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ANS fluorescence detects widespread perturbations of protein tertiary structure in ice. - Abstract - Europe PMC
Inactivation and Unfolding of Protein Tyrosine Phosphatase from Thermus thermophilus HB27 during Urea and Guanidine Hydrochloride Denaturation | PLOS ONE
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Molecules | Free Full-Text | Revisiting the Rate-Limiting Step of the ANS– Protein Binding at the Protein Surface and Inside the Hydrophobic Cavity
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Application of ANS fluorescent probes to identify hydrophobic sites on the surface of DREAM - ScienceDirect
1-Anilino-8-Naphthalene Sulfonate (ANS) Is Not a Desirable Probe for Determining the Molten Globule State of Chymopapain | PLOS ONE
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Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis | Nature Structural & Molecular Biology
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Protein Folding Mediated by an Intramolecular Chaperone: Energy Landscape for Unimolecular Pro-Subtilisin E Maturation
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Figure 5 from 4,4'-Bis (1-anilinonaphthalene 8-sulfonate) (bis-ANS): a new probe of the active site of myosin. | Semantic Scholar
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PDF) ANS Fluorescence Detects Widespread Perturbations of Protein Tertiary Structure in Ice | edi gabellieri - Academia.edu
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Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy | Nature
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Spectroscopic Studies on Unfolding Processes of Apo-Neuroglobin Induced by Guanidine Hydrochloride and Urea
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ANS Fluorescence Detects Widespread Perturbations of Protein Tertiary Structure in Ice: Biophysical Journal
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Multiphoton ANS Fluorescence Microscopy as an in vivo Sensor for Protein Misfolding Stress Tingwei Guo ppt download
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Multiphoton ANS Fluorescence Microscopy as an in vivo Sensor for Protein Misfolding Stress Tingwei Guo ppt download
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A. Representative fluorescence spectra of ANS in a variety of solvents... | Download Scientific Diagram
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Spectroscopic Studies on Unfolding Processes of Apo-Neuroglobin Induced by Guanidine Hydrochloride and Urea
1-anilinonaphthalene-8-sulfonate (ANS); a versatile fluorescent probe from protein folding study to drug design
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