Structural comparison of in vitro evolved proteins with biological proteins will help determine the extent to which biological proteins sample the structural diversity available in protein sequence space. We have previously isolated a family of nonbiological ATP binding proteins from an unconstrained random sequence library. One of these proteins was further optimized for high-affinity binding ...

Densities and viscosities of aqueous solutions of urea and guanidine hydrochloride at 250 have been measured, and equations are presented which describe their variation with concentration. Densities and viscosities of similar solutions containing additional solutes (buffers, NaCI, -mercaptoethanol) have been measured, and the possibility of predicting these results from information on solutions...

Listing Use your browser’s Print button, or File-Print command sequence. 530356: Effects of guanidine hydrochloride on the structure and properties of beta-casein in solution and at interface with air PHYS 0 [530356]: Effects of guanidine hydrochloride on the structure and properties of beta-casein in solution and at interface with air Adel Aschi, Departement of Physics, Tunisia University, Lab...

To obtain more information about the structural properties and conformational stabilities of GFP-like fluorescent proteins, we have undertaken a systematic analysis of series of green and red fluorescent proteins with different association states. The list of studied proteins includes EGFP (green monomer), zFP506 (green tetramer), mRFP1 (red monomer), "dimer2" (red dimer), and DsRed1 (red tetra...

Semisynthetic green fluorescent proteins (GFPs) can be prepared by producing truncated GFPs recombinantly and assembling them with synthetic beta-strands of GFP. The yield from expressing the truncated GFPs is low, and the chromophore is either partially formed or not formed. An alternative method is presented in which full-length proteins are produced recombinantly with a protease site inserte...

Protein folding is a central problem in the biological sciences. To generate residue-specific information on the equilibrium folding of cytochrome c, we have semisynthesized the protein with specifically deuterated residues. The C-D bonds may be easily visualized in an otherwise transparent region of the IR spectra, even at high protein and denaturant concentrations. Plotted as a function of ad...

To understand how proteins fold in vivo, it is important to investigate the effects of macromolecular crowding on protein folding. Here, the influence of crowding on in vitro apoflavodoxin folding, which involves a relatively stable off-pathway intermediate with molten globule characteristics, is reported. To mimic crowded conditions in cells, dextran 20 at 30% (w/v) is used, and its effects ar...

G-100 is used for higher molecular mass proteins. The solutions of proteins are prepared in guanidine hydrochloride (10 mg mL ), and cytochromec (10 mg mL ) is used as an internal standard. Descending chromatography is carried out at room temperature under an inclination angle of 253 to the horizontal. After 3 h of development the quotient Rs protein/Rs cytochrome c is calculated for each prote...