Poly Ala vs Poly Gly
Scott-
I'm not absolutely certain of the answer, but perhaps my thoughts will
help you get closer. Poly-L-Ala is a model polymer (as is Poly-L-Glu) of
peptides that readily assume an alpha helical conformation. The methyl side
chain ("R" group) of Ala is both hydrophobic enough and bulky enough
to exclude
water, yet not so bulky as to cause unfavorable van der Waal's contacts between
adjacent residues; thus, a helical structure is favored. Gly is commonly
assumed to be a "helix breaker" because it has an "R" group
of Hydrogen which
lacks the hydrophobicity and steric bulk needed to exclude water from the
helix. If water has access to the helix, the carbonyl...HN- hydrogen bonds
can be broken by exchange and the helix would "fall apart" (revert to
another
conformation). This should be the case for poly-Gly. Thus, if you do energy
minimization/dynamics for poly-Gly in vacuuo, I would assume that helical
structure would result (left of right handed pitch), because the hydrogen bonds
could form and the side chain (hydrogen) would offer no steric repulsion.
However, it would be essentially impossible for helical structure to exist in
the presence of water. So, my answere is *both* helical and non-helical,
depending on the experimental or computational conditions (vacuum/organic
solvent vs water). Hope this helps!
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Shaun D. Black | Bitnet: black (+ at +) ohstphrm.bitnet
Ohio State University | Internet: black (+ at +)
ohstphrm.pharmacy.ohio-state.edu
College of Pharmacy | Phone: (614) 292-3925
500 West 12th Avenue | FAX: (614) 292-2435
Columbus, OH 43210-1291 | :-)
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