Add to ORKGWe recently described the high-resolution X-ray structure of a helical bundle composed of eight copies of the β-peptide Zwit-1F. Like many proteins in Nature, the Zwit-1F octamer contains parallel and antiparallel helices, extensive inter-helical electrostatic interactions, and a solvent-excluded hydrophobic core. Here we explore the stability of the Zwit-1F octamer using circular dichroism (CD) spectroscopy, analytical ultracentrifugation (AU), differential scanning calorimetry (DSC), and NMR. These studies demonstrate that the thermodynamic and kinetic properties of Zwit-1F closely resemble those of α-helical bundle proteins. Together these studies should provide a model for the design of β-peptide proteins with biological functions
In the natural peptides, helices are stabilized by hydrogen bonds that point backward along the sequ...
The understanding of fast folding dynamics of single α-helices comes mostly from studies on rational...
AbstractMini-proteins that contain <50 amino acids often serve as model systems for studying protein...
We recently described the high-resolution X-ray structure of a helical bundle composed of eight copi...
We recently reported that β-peptides can form discrete hetero-oligomers in aqueous solution. Here we...
Proteins composed of α-amino acids are essential components of the machinery required for life. Stan...
AbstractBeta-peptides are emerging as an attractive class of peptidomimetic molecules. In contrast t...
AbstractCollagen is the fundamental structural protein, comprising 25–35% of the total body protein,...
AbstractWe test molecular level hypotheses for the high thermal stability of α-helical conformations...
AbstractWe have performed experimental measurements and computer simulations of the equilibrium stru...
The protein-folding problem has greatly advanced over several decades, and our understanding of prot...
AbstractA simplified interaction potential for protein folding studies at the atomic level is discus...
AbstractSecondary structure is not typically observed for small peptides in solution. Several of the...
Honors (Bachelor's)BiochemistryMathematicsUniversity of Michiganhttp://deepblue.lib.umich.edu/bitstr...
Thermal unfolding of proteins is used extensively in screening of drug candidates because molecular ...
In the natural peptides, helices are stabilized by hydrogen bonds that point backward along the sequ...
The understanding of fast folding dynamics of single α-helices comes mostly from studies on rational...
AbstractMini-proteins that contain <50 amino acids often serve as model systems for studying protein...
We recently described the high-resolution X-ray structure of a helical bundle composed of eight copi...
We recently reported that β-peptides can form discrete hetero-oligomers in aqueous solution. Here we...
Proteins composed of α-amino acids are essential components of the machinery required for life. Stan...
AbstractBeta-peptides are emerging as an attractive class of peptidomimetic molecules. In contrast t...
AbstractCollagen is the fundamental structural protein, comprising 25–35% of the total body protein,...
AbstractWe test molecular level hypotheses for the high thermal stability of α-helical conformations...
AbstractWe have performed experimental measurements and computer simulations of the equilibrium stru...
The protein-folding problem has greatly advanced over several decades, and our understanding of prot...
AbstractA simplified interaction potential for protein folding studies at the atomic level is discus...
AbstractSecondary structure is not typically observed for small peptides in solution. Several of the...
Honors (Bachelor's)BiochemistryMathematicsUniversity of Michiganhttp://deepblue.lib.umich.edu/bitstr...
Thermal unfolding of proteins is used extensively in screening of drug candidates because molecular ...
In the natural peptides, helices are stabilized by hydrogen bonds that point backward along the sequ...
The understanding of fast folding dynamics of single α-helices comes mostly from studies on rational...
AbstractMini-proteins that contain <50 amino acids often serve as model systems for studying protein...