TY  - JOUR
AU  - Stanković, Ivana
AU  - Bozinovski, Dragana M.
AU  - Brothers, Edward N.
AU  - Belić, Milivoj
AU  - Hall, Michael B.
AU  - Zarić, Snežana D.
PY  - 2017
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/2115
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  - American Chemical Society (ACS)
T2  - Crystal Growth & 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 and Bozinovski, Dragana M. and Brothers, Edward N. and Belić, Milivoj 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 = "American Chemical Society (ACS)",
journal = "Crystal Growth & 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., Bozinovski, D. M., Brothers, E. N., Belić, M., Hall, M. B.,& Zarić, S. D.. (2017). Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. in Crystal Growth & Design
American Chemical Society (ACS)., 17(12), 6353-6362.
https://doi.org/10.1021/acs.cgd.7b01035

Stanković I, Bozinovski DM, Brothers EN, Belić M, Hall MB, Zarić SD. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. in Crystal Growth & Design. 2017;17(12):6353-6362.
doi:10.1021/acs.cgd.7b01035 .

Stanković, Ivana, Bozinovski, Dragana M., Brothers, Edward N., Belić, Milivoj, Hall, Michael B., Zarić, Snežana D., "Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data" in Crystal Growth & Design, 17, no. 12 (2017):6353-6362,
https://doi.org/10.1021/acs.cgd.7b01035 . .