β-Sheet Preferences from First Principles

The natural amino acids have different preferences of occurring in specific types of secondary protein structure. Simulations are performed on periodic model β-sheets of 14 different amino acids, at the level of density functional theory, employing the generalized gradient approximation. We find tha...

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Bibliographic Details
Published in:Journal of the American Chemical Society 2003-12, Vol.125 (52), p.16383-16386
Main Authors: Rossmeisl, Jan, Kristensen, Iben, Gregersen, Misha, Jacobsen, Karsten W, Nørskov, Jens K
Format: Article
Language:English
Subjects:
Amino Acids - chemistry
Atomic and molecular physics
Bond strengths, dissociation energies
Computer Simulation
Exact sciences and technology
Models, Chemical
Molecular properties and interactions with photons
Physics
Properties of molecules and molecular ions
Protein Structure, Secondary
Proteins - chemistry
Thermodynamics
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Summary:The natural amino acids have different preferences of occurring in specific types of secondary protein structure. Simulations are performed on periodic model β-sheets of 14 different amino acids, at the level of density functional theory, employing the generalized gradient approximation. We find that the statistically observed β-sheet propensities correlate very well with the calculated binding energies. Analysis of the calculations shows that the β-sheet propensities are determined by the local flexibility of the individual polypeptide strands.
ISSN:0002-7863
1520-5126
DOI:10.1021/ja0359658