Abstract
The interaction between the aromatic ring of an amino acid and the a-helical polypeptide backbone was investigated by studying the conformation of α-helical Ala-based model peptides, with Tyr replacement in the N-terminal and inner helical positions, using 1H NMR, molecular dynamics (MD) simulations, and a protein database search. NOE cross-peaks between the hydrogens of the aromatic ring at position i and the hydrogen of the backbone amide in positions i, i+1, i+3 and i+4 indicated the proximity of the aromatic ring to the backbone. Interaction between the aromatic ring and the backbone seemed to be highly dependent on the orientation of the aromatic side chain to the helical backbone because aromatic-backbone amide, aromatic - carbonyl, and aromatic - HCα interactions were observed in MD. Solvent screening by the aromatic side chain decreased the solvent accessible surface area of some polar backbone groups by more than 80%. These results indicate that aromatic - backbone interactions commonly occur in helical structures in proteins.
| Original language | English |
|---|---|
| Pages (from-to) | 9287-9296 |
| Number of pages | 10 |
| Journal | Journal of Physical Chemistry B |
| Volume | 108 |
| Issue number | 26 |
| DOIs | |
| State | Published - Jul 1 2004 |
Fingerprint
All Science Journal Classification (ASJC) codes
- Physical and Theoretical Chemistry
Cite this
Aromatic - Backbone interactions in α-helices. / Tóth, Gergely; Köver, Katalin E.; Murphy, Richard F.; Lovas, Sándor.
In: Journal of Physical Chemistry B, Vol. 108, No. 26, 01.07.2004, p. 9287-9296.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Aromatic - Backbone interactions in α-helices
AU - Tóth, Gergely
AU - Köver, Katalin E.
AU - Murphy, Richard F.
AU - Lovas, Sándor
PY - 2004/7/1
Y1 - 2004/7/1
N2 - The interaction between the aromatic ring of an amino acid and the a-helical polypeptide backbone was investigated by studying the conformation of α-helical Ala-based model peptides, with Tyr replacement in the N-terminal and inner helical positions, using 1H NMR, molecular dynamics (MD) simulations, and a protein database search. NOE cross-peaks between the hydrogens of the aromatic ring at position i and the hydrogen of the backbone amide in positions i, i+1, i+3 and i+4 indicated the proximity of the aromatic ring to the backbone. Interaction between the aromatic ring and the backbone seemed to be highly dependent on the orientation of the aromatic side chain to the helical backbone because aromatic-backbone amide, aromatic - carbonyl, and aromatic - HCα interactions were observed in MD. Solvent screening by the aromatic side chain decreased the solvent accessible surface area of some polar backbone groups by more than 80%. These results indicate that aromatic - backbone interactions commonly occur in helical structures in proteins.
AB - The interaction between the aromatic ring of an amino acid and the a-helical polypeptide backbone was investigated by studying the conformation of α-helical Ala-based model peptides, with Tyr replacement in the N-terminal and inner helical positions, using 1H NMR, molecular dynamics (MD) simulations, and a protein database search. NOE cross-peaks between the hydrogens of the aromatic ring at position i and the hydrogen of the backbone amide in positions i, i+1, i+3 and i+4 indicated the proximity of the aromatic ring to the backbone. Interaction between the aromatic ring and the backbone seemed to be highly dependent on the orientation of the aromatic side chain to the helical backbone because aromatic-backbone amide, aromatic - carbonyl, and aromatic - HCα interactions were observed in MD. Solvent screening by the aromatic side chain decreased the solvent accessible surface area of some polar backbone groups by more than 80%. These results indicate that aromatic - backbone interactions commonly occur in helical structures in proteins.
UR - http://www.scopus.com/inward/record.url?scp=18544410179&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=18544410179&partnerID=8YFLogxK
U2 - 10.1021/jp037945y
DO - 10.1021/jp037945y
M3 - Article
VL - 108
SP - 9287
EP - 9296
JO - Journal of Physical Chemistry B Materials
JF - Journal of Physical Chemistry B Materials
SN - 1520-6106
IS - 26
ER -