TY  - JOUR
AU  - Janjić, Goran
AU  - Malkov, Sasa N
AU  - Zivkovic, Miodrag V
AU  - Zarić, Snežana D.
PY  - 2014
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/1404
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 and Malkov, Sasa N and Zivkovic, 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., Malkov, S. N., Zivkovic, 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 G, Malkov SN, Zivkovic 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, Malkov, Sasa N, Zivkovic, 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, Saga N.
AU  - Zivkovic, Miodrag V.
AU  - Beljanski, Milos V.
AU  - Stojanović, Srđan
AU  - Zarić, Snežana D.
PY  - 2009
UR  - https://cer.ihtm.bg.ac.rs/handle/123456789/550
AB  - Using the data from Protein Data Bank the correlations of primary and secondary structures of proteins were analyzed. The correlation values of the amino acids and the eight secondary structure types were calculated, where the position of the amino acid and the position in sequence with the particular secondary structure differ at most 25. The diagrams describing these results indicate that correlations are significant at distances between -9 and 10. The results show that the substituents on C beta or C gamma atoms of amino acid play major role in their preference for particular secondary structure at the same position in the sequence, while the polarity of amino acid has significant influence on alpha-helices and strands at some distance in the sequence. The diagrams corresponding to polar amino acids are noticeably asymmetric. The diagrams point out the exchangeability of residues in the proteins; the amino acids with similar diagrams have similar local folding requirements.
PB  - Springer, New York
T2  - Protein Journal
T1  - A Reexamination of Correlations of Amino Acids with Particular Secondary Structures
VL  - 28
IS  - 2
SP  - 74
EP  - 86
DO  - 10.1007/s10930-009-9166-3
ER  - 

@article{
author = "Malkov, Saga N. and Zivkovic, Miodrag V. and Beljanski, Milos V. and Stojanović, Srđan and Zarić, Snežana D.",
year = "2009",
abstract = "Using the data from Protein Data Bank the correlations of primary and secondary structures of proteins were analyzed. The correlation values of the amino acids and the eight secondary structure types were calculated, where the position of the amino acid and the position in sequence with the particular secondary structure differ at most 25. The diagrams describing these results indicate that correlations are significant at distances between -9 and 10. The results show that the substituents on C beta or C gamma atoms of amino acid play major role in their preference for particular secondary structure at the same position in the sequence, while the polarity of amino acid has significant influence on alpha-helices and strands at some distance in the sequence. The diagrams corresponding to polar amino acids are noticeably asymmetric. The diagrams point out the exchangeability of residues in the proteins; the amino acids with similar diagrams have similar local folding requirements.",
publisher = "Springer, New York",
journal = "Protein Journal",
title = "A Reexamination of Correlations of Amino Acids with Particular Secondary Structures",
volume = "28",
number = "2",
pages = "74-86",
doi = "10.1007/s10930-009-9166-3"
}

Malkov, S. N., Zivkovic, M. V., Beljanski, M. V., Stojanović, S.,& Zarić, S. D.. (2009). A Reexamination of Correlations of Amino Acids with Particular Secondary Structures. in Protein Journal
Springer, New York., 28(2), 74-86.
https://doi.org/10.1007/s10930-009-9166-3

Malkov SN, Zivkovic MV, Beljanski MV, Stojanović S, Zarić SD. A Reexamination of Correlations of Amino Acids with Particular Secondary Structures. in Protein Journal. 2009;28(2):74-86.
doi:10.1007/s10930-009-9166-3 .

Malkov, Saga N., Zivkovic, Miodrag V., Beljanski, Milos V., Stojanović, Srđan, Zarić, Snežana D., "A Reexamination of Correlations of Amino Acids with Particular Secondary Structures" in Protein Journal, 28, no. 2 (2009):74-86,
https://doi.org/10.1007/s10930-009-9166-3 . .