Consequences of Non-Uniformity in the Stoichiometry of Component Fractions within One and Two Loops Models of α-Helical Peptides
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Author(s)
1United State Department of Agriculture, Agricultural Research Service, Beltsville, Maryland, USA.
2Department of Biology, School of Computer, Mathematical, and Natural Sciences, Morgan State University, Baltimore, Maryland, USA.
3Clarence M. Mitchell Jr. School of Engineering, Morgan State University, Baltimore, Maryland, USA.
2Department of Biology, School of Computer, Mathematical, and Natural Sciences, Morgan State University, Baltimore, Maryland, USA.
3Clarence M. Mitchell Jr. School of Engineering, Morgan State University, Baltimore, Maryland, USA.
A 3-D electrostatic density map generated using the
Wavefront Topology System and Finite Element Method clearly demonstrates
the non-uniformity and periodicity present in even a single loop of an
α-helix. The four dihedral angles (N-C*-C-N, C*-C-N-C*, and C-N-C*-C)
fully define a helical shape independent of its length: the three
dihedral angles, φ = -33.5°, ω = 177.3°, and Ψ = -69.4°, generate the
precise (and identical) redundancy in a one loop (or longer) α-helical
shape (pitch = 1.59
/residue; r = 2.25
).
Nevertheless the pattern of dihedral angles within an 11 and a
22-peptide backbone atom sequence cannot be distributed evenly because
the stoichiometry in fraction of four atoms never divides evenly into 11
or 22 backbone atoms. Thus, three sequential sets of 11 backbone atoms
in an α-helix will have a discretely different chemical formula and
correspondingly different combinations of molecular forces depending
upon the assigned starting atom in an 11-step sequence. We propose that
the unit cell of one loop of an α-helix occurs in the peptide backbone
sequence C-(N-C*-C)3-N which contains an odd number of C* plus even
number of amide groups. A two-loop pattern (C*-C-N)7-C* contains an even
number of C* atoms plus an odd number of amide groups. Dividing the
two-loop pattern into two equal lengths, one fraction will have an extra
half amide (N-H) and the other fraction will have an extra half amide
C=O, i.e., the stoichiometry of each half will be different. Also, since
the length of N-C*-C-N, C*-C-N-C*, and C-N-C*-C are unequal, the
summation of the number of each in any fraction of n loops of an α-helix
in sequence will always have unequal length, depending upon the
starting atom (N, C*, or C).
KEYWORDS
Cite this paper
Schmidt, W. , Hapeman, C. , Wachira, J. and Thomas,
C. (2014) Consequences of Non-Uniformity in the Stoichiometry of
Component Fractions within One and Two Loops Models of α-Helical
Peptides. Journal of Biophysical Chemistry, 5, 125-133. doi: 10.4236/jbpc.2014.54014.
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