PDF) ANS Fluorescence Detects Widespread Perturbations of Protein Tertiary Structure in Ice | edi gabellieri - Academia.edu
ANS fluorescence: Potential to discriminate hydrophobic sites of proteins in solid states - ScienceDirect
Extrinsic Fluorescent Dyes as Tools for Protein Characterization | SpringerLink
ANS Binding Reveals Common Features of Cytotoxic Amyloid Species | ACS Chemical Biology
Application of ANS fluorescent probes to identify hydrophobic sites on the surface of DREAM - ScienceDirect
Visualizing transient protein-folding intermediates by tryptophan-scanning mutagenesis | Nature Structural & Molecular Biology
1-anilinonaphthalene-8-sulfonate (ANS); a versatile fluorescent probe from protein folding study to drug design
Article
Heterogeneity in Protein Folding and Unfolding Reactions | Chemical Reviews
Protein Folding Mediated by an Intramolecular Chaperone: Energy Landscape for Unimolecular Pro-Subtilisin E Maturation
ANS Interacts with the Ca2+-ATPase Nucleotide Binding Site | SpringerLink
1-anilinonaphthalene-8-sulfonate (ANS); a versatile fluorescent probe from protein folding study to drug design
Figure 5 from 4,4'-Bis (1-anilinonaphthalene 8-sulfonate) (bis-ANS): a new probe of the active site of myosin. | Semantic Scholar
1-Anilino-8-Naphthalene Sulfonate (ANS) Is Not a Desirable Probe for Determining the Molten Globule State of Chymopapain | PLOS ONE
Protein fluorescence characterization in the presence of ANS. Panel A:... | Download Scientific Diagram
Fluorescence spectra of ANS upon binding to hFGF-1 in its native (0 M... | Download Scientific Diagram
Spectroscopic Studies on Unfolding Processes of Apo-Neuroglobin Induced by Guanidine Hydrochloride and Urea
Perturbation of Protein Tertiary Structure in Frozen Solutions Revealed by 1-Anilino-8-Naphthalene Sulfonate Fluorescence: Biophysical Journal
1-anilinonaphthalene-8-sulfonate (ANS); a versatile fluorescent probe from protein folding study to drug design
Molecules | Free Full-Text | Revisiting the Rate-Limiting Step of the ANS– Protein Binding at the Protein Surface and Inside the Hydrophobic Cavity
Effect of Signal Peptide on Stability and Folding of Escherichia coli Thioredoxin | PLOS ONE
Interactions with 8‐Anilinonaphthalene‐1‐sulfonic Acid (ANS) and Surface Hydrophobicity of Black Gram (Vigna mungo) Phaseolin - Deshpande - 2018 - Journal of Food Science - Wiley Online Library
Conformational Change and Intermediates in the Unfolding of α1-Antichymotrypsin*
Interactions with 8‐Anilinonaphthalene‐1‐sulfonic Acid (ANS) and Surface Hydrophobicity of Black Gram (Vigna mungo) Phaseolin - Deshpande - 2018 - Journal of Food Science - Wiley Online Library
Evidence for close side-chain packing in an early protein folding intermediate previously assumed to be a molten globule | PNAS
