What are the preferred horizontal displacements of aromatic-aromatic interactions in proteins? Comparison with the calculated benzene-benzene potential energy surface
Само за регистроване кориснике
2014
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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).
Извор:
Physical Chemistry Chemical Physics, 2014, 16, 23, 11173-11177Издавач:
- Royal Soc Chemistry, Cambridge
Финансирање / пројекти:
- Нековалентне интеракције pi-система и њихова улога у молекулском препознавању (RS-MESTD-Basic Research (BR or ON)-172065)
- AVH foundation
DOI: 10.1039/c3cp54474e
ISSN: 1463-9076
PubMed: 24805772
WoS: 000336796800008
Scopus: 2-s2.0-84901267472
Институција/група
Hemijski fakultet / Faculty of ChemistryTY - 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 . .