کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
1987567 1540290 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Dissecting the key residues crucial for the species-specific thermostability of muscle-type creatine kinase
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی زیست شیمی
پیش نمایش صفحه اول مقاله
Dissecting the key residues crucial for the species-specific thermostability of muscle-type creatine kinase
چکیده انگلیسی

Species-specific protein thermal stability is closely correlated to the living conditions of the organism, especially to its body temperature. In this research, human and zebrafish muscle-type creatine kinases (MMCKs) were taken as model proteins to investigate the molecular adaptation of proteins in poikilothermal and homoiothermal animals. Both the optimal temperature for catalysis and the thermal stability of human MMCK was much higher than those of zebrafish MMCK. Sequence alignment identified 9 amino acid variations conserved in either the teleost MMCKs or the mammal and electric ray MMCKs. Bidirectional mutations were performed to find the residues with beneficial mutations. The results showed that two residues close to the dimer interface of MMCK, the 46th and 146th residue, were crucial for species-specific thermal stability.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: International Journal of Biological Macromolecules - Volume 47, Issue 3, 1 October 2010, Pages 366–370
نویسندگان
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