Reinvestigation of the aromatic side-chains in the basic pancreatic trypsin inhibitor by heteronuclear two-dimensional nuclear magnetic resonance
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Structural Biology
Reference19 articles.
1. Sequential resonance assignments in protein 1H nuclear magnetic resonance spectra
2. Complete tyrosine assignments in the high field proton nuclear magnetic resonance spectrum of the bovine pancreatic trypsin inhibitor
3. Activation volumes for the rotational motion of interior aromatic rings in globular proteins determined by high resolution 1 H NMR at variable pressure
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1. Free-Energy Landscape and Rate Estimation of the Aromatic Ring Flips in Basic Pancreatic Trypsin Inhibitors Using Metadynamics;Journal of Chemical Theory and Computation;2023-09-12
2. NMR Studies of Aromatic Ring Flips to Probe Conformational Fluctuations in Proteins;The Journal of Physical Chemistry B;2023-01-14
3. Characterizing Fast Conformational Exchange of Aromatic Rings Using Residual Dipolar Couplings: Distinguishing Jumplike Flips from Other Exchange Mechanisms;The Journal of Physical Chemistry B;2022-09-30
4. Conformational dynamics in peptide toxins: Implications for receptor interactions and molecular design;Toxicon;2021-10
5. Transition-State Compressibility and Activation Volume of Transient Protein Conformational Fluctuations;JACS Au;2021-06-03
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