Folding of Proteins of Proteins that Cannot be Folded
Format
Oral Presentation
Faculty Mentor Name
C. Michael McCallum
Abstract/Artist Statement
N-terminal cysteine-capping has been shown to increase helical stabilization of small peptides in the gas phase. We now show that this property plays an integral role in aqueous environments, stabilizing favorable interactions between charges and with water in biologically important peptide fragments. Replica Exchange Molecular Dynamics (REX-MD) along with Quantum Mechanical techniques are used to study this and other effects on the folding of a helical segment of the Yap 1 protein from yeast. The initial unfolding of sequences from the Lacl and 434Cro helix-tum-helix (HTH) motifs from a bacterial family of DNA regulation proteins was also studied, which included a simulation of the full434Cro HTH motif.
Location
Wendell Phillips Center, Room 151
Start Date
3-5-2008 9:00 AM
End Date
3-5-2008 12:30 PM
Folding of Proteins of Proteins that Cannot be Folded
Wendell Phillips Center, Room 151
N-terminal cysteine-capping has been shown to increase helical stabilization of small peptides in the gas phase. We now show that this property plays an integral role in aqueous environments, stabilizing favorable interactions between charges and with water in biologically important peptide fragments. Replica Exchange Molecular Dynamics (REX-MD) along with Quantum Mechanical techniques are used to study this and other effects on the folding of a helical segment of the Yap 1 protein from yeast. The initial unfolding of sequences from the Lacl and 434Cro helix-tum-helix (HTH) motifs from a bacterial family of DNA regulation proteins was also studied, which included a simulation of the full434Cro HTH motif.