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Summary

This summary is machine-generated.

Beta-sheet is the most stable protein structure, while alpha-sheet conformations are less stable in solution. Computational methods reveal differences in stability and spectral properties between these protein secondary structures.

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Area of Science:

Biophysics
Computational Chemistry
Protein Science

Background:

Pauling and Corey proposed alpha-sheet as a protein secondary structure alongside alpha-helix and beta-sheet.
Alpha-sheet is increasingly implicated in amyloidogenic intermediates.

Purpose of the Study:

To investigate the solution-phase stability of antiparallel beta-sheet and two alpha-sheet conformations.
To compare theoretical predictions with force field results and experimental spectra.

Main Methods:

Density functional theory (DFT) calculations at the B3LYP/cc-pVTZ//B3LYP/6-31G* level.
Geometry optimization, single-point energy calculations, and inclusion of thermodynamic contributions.
Modeling peptides as two-strand acetyl-(Ala)(2)-N-methylamine.

Main Results:

Beta-sheet is the most stable conformation.
Pauling and Corey's alpha-sheet conformation has a 13.6 kcal/mol higher free energy than beta-sheet.
Alpha-sheet structures showed distortion in solution and distinct amide I IR spectra compared to beta-sheet.
AMBER parm94 force field predicted minimal energy difference between alpha-sheet and beta-sheet.

Conclusions:

Beta-sheet is thermodynamically more favorable than alpha-sheet conformations in solution.
DFT results contrast with AMBER force field predictions for alpha-sheet and beta-sheet stability.
Further investigation is needed for longer peptide chains and alpha-sheet stability in water.