Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data
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2017
Authors
Stanković, Ivana M.Božinovski, Dragana M.
Brothers, Edward N.
Belić, Milivoj R.
Hall, Michael B.
Zarić, Snežana D.
Article (Published version)
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Aromatic-aromatic interactions have long been considered important in the self assembly of amyloids. In spite of their importance, aromatic amino acids are not detected in every amyloid. In the present study, the occurrence and geometry of these interactions were analyzed for the amyloid structures found in the Protein Data Bank. The data confirm that aromatic amino acids are not crucial for amyloid fibril formation. In fact, aromatic-aliphatic interactions are more frequent than the aromatic-aromatic interactions. Aromatic-aliphatic interactions are present in higher numbers of structures and in certain amyloid sequences they are more frequent than aromatic-aromatic interactions. An analysis of aromatic/aromatic interactions shows different interaction geometries in intrasheet and intersheet contacts; the intrasheet aromatic-aromatic interactions are mostly parallel and displaced, while intersheet interactions are not parallel. Thus, among the aromatic-aromatic interactions there are ...important edge-to-face attractions in addition to parallel stacking ones.
Source:
Crystal Growth and Design, 2017, 17, 12, 6353-6362Publisher:
- Amer Chemical Soc, Washington
Funding / projects:
- Noncovalent interactions of pi-systems and their role in molecular recognition (RS-MESTD-Basic Research (BR or ON)-172065)
- NPRP grant from Qatar National Research Fund (a member of the Qatar Foundation) [NPRP8-425-1-087]
Note:
- Supplementary material: http://cherry.chem.bg.ac.rs/handle/123456789/3079
DOI: 10.1021/acs.cgd.7b01035
ISSN: 1528-7483
WoS: 000417669900025
Scopus: 2-s2.0-85046349132
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Hemijski fakultet / Faculty of ChemistryTY - JOUR AU - Stanković, Ivana M. AU - Božinovski, Dragana M. AU - Brothers, Edward N. AU - Belić, Milivoj R. AU - Hall, Michael B. AU - Zarić, Snežana D. PY - 2017 UR - https://cherry.chem.bg.ac.rs/handle/123456789/2566 AB - Aromatic-aromatic interactions have long been considered important in the self assembly of amyloids. In spite of their importance, aromatic amino acids are not detected in every amyloid. In the present study, the occurrence and geometry of these interactions were analyzed for the amyloid structures found in the Protein Data Bank. The data confirm that aromatic amino acids are not crucial for amyloid fibril formation. In fact, aromatic-aliphatic interactions are more frequent than the aromatic-aromatic interactions. Aromatic-aliphatic interactions are present in higher numbers of structures and in certain amyloid sequences they are more frequent than aromatic-aromatic interactions. An analysis of aromatic/aromatic interactions shows different interaction geometries in intrasheet and intersheet contacts; the intrasheet aromatic-aromatic interactions are mostly parallel and displaced, while intersheet interactions are not parallel. Thus, among the aromatic-aromatic interactions there are important edge-to-face attractions in addition to parallel stacking ones. PB - Amer Chemical Soc, Washington T2 - Crystal Growth and Design T1 - Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data VL - 17 IS - 12 SP - 6353 EP - 6362 DO - 10.1021/acs.cgd.7b01035 ER -
@article{ author = "Stanković, Ivana M. and Božinovski, Dragana M. and Brothers, Edward N. and Belić, Milivoj R. and Hall, Michael B. and Zarić, Snežana D.", year = "2017", abstract = "Aromatic-aromatic interactions have long been considered important in the self assembly of amyloids. In spite of their importance, aromatic amino acids are not detected in every amyloid. In the present study, the occurrence and geometry of these interactions were analyzed for the amyloid structures found in the Protein Data Bank. The data confirm that aromatic amino acids are not crucial for amyloid fibril formation. In fact, aromatic-aliphatic interactions are more frequent than the aromatic-aromatic interactions. Aromatic-aliphatic interactions are present in higher numbers of structures and in certain amyloid sequences they are more frequent than aromatic-aromatic interactions. An analysis of aromatic/aromatic interactions shows different interaction geometries in intrasheet and intersheet contacts; the intrasheet aromatic-aromatic interactions are mostly parallel and displaced, while intersheet interactions are not parallel. Thus, among the aromatic-aromatic interactions there are important edge-to-face attractions in addition to parallel stacking ones.", publisher = "Amer Chemical Soc, Washington", journal = "Crystal Growth and Design", title = "Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data", volume = "17", number = "12", pages = "6353-6362", doi = "10.1021/acs.cgd.7b01035" }
Stanković, I. M., Božinovski, D. M., Brothers, E. N., Belić, M. R., Hall, M. B.,& Zarić, S. D.. (2017). Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. in Crystal Growth and Design Amer Chemical Soc, Washington., 17(12), 6353-6362. https://doi.org/10.1021/acs.cgd.7b01035
Stanković IM, Božinovski DM, Brothers EN, Belić MR, Hall MB, Zarić SD. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. in Crystal Growth and Design. 2017;17(12):6353-6362. doi:10.1021/acs.cgd.7b01035 .
Stanković, Ivana M., Božinovski, Dragana M., Brothers, Edward N., Belić, Milivoj R., Hall, Michael B., Zarić, Snežana D., "Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data" in Crystal Growth and Design, 17, no. 12 (2017):6353-6362, https://doi.org/10.1021/acs.cgd.7b01035 . .