A Reexamination of Correlations of Amino Acids with Particular Secondary Structures
Само за регистроване кориснике
2009
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
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.
Кључне речи:
Protein / Amino acid / Protein secondary structure / Statistical correlationИзвор:
Protein Journal, 2009, 28, 2, 74-86Издавач:
- Springer, New York
Финансирање / пројекти:
- Аутоматско резоновање и напредне обраде великих количина података и текста (RS-MESTD-MPN2006-2010-144030)
- Проучавање односа реактивности, нековалентних интеракција и структуре молекула и моделовање хемијских система (RS-MESTD-MPN2006-2010-142037)
DOI: 10.1007/s10930-009-9166-3
ISSN: 1572-3887
PubMed: 19280326
WoS: 000266563000003
Scopus: 2-s2.0-63449106826
Институција/група
IHTMTY - 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 . .