Results 251 to 260 of about 131,881 (286)
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Multiple denaturational transitions in fibrillar collagen
Biopolymers, 1986AbstractThe heat denaturation of pepsinized bovine nonfibrillar and fibrillar collagen was studied by differential scanning calorimetry. For fibrillar preparations that had been rapidly precipitated with stirring at low ionic strength, then resuspended at physiological ionic strength, multiple denaturational transitions were observed.
D G, Wallace +5 more
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Kinetic transition in model proteins with a denatured native spinodal
Physical Review E, 2002The relaxation kinetics of three-dimensional lattice model proteins with Gō potential is studied. A kinetic transition from an exponential behavior to a nonexponential one with a denatured native spinodal is characterized. The transition temperatures T(k), obtained from simulations and a semiquantitative estimation, are found to be the same. The change
Jun, Wang, Ke, Fan, Wei, Wang
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Denaturation: an example of a catastrophe II. Two-state transitions
Journal of Theoretical Biology, 1976Abstract In this paper statistical arguments are used within the framework of catastrophe theory to provide a quantitative description of protein transconformation reactions. For a protein-denaturant system, the accessible states (native and denatured) are characterized in terms of approximating Gaussian distributions.
Craig J. Benham, John J. Kozak
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Structural Transitions in the Protein L Denatured State Ensemble
Biochemistry, 1999We use a broad array of biophysical methods to probe the extent of structure and time scale of structural transitions in the protein L denatured state ensemble. Measurement of amide proton exchange protection during the first several milliseconds following initiation of refolding in 0.4 M sodium sulfate revealed weak protection in the first beta ...
M L, Scalley +3 more
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Journal of Molecular Biology, 2006
The development of electrostatic interactions during the folding of the N-terminal domain of the ribosomal protein L9 (NTL9) is investigated by pH-dependent rate equilibrium free energy relationships. We show that Asp8, among six acidic residues, is involved in non-native, electrostatic interactions with K12 in the transition state for folding as well ...
Jae-Hyun, Cho, Daniel P, Raleigh
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The development of electrostatic interactions during the folding of the N-terminal domain of the ribosomal protein L9 (NTL9) is investigated by pH-dependent rate equilibrium free energy relationships. We show that Asp8, among six acidic residues, is involved in non-native, electrostatic interactions with K12 in the transition state for folding as well ...
Jae-Hyun, Cho, Daniel P, Raleigh
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Post‐denaturational exothermic transition in soya isolate
International Journal of Food Science & Technology, 1987SummaryA previously unreported exothermic transition has been observed in soya isolate following the normal endothermic transitions associated with the denaturation of the 7S and 11S globulins.The concentration dependence of the peak temperature (Tm) and enthalpy (δH) of the transition has been investigated using differential scanning calorimetry.
P. R. SHEARD +2 more
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Biochemical and Biophysical Research Communications, 1990
During a previous investigation of the thermal denaturation of the membrane spanning domain of the human erythrocyte band 3 protein, a novel transition was noted. The most significant aspect of this transition is its reversibility, since both the endothermic and the functional denaturation of band 3 are clearly irreversible.
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During a previous investigation of the thermal denaturation of the membrane spanning domain of the human erythrocyte band 3 protein, a novel transition was noted. The most significant aspect of this transition is its reversibility, since both the endothermic and the functional denaturation of band 3 are clearly irreversible.
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Denaturant-Induced Conformational Transitions in Intrinsically Disordered Proteins
2012Intrinsically disordered proteins (IDPs) differ from ordered proteins at several levels: structural, functional, and conformational. Amino acid biases also drive atypical responses of IDPs to changes in their environment. Among several specific features, the conformational behavior of IDPs is characterized by the low cooperativity (or the complete lack
NEYROZ, PAOLO +2 more
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Multiphasic conformation transition of globular proteins under denaturating perturbation
Biopolymers, 1983AbstractDenaturation profiles of 17 globular proteins were studied by the spectroscopic and chromatographic methods with high‐data‐point density. The denaturational transitions are broadly classified into three types according to their multiphasic characteristics.
A, Wada, Y, Saito, M, Ohogushi
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Quantitative Analysis of Nonequilibrium, Denaturant-Dependent Protein Folding Transitions
Journal of the American Chemical Society, 2007The free energy of folding of small, one-domain proteins is generally measured with denaturant-induced unfolding/refolding equilibria based on the two-state model of protein folding. There is however an increasing number of reports on proteins that do not attain their folding equilibrium and show, even after long-term incubation, unfolding transitions ...
Erilov D, Puorger C, Glockshuber R
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