Title

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

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May 3rd, 9:00 AM May 3rd, 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.