Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance

1987/07/01 by Gerhard Wagner, Daniel Brühwiler, Kurt Wüthrich · 10 citations
Biochemistry, Genetics and Molecular Biology · Physics and Astronomy · Chemistry · #Protein Structure and Dynamics #Spectroscopy and Quantum Chemical Studies #Molecular spectroscopy and chirality

paper · doi:10.1016/0022-2836(87)90524-9

Cited by

• Slow ring flips in aromatic cluster of GB1 studied by aromatic 13C relaxation dispersion methods
• Atomic-Level Characterization of the Structural Dynamics of Proteins
• Global motions exhibited by proteins in micro- to milliseconds simulations concur with anisotropic network model predictions. [europepmc]
• Localization of Millisecond Dynamics: Dihedral Entropy from Accelerated MD. [europepmc]
• Site-selective 13 C labeling of proteins using erythrose. [europepmc]
• Slow ring flips in aromatic cluster of GB1 studied by aromatic 13 C relaxation dispersion methods. [europepmc]
• Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations. [europepmc]
• Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms. [europepmc]
• NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins. [europepmc]
• Free-Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitors Using Metadynamics. [europepmc]