Journal of Enzyme Inhibition and Medicinal Chemistry 2020, 35 Human carbonic anhydrases and post-translational modifications: a hidden world possibly affecting protein properties and functions. Supuran, Andrea Scaloni, Giuseppina De Simone. Post-translational modifications in tumor-associated carbonic anhydrases. Carbonic Anhydrase as a Model for Biophysical and Physical-Organic Studies of Proteins and Protein−Ligand Binding. Journal of the American Chemical Society 2010, 132 Neutralizing Positive Charges at the Surface of a Protein Lowers Its Rate of Amide Hydrogen Exchange without Altering Its Structure or Increasing Its Thermostability. Pollastri, Andrew Lee, Basar Bilgicer, Steven P. ![]() Shaw, Haribabu Arthanari, Max Narovlyansky, Armando Durazo, Dominique P. ![]() The Journal of Physical Chemistry B 2011, 115 Influence of Fluorocarbon and Hydrocarbon Acyl Groups at the Surface of Bovine Carbonic Anhydrase II on the Kinetics of Denaturation by Sodium Dodecyl Sulfate. Denaturation of Proteins by SDS and Tetraalkylammonium Dodecyl Sulfates. The Journal of Physical Chemistry B 2016, 120 Acetylation of Surface Lysine Groups of a Protein Alters the Organization and Composition of Its Crystal Contacts. Kyungtae Kang, Jeong-Mo Choi, Jerome M.This article is cited by 29 publications. This study reinforces the idea that charged residues on the surface of BCA do not guide protein folding and raises the broader question of why proteins have charged residues on their surface, outside of the region of the active site. This study suggests that large differences in the net charge of the polypeptide have no significant influence on the structure, the ability to refold, or the rate of refolding of this protein from solutions containing SDS. ![]() When the SDS was removed by dialysis, both proteins were regenerated in native form. SDS at concentrations above ∼10 mM denatured both proteins. Both BCA and BCA-Ac 18 are catalytically active, and circular dichroism spectroscopy (CD) suggests that they have similar secondary and tertiary structures. Acetylation of BCA with acetic anhydride converts all 18 lysine-ε-NH 3 + groups to lysine-ε-NHCOCH 3 groups and generates BCA-Ac 18. This study compares the folding of two polypeptides bovine carbonic anhydrase (BCA) and peracetylated BCA (BCA-Ac 18) having the same sequence of amino acids but differing by 18 formal units of charge, from a solution containing denaturing concentrations of sodium dodecyl sulfate (SDS).
0 Comments
Leave a Reply. |
AuthorWrite something about yourself. No need to be fancy, just an overview. ArchivesCategories |