Journal Issue - Volume 11 Issue 7 (July 2002)
Charge states rather than propensity for β‐structure determine enhanced fibrillogenesis in wild‐type Alzheimer's β‐amyloid peptide compared to E22Q Dutch mutant
- Francesca Massi, D. Klimov, D. Thirumalai, John E. Straub
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.3150102 (p 1639-1647)
Abstract The activity of the Alzheimer's amyloid β‐peptide is a sensitive function of the peptide's sequence. Increased fibril elongation rate of the E22Q Dutch mutant of the Alzheimer's amyloid β‐peptide relative to that of the wild‐type peptide has been observed. The increased activity has been attributed to a larger propensity for the formation of β structure in the monomeric E22Q mutant peptide in solution relative to the WT...
α‐Crystallin binds to the aggregation‐prone molten‐globule state of alkaline protease: Implications for preventing irreversible thermal denaturation
- Aparna Tanksale, Mohini Ghatge, Vasanti Deshpande
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.0201802 (p 1720-1728)
Abstract α‐Crystallin, the major eye‐lens protein with sequence homology with heat‐shock proteins (HSPs), acts like a molecular chaperone by suppressing the aggregation of damaged crystallins and proteins. To gain more insight into its chaperoning ability, we used a protease as the model system that is known to require a propeptide (intramolecular chaperone) for its proper folding. The protease (“N” state) from Conidiobolus...
Mapping the surface of Escherichia coli peptide deformylase by NMR with organic solvents
- Douglas W. Byerly, Craig A. McElroy, Mark P. Foster
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.0203402 (p 1850-1853)
Abstract Identifying potential ligand binding sites on a protein surface is an important first step for targeted structure‐based drug discovery. While performing control experiments with Escherichia coli peptide deformylase (PDF), we noted that the organic solvents used to solubilize some ligands perturbed many of the same resonances in PDF as the small molecule inhibitors. To further explore this observation, we recorded 15N HSQC spectra of E....
Prediction of the membrane‐spanning β‐strands of the major outer membrane protein of Chlamydia
- María José Rodríguez‐Marañón, Robin M. Bush, Ellena M. Peterson, Tilman Schirmer, Luis M. de la Maza
- Published in Wiley Interscience on Jan 01, 2009
- DOI: 10.1110/ps.3650102 (p 1854-1861)
Abstract There is preliminary experimental evidence indicating that the major outer‐membrane protein (MOMP) of Chlamydia is a porin. We tested this hypothesis for the MOMP of the mouse pneumonitis serovar of Chlamydia trachomatis using two secondary structure prediction methods. First, an algorithm that calculates the mean hydrophobicity of one side of putative β‐strands predicted the positions of 16 transmembrane segments, a structure common to known...
