TY  - JOUR
AU  - Božinovski, Dragana M.
AU  - Petrović, Predrag
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2154
AB  - The interaction of amyloid -sheet segments with graphene-flake models is investigated by using DFT calculations. The structure of -sheets of selected amyloid segments is based on crystal structures obtained from the Protein Data Bank. Our study, based on DFT calculations for model systems, indicates that the interaction in amyloid-graphene aggregates can be stronger than the interaction in the respective amyloid-amyloid aggregates. The results also indicate an important specific role of aromatic sidechains in amyloid-graphene interactions. This work confirms recent experimental evidence that graphene and its modifications inhibit the aggregation of -amyloid peptides.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemphyschem
T1  - Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene
VL  - 19
IS  - 10
SP  - 1226
EP  - 1233
DO  - 10.1002/cphc.201700847
ER  - 

@article{
author = "Božinovski, Dragana M. and Petrović, Predrag and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2018",
abstract = "The interaction of amyloid -sheet segments with graphene-flake models is investigated by using DFT calculations. The structure of -sheets of selected amyloid segments is based on crystal structures obtained from the Protein Data Bank. Our study, based on DFT calculations for model systems, indicates that the interaction in amyloid-graphene aggregates can be stronger than the interaction in the respective amyloid-amyloid aggregates. The results also indicate an important specific role of aromatic sidechains in amyloid-graphene interactions. This work confirms recent experimental evidence that graphene and its modifications inhibit the aggregation of -amyloid peptides.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemphyschem",
title = "Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene",
volume = "19",
number = "10",
pages = "1226-1233",
doi = "10.1002/cphc.201700847"
}

Božinovski, D. M., Petrović, P., Belić, M. R.,& Zarić, S. D.. (2018). Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene. in Chemphyschem
Wiley-V C H Verlag Gmbh, Weinheim., 19(10), 1226-1233.
https://doi.org/10.1002/cphc.201700847

Božinovski DM, Petrović P, Belić MR, Zarić SD. Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene. in Chemphyschem. 2018;19(10):1226-1233.
doi:10.1002/cphc.201700847 .

Božinovski, Dragana M., Petrović, Predrag, Belić, Milivoj R., Zarić, Snežana D., "Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene" in Chemphyschem, 19, no. 10 (2018):1226-1233,
https://doi.org/10.1002/cphc.201700847 . .

TY  - JOUR
AU  - Božinovski, Dragana M.
AU  - Petrović, Predrag
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3226
AB  - The interaction of amyloid -sheet segments with graphene-flake models is investigated by using DFT calculations. The structure of -sheets of selected amyloid segments is based on crystal structures obtained from the Protein Data Bank. Our study, based on DFT calculations for model systems, indicates that the interaction in amyloid-graphene aggregates can be stronger than the interaction in the respective amyloid-amyloid aggregates. The results also indicate an important specific role of aromatic sidechains in amyloid-graphene interactions. This work confirms recent experimental evidence that graphene and its modifications inhibit the aggregation of -amyloid peptides.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemphyschem
T1  - Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene
VL  - 19
IS  - 10
SP  - 1226
EP  - 1233
DO  - 10.1002/cphc.201700847
ER  - 

@article{
author = "Božinovski, Dragana M. and Petrović, Predrag and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2018",
abstract = "The interaction of amyloid -sheet segments with graphene-flake models is investigated by using DFT calculations. The structure of -sheets of selected amyloid segments is based on crystal structures obtained from the Protein Data Bank. Our study, based on DFT calculations for model systems, indicates that the interaction in amyloid-graphene aggregates can be stronger than the interaction in the respective amyloid-amyloid aggregates. The results also indicate an important specific role of aromatic sidechains in amyloid-graphene interactions. This work confirms recent experimental evidence that graphene and its modifications inhibit the aggregation of -amyloid peptides.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemphyschem",
title = "Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene",
volume = "19",
number = "10",
pages = "1226-1233",
doi = "10.1002/cphc.201700847"
}

Božinovski, D. M., Petrović, P., Belić, M. R.,& Zarić, S. D.. (2018). Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene. in Chemphyschem
Wiley-V C H Verlag Gmbh, Weinheim., 19(10), 1226-1233.
https://doi.org/10.1002/cphc.201700847

Božinovski DM, Petrović P, Belić MR, Zarić SD. Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene. in Chemphyschem. 2018;19(10):1226-1233.
doi:10.1002/cphc.201700847 .

Božinovski, Dragana M., Petrović, Predrag, Belić, Milivoj R., Zarić, Snežana D., "Insight into the Interactions of Amyloid -Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids that Interact with Graphene" in Chemphyschem, 19, no. 10 (2018):1226-1233,
https://doi.org/10.1002/cphc.201700847 . .

TY  - DATA
AU  - Božinovski, Dragana M.
AU  - Petrović, Predrag
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2018
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3227
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemphyschem
T1  - Supplementary data for the article: Božinovski, D. M.; Petrović, P. V.; Belić, M. R.; Zarić, S. D. Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids That Interact with Graphene. ChemPhysChem 2018, 19 (10), 1226–1233. https://doi.org/10.1002/cphc.201700847
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3227
ER  - 

@misc{
author = "Božinovski, Dragana M. and Petrović, Predrag and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2018",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemphyschem",
title = "Supplementary data for the article: Božinovski, D. M.; Petrović, P. V.; Belić, M. R.; Zarić, S. D. Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids That Interact with Graphene. ChemPhysChem 2018, 19 (10), 1226–1233. https://doi.org/10.1002/cphc.201700847",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3227"
}

Božinovski, D. M., Petrović, P., Belić, M. R.,& Zarić, S. D.. (2018). Supplementary data for the article: Božinovski, D. M.; Petrović, P. V.; Belić, M. R.; Zarić, S. D. Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids That Interact with Graphene. ChemPhysChem 2018, 19 (10), 1226–1233. https://doi.org/10.1002/cphc.201700847. in Chemphyschem
Wiley-V C H Verlag Gmbh, Weinheim..
https://hdl.handle.net/21.15107/rcub_cherry_3227

Božinovski DM, Petrović P, Belić MR, Zarić SD. Supplementary data for the article: Božinovski, D. M.; Petrović, P. V.; Belić, M. R.; Zarić, S. D. Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids That Interact with Graphene. ChemPhysChem 2018, 19 (10), 1226–1233. https://doi.org/10.1002/cphc.201700847. in Chemphyschem. 2018;.
https://hdl.handle.net/21.15107/rcub_cherry_3227 .

Božinovski, Dragana M., Petrović, Predrag, Belić, Milivoj R., Zarić, Snežana D., "Supplementary data for the article: Božinovski, D. M.; Petrović, P. V.; Belić, M. R.; Zarić, S. D. Insight into the Interactions of Amyloid β-Sheets with Graphene Flakes: Scrutinizing the Role of Aromatic Residues in Amyloids That Interact with Graphene. ChemPhysChem 2018, 19 (10), 1226–1233. https://doi.org/10.1002/cphc.201700847" in Chemphyschem (2018),
https://hdl.handle.net/21.15107/rcub_cherry_3227 .

TY  - JOUR
AU  - Ninković, Dragan
AU  - Malenov, Dušan P.
AU  - Petrović, Predrag
AU  - Brothers, Edward N.
AU  - Niu, Shuqiang
AU  - Hall, Michael B.
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3118
AB  - The role of aromatic and nonaromatic amino acids in amyloid formation has been elucidated by calculating interaction energies between -sheets in amyloid model systems using density functional theory (B3LYP-D3/6-31G*). The model systems were based on experimental crystal structures of two types of amyloids: (1)with aromatic amino acids, and (2)without aromatic amino acids. Data show that these two types of amyloids have similar interaction energies, supporting experimental findings that aromatic amino acids are not essential for amyloid formation. However, different factors contribute to the stability of these two types of amyloids. In the former, the presence of aromatic amino acids significantly contributes to the strength of interactions between side chains; interactions between aromatic and aliphatic side chains are the strongest, followed by aromatic-aromatic interactions, while aliphatic-aliphatic interactions are the weakest. In the latter, that is, the amyloids without aromatic residues, stability is provided by interactions of aliphatic side chains with the backbone and, in some cases, by hydrogen bonds.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemistry - A European Journal
T1  - Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids
VL  - 23
IS  - 46
SP  - 11046
EP  - 11053
DO  - 10.1002/chem.201701351
ER  - 

@article{
author = "Ninković, Dragan and Malenov, Dušan P. and Petrović, Predrag and Brothers, Edward N. and Niu, Shuqiang and Hall, Michael B. and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2017",
abstract = "The role of aromatic and nonaromatic amino acids in amyloid formation has been elucidated by calculating interaction energies between -sheets in amyloid model systems using density functional theory (B3LYP-D3/6-31G*). The model systems were based on experimental crystal structures of two types of amyloids: (1)with aromatic amino acids, and (2)without aromatic amino acids. Data show that these two types of amyloids have similar interaction energies, supporting experimental findings that aromatic amino acids are not essential for amyloid formation. However, different factors contribute to the stability of these two types of amyloids. In the former, the presence of aromatic amino acids significantly contributes to the strength of interactions between side chains; interactions between aromatic and aliphatic side chains are the strongest, followed by aromatic-aromatic interactions, while aliphatic-aliphatic interactions are the weakest. In the latter, that is, the amyloids without aromatic residues, stability is provided by interactions of aliphatic side chains with the backbone and, in some cases, by hydrogen bonds.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemistry - A European Journal",
title = "Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids",
volume = "23",
number = "46",
pages = "11046-11053",
doi = "10.1002/chem.201701351"
}

Ninković, D., Malenov, D. P., Petrović, P., Brothers, E. N., Niu, S., Hall, M. B., Belić, M. R.,& Zarić, S. D.. (2017). Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids. in Chemistry - A European Journal
Wiley-V C H Verlag Gmbh, Weinheim., 23(46), 11046-11053.
https://doi.org/10.1002/chem.201701351

Ninković D, Malenov DP, Petrović P, Brothers EN, Niu S, Hall MB, Belić MR, Zarić SD. Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids. in Chemistry - A European Journal. 2017;23(46):11046-11053.
doi:10.1002/chem.201701351 .

Ninković, Dragan, Malenov, Dušan P., Petrović, Predrag, Brothers, Edward N., Niu, Shuqiang, Hall, Michael B., Belić, Milivoj R., Zarić, Snežana D., "Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids" in Chemistry - A European Journal, 23, no. 46 (2017):11046-11053,
https://doi.org/10.1002/chem.201701351 . .

TY  - DATA
AU  - Ninković, Dragan
AU  - Malenov, Dušan P.
AU  - Petrović, Predrag
AU  - Brothers, Edward N.
AU  - Niu, Shuqiang
AU  - Hall, Michael B.
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/3119
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemistry - A European Journal
T1  - Supplementary data for article:   Ninković, D. B.; Malenov, D. P.; Petrović, P. V.; Brothers, E. N.; Niu, S.; Hall, M. B.; Belić, M. R.; Zarić, S. D. Unexpected Importance of Aromatic–Aliphatic and Aliphatic Side Chain–Backbone Interactions in the Stability of Amyloids. Chemistry - A European Journal 2017, 23 (46), 11046–11053. https://doi.org/10.1002/chem.201701351
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3119
ER  - 

@misc{
author = "Ninković, Dragan and Malenov, Dušan P. and Petrović, Predrag and Brothers, Edward N. and Niu, Shuqiang and Hall, Michael B. and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2017",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemistry - A European Journal",
title = "Supplementary data for article:   Ninković, D. B.; Malenov, D. P.; Petrović, P. V.; Brothers, E. N.; Niu, S.; Hall, M. B.; Belić, M. R.; Zarić, S. D. Unexpected Importance of Aromatic–Aliphatic and Aliphatic Side Chain–Backbone Interactions in the Stability of Amyloids. Chemistry - A European Journal 2017, 23 (46), 11046–11053. https://doi.org/10.1002/chem.201701351",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3119"
}

Ninković, D., Malenov, D. P., Petrović, P., Brothers, E. N., Niu, S., Hall, M. B., Belić, M. R.,& Zarić, S. D.. (2017). Supplementary data for article:   Ninković, D. B.; Malenov, D. P.; Petrović, P. V.; Brothers, E. N.; Niu, S.; Hall, M. B.; Belić, M. R.; Zarić, S. D. Unexpected Importance of Aromatic–Aliphatic and Aliphatic Side Chain–Backbone Interactions in the Stability of Amyloids. Chemistry - A European Journal 2017, 23 (46), 11046–11053. https://doi.org/10.1002/chem.201701351. in Chemistry - A European Journal
Wiley-V C H Verlag Gmbh, Weinheim..
https://hdl.handle.net/21.15107/rcub_cherry_3119

Ninković D, Malenov DP, Petrović P, Brothers EN, Niu S, Hall MB, Belić MR, Zarić SD. Supplementary data for article:   Ninković, D. B.; Malenov, D. P.; Petrović, P. V.; Brothers, E. N.; Niu, S.; Hall, M. B.; Belić, M. R.; Zarić, S. D. Unexpected Importance of Aromatic–Aliphatic and Aliphatic Side Chain–Backbone Interactions in the Stability of Amyloids. Chemistry - A European Journal 2017, 23 (46), 11046–11053. https://doi.org/10.1002/chem.201701351. in Chemistry - A European Journal. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3119 .

Ninković, Dragan, Malenov, Dušan P., Petrović, Predrag, Brothers, Edward N., Niu, Shuqiang, Hall, Michael B., Belić, Milivoj R., Zarić, Snežana D., "Supplementary data for article:   Ninković, D. B.; Malenov, D. P.; Petrović, P. V.; Brothers, E. N.; Niu, S.; Hall, M. B.; Belić, M. R.; Zarić, S. D. Unexpected Importance of Aromatic–Aliphatic and Aliphatic Side Chain–Backbone Interactions in the Stability of Amyloids. Chemistry - A European Journal 2017, 23 (46), 11046–11053. https://doi.org/10.1002/chem.201701351" in Chemistry - A European Journal (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3119 .

TY  - JOUR
AU  - Ninković, Dragan
AU  - Malenov, Dušan P.
AU  - Petrović, Predrag
AU  - Brothers, Edward N.
AU  - Niu, Shuqiang
AU  - Hall, Michael B.
AU  - Belić, Milivoj R.
AU  - Zarić, Snežana D.
PY  - 2017
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/2506
AB  - The role of aromatic and nonaromatic amino acids in amyloid formation has been elucidated by calculating interaction energies between -sheets in amyloid model systems using density functional theory (B3LYP-D3/6-31G*). The model systems were based on experimental crystal structures of two types of amyloids: (1)with aromatic amino acids, and (2)without aromatic amino acids. Data show that these two types of amyloids have similar interaction energies, supporting experimental findings that aromatic amino acids are not essential for amyloid formation. However, different factors contribute to the stability of these two types of amyloids. In the former, the presence of aromatic amino acids significantly contributes to the strength of interactions between side chains; interactions between aromatic and aliphatic side chains are the strongest, followed by aromatic-aromatic interactions, while aliphatic-aliphatic interactions are the weakest. In the latter, that is, the amyloids without aromatic residues, stability is provided by interactions of aliphatic side chains with the backbone and, in some cases, by hydrogen bonds.
PB  - Wiley-V C H Verlag Gmbh, Weinheim
T2  - Chemistry. A European Journal
T1  - Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids
VL  - 23
IS  - 46
SP  - 11046
EP  - 11053
DO  - 10.1002/chem.201701351
ER  - 

@article{
author = "Ninković, Dragan and Malenov, Dušan P. and Petrović, Predrag and Brothers, Edward N. and Niu, Shuqiang and Hall, Michael B. and Belić, Milivoj R. and Zarić, Snežana D.",
year = "2017",
abstract = "The role of aromatic and nonaromatic amino acids in amyloid formation has been elucidated by calculating interaction energies between -sheets in amyloid model systems using density functional theory (B3LYP-D3/6-31G*). The model systems were based on experimental crystal structures of two types of amyloids: (1)with aromatic amino acids, and (2)without aromatic amino acids. Data show that these two types of amyloids have similar interaction energies, supporting experimental findings that aromatic amino acids are not essential for amyloid formation. However, different factors contribute to the stability of these two types of amyloids. In the former, the presence of aromatic amino acids significantly contributes to the strength of interactions between side chains; interactions between aromatic and aliphatic side chains are the strongest, followed by aromatic-aromatic interactions, while aliphatic-aliphatic interactions are the weakest. In the latter, that is, the amyloids without aromatic residues, stability is provided by interactions of aliphatic side chains with the backbone and, in some cases, by hydrogen bonds.",
publisher = "Wiley-V C H Verlag Gmbh, Weinheim",
journal = "Chemistry. A European Journal",
title = "Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids",
volume = "23",
number = "46",
pages = "11046-11053",
doi = "10.1002/chem.201701351"
}

Ninković, D., Malenov, D. P., Petrović, P., Brothers, E. N., Niu, S., Hall, M. B., Belić, M. R.,& Zarić, S. D.. (2017). Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids. in Chemistry. A European Journal
Wiley-V C H Verlag Gmbh, Weinheim., 23(46), 11046-11053.
https://doi.org/10.1002/chem.201701351

Ninković D, Malenov DP, Petrović P, Brothers EN, Niu S, Hall MB, Belić MR, Zarić SD. Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids. in Chemistry. A European Journal. 2017;23(46):11046-11053.
doi:10.1002/chem.201701351 .

Ninković, Dragan, Malenov, Dušan P., Petrović, Predrag, Brothers, Edward N., Niu, Shuqiang, Hall, Michael B., Belić, Milivoj R., Zarić, Snežana D., "Unexpected Importance of Aromatic-Aliphatic and Aliphatic Side Chain-Backbone Interactions in the Stability of Amyloids" in Chemistry. A European Journal, 23, no. 46 (2017):11046-11053,
https://doi.org/10.1002/chem.201701351 . .

TY  - 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 . .

TY  - DATA
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/123456789/3079
PB  - Amer Chemical Soc, Washington
T2  - Crystal Growth and Design
T1  - Supplementary data for article:  Stanković, I. M.; Božinovski, D. M.; Brothers, E. N.; Belić, M. R.; Hall, M. B.; Zarić, S. D. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. Crystal Growth and Design 2017, 17 (12), 6353–6362. https://doi.org/10.1021/acs.cgd.7b01035
UR  - https://hdl.handle.net/21.15107/rcub_cherry_3079
ER  - 

@misc{
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",
publisher = "Amer Chemical Soc, Washington",
journal = "Crystal Growth and Design",
title = "Supplementary data for article:  Stanković, I. M.; Božinovski, D. M.; Brothers, E. N.; Belić, M. R.; Hall, M. B.; Zarić, S. D. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. Crystal Growth and Design 2017, 17 (12), 6353–6362. https://doi.org/10.1021/acs.cgd.7b01035",
url = "https://hdl.handle.net/21.15107/rcub_cherry_3079"
}

Stanković, I. M., Božinovski, D. M., Brothers, E. N., Belić, M. R., Hall, M. B.,& Zarić, S. D.. (2017). Supplementary data for article:  Stanković, I. M.; Božinovski, D. M.; Brothers, E. N.; Belić, M. R.; Hall, M. B.; Zarić, S. D. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. Crystal Growth and Design 2017, 17 (12), 6353–6362. https://doi.org/10.1021/acs.cgd.7b01035. in Crystal Growth and Design
Amer Chemical Soc, Washington..
https://hdl.handle.net/21.15107/rcub_cherry_3079

Stanković IM, Božinovski DM, Brothers EN, Belić MR, Hall MB, Zarić SD. Supplementary data for article:  Stanković, I. M.; Božinovski, D. M.; Brothers, E. N.; Belić, M. R.; Hall, M. B.; Zarić, S. D. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. Crystal Growth and Design 2017, 17 (12), 6353–6362. https://doi.org/10.1021/acs.cgd.7b01035. in Crystal Growth and Design. 2017;.
https://hdl.handle.net/21.15107/rcub_cherry_3079 .

Stanković, Ivana M., Božinovski, Dragana M., Brothers, Edward N., Belić, Milivoj R., Hall, Michael B., Zarić, Snežana D., "Supplementary data for article:  Stanković, I. M.; Božinovski, D. M.; Brothers, E. N.; Belić, M. R.; Hall, M. B.; Zarić, S. D. Interactions of Aromatic Residues in Amyloids: A Survey of Protein Data Bank Crystallographic Data. Crystal Growth and Design 2017, 17 (12), 6353–6362. https://doi.org/10.1021/acs.cgd.7b01035" in Crystal Growth and Design (2017),
https://hdl.handle.net/21.15107/rcub_cherry_3079 .