Literature DB >> 15896898

The study of bimolecular reactions under non-pseudo-first order conditions.

Francesco Malatesta1.   

Abstract

In this work a new equation which describes the time evolution of bimolecular reactions is derived and tested by experiment. The equation is general and the results show that second-order reactions of any simple type may be accurately described by a quotient of exponential functions. The model and reagent concentration dependent observed rate constants show a complex non-linear behaviour when experimental conditions deviate from pseudo-first order nevertheless reducing to the well-known linear dependence when pseudo-first order conditions are met.

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Year:  2005        PMID: 15896898     DOI: 10.1016/j.bpc.2005.04.006

Source DB:  PubMed          Journal:  Biophys Chem        ISSN: 0301-4622            Impact factor:   2.352


  33 in total

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4.  Kinetic Methods of Deducing Binding Mechanisms Involving Intrinsically Disordered Proteins.

Authors:  Elin Karlsson; Per Jemth
Journal:  Methods Mol Biol       Date:  2021

5.  Slow, reversible, coupled folding and binding of the spectrin tetramerization domain.

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Journal:  Biophys J       Date:  2012-11-20       Impact factor: 4.033

6.  Fast association and slow transitions in the interaction between two intrinsically disordered protein domains.

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7.  Allosteric feedback inhibition of pyridoxine 5'-phosphate oxidase from Escherichia coli.

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8.  Affinity of IDPs to their targets is modulated by ion-specific changes in kinetics and residual structure.

Authors:  Basile I M Wicky; Sarah L Shammas; Jane Clarke
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9.  Coupled Binding and Helix Formation Monitored by Synchrotron-Radiation Circular Dichroism.

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Journal:  Biophys J       Date:  2019-07-19       Impact factor: 4.033

10.  On the acquisition and analysis of microscale thermophoresis data.

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Journal:  Anal Biochem       Date:  2015-12-29       Impact factor: 3.365

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