K2D2: estimation of protein secondary structure from circular dichroism spectra May 14, 2008
Circular dichroism spectroscopy is a widely used technique to analyze the secondary structure of proteins in solution. Predictive methods use the circular dichroism spectra from proteins of known tertiary structure to assess the secondary structure contents of a protein with unknown structure given its circular dichroism spectrum ... We developed K2D2, a method with an associated web server to estimate protein secondary structure from circular dichroism spectra. (BioMed Central)
Short Bacterial Protein Is Surprisingly Versatile Jan 23, 2008
However, the MIT researchers used a technique called circular dichroism spectroscopy to reveal that at concentrations similar to those in living bacteria, UmuD appears as a random coil. As the intrinsically disordered proteins bind with other proteins, they may change their shape, allowing them to then interact with different proteins, potentially creating a chronological sequence of interactions as proteins bind and then are cast off. (Science Daily)
Proteins pack tighter in crowded native state Nov 13, 2007
The secondary structure of the folded protein increased by as much as 25 percent based on circular dichroism data. From the simulations, it is evident that these changes occur in the ends of the helices and in the core, where the peptide chain packs better," Cheung said. Also, the unfolded state becomes more compact, as predicted by excluded volume theory. These effects on the folded and unfolded states made the native state of the protein 20 degrees Celsius more resistant to thermal... (EurekAlert!)
Crystal structure of hyperthermophilic esterase EstE1 and the relationship between its dimerization and thermostability properties Jul 12, 2007
Circular dichroism spectroscopy and heat inactivation kinetic analysis of EstE1 mutants, which were generated by structure-based site-directed mutagenesis of amino acid residues participating in EstE1 dimerization, revealed that hydrophobic interactions through Val274 and Phe276 on the 8 strand of each monomer play a major role in the dimerization of EstE1. In contrast, the intermolecular salt bridges contribute less significantly to the dimerization and thermostability of EstE1. (BioMed Central)
Hydrogen bonds shown to play 'conserved' role in protein folding Feb 11, 2006
" The Duke researchers' experiments were "technically challenging," Fitzgerald said. As a first step, his former graduate student Wales had to make sure they could synthesize appropriately "unnatural" mutant forms of the Arc and CopG proteins in the test tube. While scientists commonly use automated recombinant DNA technology to engineer proteins, that technique doesn't work very well to introduce unnatural mutant sequences that could selectively delete individual hydrogen bonds while keeping... (EurekAlert!)
