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| Home | Research | Mount Holyoke | Liverpool | |
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Ultimate Goal: |
To understand the earliest steps in protein folding, specifically the folding of alpha helices. | ||
| Techniques Employed: | Laser induced temperature jumps. Infrared spectroscopy (using both FTIR spectrometer and a continuous wave IR laser). |
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| Peptides Studied: | Poly(3-hydroxpropyl)-L-glutamine Poly(Alanine, Lysine, Glutamic acid, Tyrosine) Model alpha helical peptides. |
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| Main Findings: | The folding of model alpha helical peptides, was shown to occur on timescales of ~150 ns. Similar helix-coil relaxation time constants were observed for peptides with significantly larger and more complex side chains. The presence of oppositely charged amino acids (resulting in intrapeptide salt-bridges) significantly influenced folding kinetics. |
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| Advisor: | Dr. Martin Volk | |||