TY  - JOUR
AU  - Ninković, Dragan
AU  - Andrić, Jelena M.
AU  - Malkov, Sasa N.
AU  - Zarić, Snežana D.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1783
AB  - The data from protein structures from the Protein Data Bank and quantumchemical calculations indicate the importance of aromatic-aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5-5.0), while the calculations show substantially strong interactions, of about -2.0 kcal mol(-1).
PB  - Royal Soc Chemistry, Cambridge
T2  - Physical Chemistry Chemical Physics
T1  - What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface
VL  - 16
IS  - 23
SP  - 11173
EP  - 11177
DO  - 10.1039/c3cp54474e
ER  - 

@article{
author = "Ninković, Dragan and Andrić, Jelena M. and Malkov, Sasa N. and Zarić, Snežana D.",
year = "2014",
abstract = "The data from protein structures from the Protein Data Bank and quantumchemical calculations indicate the importance of aromatic-aromatic interactions at large horizontal displacements (offsets). The protein stacking interactions of the phenylalanine residue show preference for large offsets (3.5-5.0), while the calculations show substantially strong interactions, of about -2.0 kcal mol(-1).",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Physical Chemistry Chemical Physics",
title = "What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface",
volume = "16",
number = "23",
pages = "11173-11177",
doi = "10.1039/c3cp54474e"
}

Ninković, D., Andrić, J. M., Malkov, S. N.,& Zarić, S. D.. (2014). What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface. in Physical Chemistry Chemical Physics
Royal Soc Chemistry, Cambridge., 16(23), 11173-11177.
https://doi.org/10.1039/c3cp54474e

Ninković D, Andrić JM, Malkov SN, Zarić SD. What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface. in Physical Chemistry Chemical Physics. 2014;16(23):11173-11177.
doi:10.1039/c3cp54474e .

Ninković, Dragan, Andrić, Jelena M., Malkov, Sasa N., Zarić, Snežana D., "What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface" in Physical Chemistry Chemical Physics, 16, no. 23 (2014):11173-11177,
https://doi.org/10.1039/c3cp54474e . .

TY  - JOUR
AU  - Janjić, Goran V.
AU  - Malkov, Sasa N.
AU  - Živković, Miodrag V.
AU  - Zarić, Snežana D.
PY  - 2014
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/1871
AB  - The distribution of water molecules around aromatic rings in the protein structures and crystal structures of small molecules shows quite a small number of the strongest OH-pi interactions, a larger number of parallel interactions, and the largest number of the weakest CH-O interactions.
PB  - Royal Soc Chemistry, Cambridge
T2  - Physical Chemistry Chemical Physics
T1  - What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?
VL  - 16
IS  - 43
SP  - 23549
EP  - 23553
DO  - 10.1039/c4cp00929k
ER  - 

@article{
author = "Janjić, Goran V. and Malkov, Sasa N. and Živković, Miodrag V. and Zarić, Snežana D.",
year = "2014",
abstract = "The distribution of water molecules around aromatic rings in the protein structures and crystal structures of small molecules shows quite a small number of the strongest OH-pi interactions, a larger number of parallel interactions, and the largest number of the weakest CH-O interactions.",
publisher = "Royal Soc Chemistry, Cambridge",
journal = "Physical Chemistry Chemical Physics",
title = "What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?",
volume = "16",
number = "43",
pages = "23549-23553",
doi = "10.1039/c4cp00929k"
}

Janjić, G. V., Malkov, S. N., Živković, M. V.,& Zarić, S. D.. (2014). What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?. in Physical Chemistry Chemical Physics
Royal Soc Chemistry, Cambridge., 16(43), 23549-23553.
https://doi.org/10.1039/c4cp00929k

Janjić GV, Malkov SN, Živković MV, Zarić SD. What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?. in Physical Chemistry Chemical Physics. 2014;16(43):23549-23553.
doi:10.1039/c4cp00929k .

Janjić, Goran V., Malkov, Sasa N., Živković, Miodrag V., Zarić, Snežana D., "What are preferred water-aromatic interactions in proteins and crystal structures of small molecules?" in Physical Chemistry Chemical Physics, 16, no. 43 (2014):23549-23553,
https://doi.org/10.1039/c4cp00929k . .

TY  - JOUR
AU  - Malkov, Sasa N.
AU  - Živković, Miodrag V.
AU  - Beljanski, Milos V.
AU  - Hall, Michael B.
AU  - Zarić, Snežana D.
PY  - 2008
UR  - https://cherry.chem.bg.ac.rs/handle/123456789/953
AB  - The correlation between the primary and secondary structures of proteins was analysed using a large data set from the Protein Data Bank. Clear preferences of amino acids towards certain secondary structures classify amino acids into four groups: alpha-helix preferrers, strand preferrers, turn and bend preferrers, and His and Cys (the latter two amino acids show no clear preference for any secondary structure). Amino acids in the same group have similar structural characteristics at their C beta and C gamma atoms that predicts their preference for a particular secondary structure. All alpha-helix preferrers have neither polar heteroatoms on C beta and C gamma atoms, nor branching or aromatic group on the C beta atom. All strand preferrers have aromatic groups or branching groups on the C beta atom. All turn and bend preferrers have a polar heteroatom on the C beta or C gamma atoms or do not have a C beta atom at all. These new rules could be helpful in making predictions about non-natural amino acids.
PB  - Springer, New York
T2  - Journal of Molecular Modeling
T1  - A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure
VL  - 14
IS  - 8
SP  - 769
EP  - 775
DO  - 10.1007/s00894-008-0313-0
ER  - 

@article{
author = "Malkov, Sasa N. and Živković, Miodrag V. and Beljanski, Milos V. and Hall, Michael B. and Zarić, Snežana D.",
year = "2008",
abstract = "The correlation between the primary and secondary structures of proteins was analysed using a large data set from the Protein Data Bank. Clear preferences of amino acids towards certain secondary structures classify amino acids into four groups: alpha-helix preferrers, strand preferrers, turn and bend preferrers, and His and Cys (the latter two amino acids show no clear preference for any secondary structure). Amino acids in the same group have similar structural characteristics at their C beta and C gamma atoms that predicts their preference for a particular secondary structure. All alpha-helix preferrers have neither polar heteroatoms on C beta and C gamma atoms, nor branching or aromatic group on the C beta atom. All strand preferrers have aromatic groups or branching groups on the C beta atom. All turn and bend preferrers have a polar heteroatom on the C beta or C gamma atoms or do not have a C beta atom at all. These new rules could be helpful in making predictions about non-natural amino acids.",
publisher = "Springer, New York",
journal = "Journal of Molecular Modeling",
title = "A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure",
volume = "14",
number = "8",
pages = "769-775",
doi = "10.1007/s00894-008-0313-0"
}

Malkov, S. N., Živković, M. V., Beljanski, M. V., Hall, M. B.,& Zarić, S. D.. (2008). A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure. in Journal of Molecular Modeling
Springer, New York., 14(8), 769-775.
https://doi.org/10.1007/s00894-008-0313-0

Malkov SN, Živković MV, Beljanski MV, Hall MB, Zarić SD. A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure. in Journal of Molecular Modeling. 2008;14(8):769-775.
doi:10.1007/s00894-008-0313-0 .

Malkov, Sasa N., Živković, Miodrag V., Beljanski, Milos V., Hall, Michael B., Zarić, Snežana D., "A reexamination of the propensities of amino acids towards a particular secondary structure: classification of amino acids based on their chemical structure" in Journal of Molecular Modeling, 14, no. 8 (2008):769-775,
https://doi.org/10.1007/s00894-008-0313-0 . .