Parity-Violation Energy of Biomolecules - IV: Protein Secondary Structure

Statistics – Computation

Scientific paper

Rate now

  [ 0.00 ] – not rated yet Voters 0   Comments 0

Details

Scientific paper

The parity-violation energy difference between enantiomeric forms of the same amino acid sequence, from the amyloid β-peptide involved in Alzheimer's desease, in both α-helix and β-sheet configurations, is investigated with ab-initio techniques. To this end, we develop an extension of the N2 computational scheme that selectively includes neighboring amino acids to preserve the relevant H-bonds. In agreement with previous speculations, it is found that the helical α structure is associated with larger parity-violation energy differences than the corresponding β form. Implications for the evolution of biological homochirality are discussed as well as the relative importance of various effects in determining the parity-violation energy.

No associations

LandOfFree

Say what you really think

Search LandOfFree.com for scientists and scientific papers. Rate them and share your experience with other people.

Rating

Parity-Violation Energy of Biomolecules - IV: Protein Secondary Structure does not yet have a rating. At this time, there are no reviews or comments for this scientific paper.

If you have personal experience with Parity-Violation Energy of Biomolecules - IV: Protein Secondary Structure, we encourage you to share that experience with our LandOfFree.com community. Your opinion is very important and Parity-Violation Energy of Biomolecules - IV: Protein Secondary Structure will most certainly appreciate the feedback.

Rate now

     

Profile ID: LFWR-SCP-O-1002166

  Search
All data on this website is collected from public sources. Our data reflects the most accurate information available at the time of publication.