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  Secondary Structure of Ac-Alan-LysH+ Polyalanine Peptides (n = 5,10,15) in Vacuo: Helical or Not?

Rossi, M., Blum, V., Kupser, P., Helden, G. v., Bierau, F., Pagel, K., et al. (2010). Secondary Structure of Ac-Alan-LysH+ Polyalanine Peptides (n = 5,10,15) in Vacuo: Helical or Not? The Journal of Physical Chemistry Letters, 1(24), 3465-3470. doi:10.1021/jz101394u.

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 Creators:
Rossi, Mariana1, Author           
Blum, Volker1, Author           
Kupser, Peter2, Author           
Helden, Gert von2, Author           
Bierau, Frauke2, Author           
Pagel, Kevin3, Author
Meijer, Gerard2, Author           
Scheffler, Matthias1, Author           
Affiliations:
1Theory, Fritz Haber Institute, Max Planck Society, ou_634547              
2Molecular Physics, Fritz Haber Institute, Max Planck Society, ou_634545              
3Freie Universitt Berlin, Institut fr Chemie und Biochemie, D-14195 Berlin, Germany, ou_persistent22              

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Free keywords: gas-phase peptide; anharmonic effects; IR spectroscopy; density functional theory; electronic structure; alanine; helix
 Abstract: The polyalanine-based peptide series Ac-Alan-LysH+ (n = 5−20) is a prime example that a secondary structure motif that is well-known from the solution phase (here: helices) can be formed in vacuo. Here we revisit the series members n = 5,10,15, using density functional theory (van der Waals corrected generalized gradient approximation) for structure predictions, which are then corroborated by room temperature gas-phase infrared vibrational spectroscopy. We employ a quantitative comparison based on Pendry’s reliability factor (popular in surface crystallography). In particular, including anharmonic effects into calculated spectra by way of ab initio molecular dynamics produces remarkably good experiment−theory agreement. We find the longer molecules (n = 10,15) to be firmly α-helical in character. For n = 5, calculated free-energy differences show different H-bond networks to still compete closely. Vibrational spectroscopy indicates a predominance of α-helical motifs at 300 K, but the lowest-energy conformer is not a simple helix.

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Language(s): eng - English
 Dates: 2010-12-012010
 Publication Status: Published in print
 Pages: 6
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1021/jz101394u
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Title: The Journal of Physical Chemistry Letters
Source Genre: Journal
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Publ. Info: Washington DC : American Chemical Society
Pages: - Volume / Issue: 1 (24) Sequence Number: - Start / End Page: 3465 - 3470 Identifier: ISSN: 1932-7447
CoNE: https://pure.mpg.de/cone/journals/resource/954926947766_3