منابع مشابه
The estimation of polypeptide chain molecular weights by gel filtration in 6 M guanidine hydrochloride.
Gel filtration of reduced protein polypeptide chains in 6 M guanidine hydrochloride has been evaluated as a means of estimating protein or protein subunit molecular weights as suggested by Davison (Science, 161, 906 (1968)). As a gel filtration medium, 6% agarose permits useful molecular weight estimates between the extreme limits of 80,000 and 1,000. Provided weight rather than volume is used ...
متن کاملNMR identification of local structural preferences in HIV-1 protease tethered heterodimer in 6 M guanidine hydrochloride.
Understanding protein folding requires complete characterization of all the states of the protein present along the folding pathways. For this purpose nuclear magnetic resonance (NMR) has proved to be a very powerful technique because of the great detail it can unravel regarding the structure and dynamics of protein molecules. We report here NMR identification of local structural preferences in...
متن کاملPreferential solvation of bovine serum albumin in aqueous guanidine hydrochloride.
Bovine serum albumin, in aqueous guanidine hydrochloride, interacts preferentially with the solvent components, as was shown by techniques in which refractometry and light scattering and equilibrium dialysis were used. If constant salt molality after dialysis is taken as the reference state for zero binding, then 0.08 f 0.03 and 0.18 f 0.05 g of salt per g of protein is bound at 3 M and 6 M sal...
متن کاملScaling properties of glycine-rich sequences in guanidine hydrochloride solutions.
The intrinsic polymer properties of glycine-rich sequences are evaluated with a set of iso-1-cytochrome c variants with N-terminal inserts of the sequence (GGGGGK)(n) for n = 1-5. The thermodynamics and kinetics of His-heme loop formation are measured as a function of guanidine hydrochloride (GdnHCl) concentration for loop sizes ranging from 22 to 46 residues. The scaling exponent for loop form...
متن کاملDenaturation of Bovine Carbonic Anhydrase B by Guanidine Hydrochloride
The denaturation and renaturation of bovine carbonic anhydrase B is a thermodynamically reversible process, uncomplicated by aggregation or disuhide bond formation. The reaction is less cooperative than is the unfolding and refolding of most globular proteins, in that distinct successive stages can be observed both in equilibrium and kinetic measurements. This enzyme is therefore ideally suited...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 1966
ISSN: 0021-9258
DOI: 10.1016/s0021-9258(18)96726-8