the role of domain-domain interactions in the folding of the chaperone PapD
5. Dynamic NMR spectral analysis and protein folding: identification of a highly populated folding intermediate of rat intestinal fatty acid-binding protein by 19F NMR.
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1. 19F NMR chemical shifts are sensitive to remote functional group variations;Journal of Molecular Structure;2023-07
2. Electrostatic effects on 19F NMR chemical shifts in N-phenyl γ-lactam derivatives;Tetrahedron;2022-05
3. Progress in Our Understanding of 19F Chemical Shifts;Annual Reports on NMR Spectroscopy;2018
4. Synthesis of Poly-Aib Oligopeptides and Aib-Containing Peptides via the ‘Azirine/Oxazolone Method’, and Their Crystal Structures;Helvetica Chimica Acta;2011-06
5. Approaches for the measurement of solvent exposure in proteins by 19F NMR;Journal of Biomolecular NMR;2009-08-05
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