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Theory and Applications of Nitroxide-based Paramagnetic Cosolutes for Probing Intermolecular and Electrostatic Interactions on Protein Surfaces | Journal of the American Chemical Society
Atomic resolution protein allostery from the multi-state structure of a PDZ domain | Nature Communications
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Bioinformatic Analysis and Biophysical Characterization Reveal Structural Disorder in G0S2 Protein | ACS Omega
Systematic Exploration of Protein Conformational Space Using a Distance Geometry Approach | Journal of Chemical Information and Modeling
![PDF] Calculation of protein extinction coefficients from amino acid sequence data. | Semantic Scholar](https://d3i71xaburhd42.cloudfront.net/af80a5d2beee749cff2f5d98dc4a8f0dfdd48074/4-Table3-1.png "PDF] Calculation of protein extinction coefficients from amino acid sequence data. | Semantic Scholar")
PDF] Calculation of protein extinction coefficients from amino acid sequence data. | Semantic Scholar
Frontiers | NMR Methods for Structural Characterization of Protein-Protein Complexes
PDF) Three-dimensional structures of α and β chemokines
Frontiers | An Integrative Approach to Determine 3D Protein Structures Using Sparse Paramagnetic NMR Data and Physical Modeling
Determination of three-dimensional structures of proteins in solution by nuclear magnetic resonance spectroscopy
Structure determination of high-energy states in a dynamic protein ensemble | Nature
A method for validating the accuracy of NMR protein structures | Nature Communications
Nick Anthis - Protein Parameter Calculator
Functional protein dynamics on uncharted time scales detected by nanoparticle-assisted NMR spin relaxation | Science Advances
Sequence‐specific determination of protein and peptide concentrations by absorbance at 205 nm - Anthis - 2013 - Protein Science - Wiley Online Library
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Table 1 from Calculation of protein extinction coefficients from amino acid sequence data. | Semantic Scholar
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Protein 3D Structure Computed from Evolutionary Sequence Variation | PLOS ONE
Molecules | Free Full-Text | Patterns in Protein Flexibility: A Comparison of NMR “Ensembles”, MD Trajectories, and Crystallographic B-Factors
Quantitative Interpretation of Solvent Paramagnetic Relaxation for Probing Protein–Cosolute Interactions | Journal of the American Chemical Society
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Chimeric single α-helical domains as rigid fusion protein connections for protein nanotechnology and structural biology - ScienceDirect
The accuracy of NMR protein structures in the Protein Data Bank - ScienceDirect
