PENGARUH MUTASI TYROSINE TERHADAP PERUBAHAN ENERGI BEBAS GIBBS PADA PROTEIN FOTOAKTIF KUNING
Low-barrier hydrogen bond (LBHB) formation on photoactive yellow protein (PYP) has been investigated. Previous X-ray crystallography and neutron crystallography study show that hydrogen bond between the aromatic oxygen of chromophore p-coumaric acid (pCA) and carboxyl hydogen of glutamic acid (E46)...
محفوظ في:
| المؤلفون الرئيسيون: | , |
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| التنسيق: | Theses and Dissertations NonPeerReviewed |
| منشور في: |
[Yogyakarta] : Universitas Gadjah Mada
2011
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| الموضوعات: | |
| الوصول للمادة أونلاين: | https://repository.ugm.ac.id/88866/ http://etd.ugm.ac.id/index.php?mod=penelitian_detail&sub=PenelitianDetail&act=view&typ=html&buku_id=50533 |
| الوسوم: |
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| الملخص: | Low-barrier hydrogen bond (LBHB) formation on photoactive yellow
protein (PYP) has been investigated. Previous X-ray crystallography and neutron
crystallography study show that hydrogen bond between the aromatic oxygen of
chromophore p-coumaric acid (pCA) and carboxyl hydogen of glutamic acid
(E46) was a LBHB. Assuming that proton affinity matching dominates the
formation of LBHB, we used tyrosine, instead of pCA, because of similarity of
the chemical properties of pCA and tyrosine. Information about protein stability to
form the special type of hydrogen bond was analyzed from secondary structure of
proteins using circular dichroism (CD) method. Here, we found that value of
Gibbs free energy difference of mutant type is lower than the wild-type, 21,70 ±
0,02 kJ/mol and 24 ± 2 kJ/mol for mutant and wild-type in pH balance condition,
respectively. These results suggest that mutant is no more stable than the wildtype.
The loss of stability for amino acid replacement appears to be due to the loss
of hydrogen bonding and unfavorable contacts that account for the destabilization. |
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