منابع مشابه
Analysis of rate-limiting long-range contacts in the folding rate of three-state and two-state Proteins.
In the past decade, when compared to models describing the folding rates of two-state proteins, models describing the folding mechanism of three-state proteins remain quite limited due to the complexity present in the folding mechanism and lack in their experimental data. In the present work, rate-limiting long-range contacts were classified into various bins based on sequence separation distan...
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The effect of the choice of control allocation scheme upon individual control effector rate demands is examined. Three previously reported and one new variation of control allocation schemes are described and compared. The new allocation scheme exploits the maximum attainable moment-rates of a given control effector configuration and is called moment rate allocation. The bases of comparison are...
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Amyloid fibrils are aggregated and precipitated forms of protein in which the protein exists in highly ordered, long, unbranching threadlike formations that are stable and resistant to degradation by proteases. Fibril formation is an ordered process that typically involves the unfolding of a protein to partially folded states that subsequently interact and aggregate through a nucleation-depende...
متن کاملTransition State in DNA Polymerase β Catalysis: Rate-Limiting Chemistry Altered by Base-Pair Configuration
Kinetics studies of dNTP analogues having pyrophosphate-mimicking β,γ-pCXYp leaving groups with variable X and Y substitution reveal striking differences in the chemical transition-state energy for DNA polymerase β that depend on all aspects of base-pairing configurations, including whether the incoming dNTP is a purine or pyrimidine and if base-pairings are right (T•A and G•C) or wrong (T•G an...
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The hydrolysis of 0-p-phenylazophenylphosphorothioate by Escherichia coli alkaline phosphatase was studied by the stopped-flow technique. “Burst” kinetics is observed at both acid and basic pH, suggesting that a step following thiophosphorylation is rate-limiting at all pH values. At pH 8.5, activation of a second active site on the enzyme dimer is observed in the transient phase as subsrrate c...
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ژورنال
عنوان ژورنال: Queue
سال: 2014
ISSN: 1542-7730,1542-7749
DOI: 10.1145/2578508.2578510