Protein Folding Kinetics

Nölting, Bengt

doi:10.1007/978-3-662-03966-3

Cited by 84 publications

(81 citation statements)

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“…Within this model the observed spectroscopic parameter P T can be expressed as the value of the folded state times its population, plus the signal of the unfolded state times its population [32]: (2) where is the equilibrium constant at T temperature between folded and unfolded state, and denote the values of at T=0 K in the folded and unfolded state respectively, and and their temperature dependence. In particular, and parameters describe the linear Tdependence of the band position in the pre-and post-melting region, and this trend suggests a continuous variation for the arrangement of both folded and unfolded structures.…”

Section: Accepted M Manuscriptmentioning

confidence: 99%

Unfolding and aggregation of lysozyme: A thermodynamic and kinetic study by FTIR spectroscopy

Sassi

Giugliarelli

Paolantoni

et al. 2011

Biophysical Chemistry

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The unfolding of hen egg-white lysozyme dissolved both in D 2 O and CH 3 CH 2 OD/D 2 O was studied by Fourier Transform Infrared (FTIR) absorption spectroscopy at different protein concentrations.A detailed description of the local and global rearrangement of the secondary structure upon a temperature increase, in the range 295 to 365 K, was obtained through the analysis of the amide I band. Thermodynamic parameters for the melting, and the effect of the co-solvent in determining a change in thermal stability of the protein were evaluated. The protein-protein interactions were also followed as a function of temperature: a strong dependence of the cluster stability and aggregation yield on the solvent composition was observed. Finally, FTIR spectra taken at successive time steps of the aggregation enabled intermolecular contacts to be monitored as a function of time, and kinetic information to be obtained showing that both unfolded and folded states of lysozyme act as reactants for the clustering event.

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Section: Accepted M Manuscriptmentioning

confidence: 99%

Unfolding and aggregation of lysozyme: A thermodynamic and kinetic study by FTIR spectroscopy

Sassi

Giugliarelli

Paolantoni

et al. 2011

Biophysical Chemistry

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“…The calculation was performed according to the standard scheme [8]. The obtained data reveal that Ca 2+ has a significant stabilizing effect on the protein structure.…”

Section: Ggbp Ggbp/glc and Their Forms With Depleted Ca 2+ Folding-umentioning

confidence: 99%

Structure and stability of D-galactose/D-glucose-binding protein. The role of D-glucose binding and Ca ion depletion

et al. 2010

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Abstract. The effects of guanidine hydrochloride (GdnHCl) on the structure and stability of the D-galactose/D-glucose-binding protein from Escherichia coli (GGBP) and its complex with D-glucose (GGBP/Glc) were investigated by intrinsic protein fluorescence and far-UV circular dichroism (CD). The role of calcium in the stability of the protein structure was also studied. It was shown that the processes of GGBP and GGBP/Glc unfolding induced by GdnHCl followed one-step reversible denaturation mechanism. The obtained data showed that the binding of glucose to GGBP resulted in an increase of the protein stability towards the actions of the GdnHCl which made protein unfolding more cooperative. The stabilities of GGBP alone, GGBP in the presence of glucose, GGBP-depleted calcium (GGBP-Ca), and GGBP/Glc-depleted calcium (GGBP/Glc-Ca) were characterized by difference of Gibbs free energies.

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“…26) and P F,R (t, t 0 ) (ref. 37) terms in equation (1) that describe cotranslational folding mechanisms involving three states. In addition, co-translational folding can be influenced by chaperones 2,38,39 and other cellular factors 40 .…”

Section: Discussionmentioning

confidence: 99%

Accurate Prediction of Cellular Co-Translational Folding Indicates Proteins can Switch from Post- to Co-Translational Folding

Nissley

2017

Biophysical Journal

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The rates at which domains fold and codons are translated are important factors in determining whether a nascent protein will co-translationally fold and function or misfold and malfunction. Here we develop a chemical kinetic model that calculates a protein domain's co-translational folding curve during synthesis using only the domain's bulk folding and unfolding rates and codon translation rates. We show that this model accurately predicts the course of co-translational folding measured in vivo for four different protein molecules. We then make predictions for a number of different proteins in yeast and find that synonymous codon substitutions, which change translation-elongation rates, can switch some protein domains from folding post-translationally to folding co-translationally-a result consistent with previous experimental studies. Our approach explains essential features of co-translational folding curves and predicts how varying the translation rate at different codon positions along a transcript's coding sequence affects this self-assembly process.

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Protein Folding Kinetics

Cited by 84 publications

References 0 publications

Unfolding and aggregation of lysozyme: A thermodynamic and kinetic study by FTIR spectroscopy

Unfolding and aggregation of lysozyme: A thermodynamic and kinetic study by FTIR spectroscopy

Structure and stability of D-galactose/D-glucose-binding protein. The role of D-glucose binding and Ca ion depletion

Accurate Prediction of Cellular Co-Translational Folding Indicates Proteins can Switch from Post- to Co-Translational Folding

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