Factors contributing to decreased protein stability when aspartic acid residues are in beta-sheet regions.
DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNSKNYLAWYQDKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT ISSLQAEDVAVYYCQQYYSTPYSFGQGTKLEIKR
25% PEG monomethylether 550, 0.01 M zinc sulfate, 0.1 M MES pH 6.5, 0.001M Uranyl Acetate, VAPOR DIFFUSION, HANGING DROP, temperature 298K
Effect of Aspartic Acid in Beta-sheet Regions on Protein Stability
recombinant Len in hexagonal crystal form
Native Len is a homo-dimer, whereas the Q38D mutant reported in this entry appears to be a monomer in the crystal. In solution, the association constant of Q38D is 66 times lower than the native Len.
Due to the presence of uranyl ion in the crystal there is significant anomalous contribution to the diffraction at 1 Angstrom wavelength. When Friedel pairs are not averaged, the anomalous difference Patterson map calculated clearly showed the position of uranium atom. Using the anomalous data the final model has an R-factor of 0.231 and R-free of 0.264. THE ELECTRON DENSITY INDICATED ANISOROPIC MOTION OF THE URANIUM ATOM. THE POSITIONS OF URANYL OXYGENS WERE NOT CLEAR IN THE ELECTRON DENSITY MAPS. THE OXYGEN ATOMS WERE PLACED ACCORDING TO THE EXPECTED GEOMETRY AROUND THE URANIUM ATOM AND SEEM TO IMPROVE BOTH R-FACTORS.
Human Kappa-4 Immunoglobulin Light Chain, Mutant, Monomer, Uranyl ion in crystal contact, Aspartic Acid in beta-sheet, Protein Stability, IMMUNE SYSTEM
DIVMTQSPDSLAVSLGERATINCKSSQSVLYSSNSKNYLAWYQQKPGQPPKLLIYWASTRESGVPDRFSGSGSGTDFTLT ISSLQAEDVAVYYCQQYYSTPYSFGQGTKLEIKR