PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 12533538-2 2003 By lyophilizing RNase A from 40% acetic acid solutions, two dimeric aggregates, the "minor" and "major" dimers (named here N-dimer and C-dimer, respectively), form by 3D domain swapping at a ratio of 1:4. Acetic Acid 33-44 ribonuclease A family member 1, pancreatic Homo sapiens 16-23 10736157-7 2000 Moreover, the HP-RNase dimers were found to be over 4.6 orders of magnitude more stable than the dimers of bovine pancreatic RNase A obtained by lyophilization from acetic acid (K(d) > 73 mM). Acetic Acid 165-176 ribonuclease A family member 1, pancreatic Homo sapiens 14-22 10648807-3 2000 240, 2868-3874) observed that dimeric RNase A prepared by lyophilization from acetic acid could be separated into two forms. Acetic Acid 78-89 ribonuclease A family member 1, pancreatic Homo sapiens 38-45 20085318-0 2010 NMR spectroscopy reveals that RNase A is chiefly denatured in 40% acetic acid: implications for oligomer formation by 3D domain swapping. Acetic Acid 66-77 ribonuclease A family member 1, pancreatic Homo sapiens 30-37 20085318-3 2010 RNase A oligomerization is induced by 40% acetic acid, which has been assumed to mildly unfold the protein by detaching the terminal segments and consequently facilitating intersubunit swapping, once the acetic acid is removed by lyophilization and the protein is redissolved in a benign buffer. Acetic Acid 42-53 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 20085318-3 2010 RNase A oligomerization is induced by 40% acetic acid, which has been assumed to mildly unfold the protein by detaching the terminal segments and consequently facilitating intersubunit swapping, once the acetic acid is removed by lyophilization and the protein is redissolved in a benign buffer. Acetic Acid 204-215 ribonuclease A family member 1, pancreatic Homo sapiens 0-7 20085318-4 2010 Using UV difference, near UV circular dichroism, folding kinetics, and multidimensional heteronuclear NMR spectroscopy, the conformation of RNase A in 40% acetic acid and in 8 M urea has been characterized. Acetic Acid 155-166 ribonuclease A family member 1, pancreatic Homo sapiens 140-147 20085318-5 2010 These studies demonstrate that RNase A is chiefly unfolded in 40% acetic acid; it partially retains the native helices, whereas the beta-sheet is fully denatured and all X-Pro peptide bonds are predominantly in the trans conformation. Acetic Acid 66-77 ribonuclease A family member 1, pancreatic Homo sapiens 31-38