THE ROLE OF HIS 16, TYR 82 AND TRP 86 IN COLOR SHIFT, ACTIVITY AND THERMOSTABILITY OF AEQUORIN PHOTOPROTEIN

Q: How can I download an article?

To download an article from SID, first log in to the site, search for the article title, and click on the 'Download Article' option.

Q: How can I download an ISI article?

To download an ISI article on SID, enter the keyword or article title in the search bar, view the relevant results, click on the desired article, and select the 'Download Article' option.

Q: How can I access the SID database?

To access the SID database, visit SID.ir, create an account, and log in to access scientific resources.

Q: Is downloading articles from SID free?

Some articles on SID are available for free, while others require payment. Details are specified on the article's page.

GHANBARTALAB F.; ZEINODDINI M.; HOSSEINKHANI S.; ESMAEILNEZHAD M.; HOSSEINI S.E.; LAALI M.

مرکز اطلاعات علمی Scientific Information Database (SID) - Trusted Source for Research and Academic Resources

Journal Paper

Paper Information

Journal: Iranian South Medical Journal Year:2015 | Volume:18 | Issue:1 Page(s): 37-45

Download Full-Text

Persian Verion

View:

2,106

Download:

Cites:

Information Journal Paper

Title

THE ROLE OF HIS 16, TYR 82 AND TRP 86 IN COLOR SHIFT, ACTIVITY AND THERMOSTABILITY OF AEQUORIN PHOTOPROTEIN

Author(s)

Keywords

AEQUORINQ2

MUTATIONQ2

COLOR SHIFTQ2

THERMO STABILITYQ2

Abstract

Background: AEQUORIN is a calcium sensitive photoprotein composed of apoAEQUORIN (189 amino acid), oxygen and coelenterazine (imidazopyrazine chromophore). Activity of this photoprotein in calcium presence is blue photon emission (469 nm). Studies have shown that three amino acids H16, Y82, W86 are involved in COLOR SHIFT and activity of AEQUORIN. In this work, for study of structural-functional relationship, combinational mutant was used for determine of the interest places importance in single and combination state.Materials and Methods: Using site directed mutagenesis, the single and multiple MUTATIONs done in plasmid and mutated AEQUORIN in single and multiple states were prepared. Next, THERMO STABILITY, activity and COLOR SHIFT of produced protein determined using luminometer and spectrofluorimetry, respectively.Results: We found that W86 and H16 play a more critical role in COLOR SHIFT and activity respectively. In addition, MUTATION of W86 provides better term stability compared to other MUTATIONs.Conclusion: This investigation was shown that the role of W86 in AEQUORIN shift light and THERMO STABILITY is better than Y82 and H16 and this mutant could be used for effective protein production in sensor and other applications.

Cites

No record.

References

No record.

Cite

APA: Copy

GHANBARTALAB, F., ZEINODDINI, M., HOSSEINKHANI, S., ESMAEILNEZHAD, M., HOSSEINI, S.E., & LAALI, M.. (2015). THE ROLE OF HIS 16, TYR 82 AND TRP 86 IN COLOR SHIFT, ACTIVITY AND THERMOSTABILITY OF AEQUORIN PHOTOPROTEIN. IRANIAN SOUTH MEDICAL JOURNAL (ISMJ), 18(1), 37-45. SID. https://sid.ir/paper/33718/en

Vancouver: Copy

GHANBARTALAB F., ZEINODDINI M., HOSSEINKHANI S., ESMAEILNEZHAD M., HOSSEINI S.E., LAALI M.. THE ROLE OF HIS 16, TYR 82 AND TRP 86 IN COLOR SHIFT, ACTIVITY AND THERMOSTABILITY OF AEQUORIN PHOTOPROTEIN. IRANIAN SOUTH MEDICAL JOURNAL (ISMJ)[Internet]. 2015;18(1):37-45. Available from: https://sid.ir/paper/33718/en

IEEE: Copy

F. GHANBARTALAB, M. ZEINODDINI, S. HOSSEINKHANI, M. ESMAEILNEZHAD, S.E. HOSSEINI, and M. LAALI, “THE ROLE OF HIS 16, TYR 82 AND TRP 86 IN COLOR SHIFT, ACTIVITY AND THERMOSTABILITY OF AEQUORIN PHOTOPROTEIN,” IRANIAN SOUTH MEDICAL JOURNAL (ISMJ), vol. 18, no. 1, pp. 37–45, 2015, [Online]. Available: https://sid.ir/paper/33718/en

Related Journal Papers