Abstract：
:The stability of the structure of sperm whale metmyoglobin has been studied in various solutions, in the temperature range -8 degrees C to 100 degrees C, by scanning microcalorimetry, light absorption, circular dichroism, nuclear magnetic resonance spectroscopy and viscosimetry. It has been shown that in 10 mM-sodium acetate solutions (pH 3.5 to 3.9) the protein molecule undergoes a reversible conformational transition into a non-compact disordered state not only when the solution is heated above room temperature but also when it is cooled. In this state the protein does not have a tertiary structure, although it retains some residual ellipticity, which may be caused by the fluctuating alpha-helical conformation of the unfolded polypeptide chain. The disruption of the native protein structure both on cooling (cold-denaturation) and on heating (heat-denaturation) proceeds in an "all-or-none" manner, with a significant and similar increase of the protein heat capacity, but with inverse enthalpic and entropic effects: the enthalpy and entropy of the protein molecule decrease during cold-denaturation and increase during heat-denaturation.
journal_name
J Mol Bioljournal_title
Journal of molecular biologyauthors
Privalov PL,Griko YuV,Venyaminov SYu,Kutyshenko VPdoi
10.1016/0022-2836(86)90017-3subject
Has Abstractpub_date
1986-08-05 00:00:00pages
487-98issue
3eissn
0022-2836issn
1089-8638pii
0022-2836(86)90017-3journal_volume
190pub_type
杂志文章abstract：:Aminoacyl-tRNA synthetases are responsible for attaching amino acid residues to the tRNA 3'-end. The two classes of synthetases approach tRNA as mirror images, with opposite but symmetrical stereochemistries that allow the class I enzymes to attach amino acid residues to the 2'-hydroxyl group of the terminal ribose, w...
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pub_type： 杂志文章
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更新日期：1996-10-11 00:00:00
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journal_title：Journal of molecular biology
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