Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins
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Приказ свих података о документуАпстракт
Structures of porphyrin-containing proteins from the Protein Data Bank (PDB) Select January 2007, were
searched in order to find and systematically characterize hydrogen bonds and hydrophobic interactions of porphyrins in
proteins. The results revealed that every porphyrin is involved in at least one hydrogen bond, most of the porphyrins form
several, while some of them form up to thirteen hydrogen bonds. In most of the hydrogen bonds propionate groups of
porphyrins interact with side-chains of residues. The most frequently observed donor is side chain of arginine. Histidine,
lysine, threonine, serine and tyrozine form substantial number of hydrogen bonds too. The study has revealed that
hydrophobic interactions are common between porphyrin and protein. Side-chains hydrophobic interactions are more
frequent than those with backbone. The average conservation score for the amino acids making hydrogen bonds (7.2) and
hydrophobic interactions (7.3) is statistically significantly hi...gher than for the amino acids that are not involved in
noncovalent interactions (5.7) with the porphyrin, indicating importance of hydrogen bonds and hydrophobic interactions
with the porphyrin.
Кључне речи:
Hydrogen bond / hydrophobic interactions / porphyrin / rotein stability / onservation scoreИзвор:
The Open Structural Biology Journal, 2009, 3, 34-41Издавач:
- Bentham Open
Финансирање / пројекти:
- Проучавање односа реактивности, нековалентних интеракција и структуре молекула и моделовање хемијских система (RS-MESTD-MPN2006-2010-142037)
Институција/група
IHTMTY - JOUR AU - Stojanović, Srđan AU - Zarić, Snežana PY - 2009 UR - https://cer.ihtm.bg.ac.rs/handle/123456789/6511 AB - Structures of porphyrin-containing proteins from the Protein Data Bank (PDB) Select January 2007, were searched in order to find and systematically characterize hydrogen bonds and hydrophobic interactions of porphyrins in proteins. The results revealed that every porphyrin is involved in at least one hydrogen bond, most of the porphyrins form several, while some of them form up to thirteen hydrogen bonds. In most of the hydrogen bonds propionate groups of porphyrins interact with side-chains of residues. The most frequently observed donor is side chain of arginine. Histidine, lysine, threonine, serine and tyrozine form substantial number of hydrogen bonds too. The study has revealed that hydrophobic interactions are common between porphyrin and protein. Side-chains hydrophobic interactions are more frequent than those with backbone. The average conservation score for the amino acids making hydrogen bonds (7.2) and hydrophobic interactions (7.3) is statistically significantly higher than for the amino acids that are not involved in noncovalent interactions (5.7) with the porphyrin, indicating importance of hydrogen bonds and hydrophobic interactions with the porphyrin. PB - Bentham Open T2 - The Open Structural Biology Journal T1 - Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins VL - 3 SP - 34 EP - 41 DO - 10.2174/1874199100903010034 ER -
@article{ author = "Stojanović, Srđan and Zarić, Snežana", year = "2009", abstract = "Structures of porphyrin-containing proteins from the Protein Data Bank (PDB) Select January 2007, were searched in order to find and systematically characterize hydrogen bonds and hydrophobic interactions of porphyrins in proteins. The results revealed that every porphyrin is involved in at least one hydrogen bond, most of the porphyrins form several, while some of them form up to thirteen hydrogen bonds. In most of the hydrogen bonds propionate groups of porphyrins interact with side-chains of residues. The most frequently observed donor is side chain of arginine. Histidine, lysine, threonine, serine and tyrozine form substantial number of hydrogen bonds too. The study has revealed that hydrophobic interactions are common between porphyrin and protein. Side-chains hydrophobic interactions are more frequent than those with backbone. The average conservation score for the amino acids making hydrogen bonds (7.2) and hydrophobic interactions (7.3) is statistically significantly higher than for the amino acids that are not involved in noncovalent interactions (5.7) with the porphyrin, indicating importance of hydrogen bonds and hydrophobic interactions with the porphyrin.", publisher = "Bentham Open", journal = "The Open Structural Biology Journal", title = "Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins", volume = "3", pages = "34-41", doi = "10.2174/1874199100903010034" }
Stojanović, S.,& Zarić, S.. (2009). Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins. in The Open Structural Biology Journal Bentham Open., 3, 34-41. https://doi.org/10.2174/1874199100903010034
Stojanović S, Zarić S. Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins. in The Open Structural Biology Journal. 2009;3:34-41. doi:10.2174/1874199100903010034 .
Stojanović, Srđan, Zarić, Snežana, "Hydrogen bonds and hydrophobic interactions of porphyrins in porphyrin-containing proteins" in The Open Structural Biology Journal, 3 (2009):34-41, https://doi.org/10.2174/1874199100903010034 . .