Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
نویسندگان
چکیده
منابع مشابه
On the structural stability and solvent denaturation of proteins. II. Denaturation by the ureas.
The effects of the water-miscible straight chain and branched alcohols and glycols on the native conformation of sperm whale myoglobin, cytochrome c, and oc-chymotrypsinogen have been investigated by spectral, difference spectral, and optical rotatory dispersion methods. Based on the midpoints of the denaturation transitions, that is, the amount of alcohol or glycol required to produce 50% dena...
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The ribosome is a dynamic machine that undergoes many conformational rearrangements during the initiation of protein synthesis. Significant differences exist between the process of protein synthesis initiation in eubacteria and eukaryotes. In particular, the initiation of eukaryotic protein synthesis requires roughly an order of magnitude more initiation factors to promote efficient mRNA recrui...
متن کاملOn the Structural Stability and Solvent Denaturation of Proteins
The effects of the water-miscible straight chain and branched alcohols and glycols on the native conformation of sperm whale myoglobin, cytochrome c, and oc-chymotrypsinogen have been investigated by spectral, difference spectral, and optical rotatory dispersion methods. Based on the midpoints of the denaturation transitions, that is, the amount of alcohol or glycol required to produce 50% dena...
متن کاملEarly Days of Pressure Denaturation Studies of Proteins.
The denaturation of protein by pressure has been generally well known since the findings of the perfect coagulation of egg white by a pressure of 7,000 atm within 30 min by Bridgman (J Biol Chem 19:511-512, 1914), and Kiyama and Yanagimoto (Rev Phys Chem Jpn 21:41-43, 1951) confirmed that the coagulation occurs above 3,880 kg cm(-2). Grant et al. (Science 94:616, 1941) and Suzuki and Kitamura (...
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The stability of calf skin collagen (CSC) type I during thermal and chemical denaturation in the presence of glycerol was investigated. Thermal denaturation of type I collagen was performed in the presence of glycerol or in combination with urea and sodium chloride. The denaturation curves obtained in the presence of urea or sodium chloride retained their original shape without glycerol. These ...
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ژورنال
عنوان ژورنال: Protein Science
سال: 1994
ISSN: 0961-8368,1469-896X
DOI: 10.1002/pro.5560031202