Evidence for barrier-limited protein folding kinetics on the microsecond time scale (Q74546456)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9587001%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

title

Evidence for barrier-limited protein folding kinetics on the microsecond time scale (English)

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11 November 2019

author name string

M C Shastry

series ordinal

1

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11 November 2019

H Roder

series ordinal

2

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11 November 2019

publication date

1 May 1998

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Nature structural biology

11 November 2019

published in

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11 November 2019

volume

5

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11 November 2019

issue

5

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11 November 2019

page(s)

385-392

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Submillisecond kinetics of protein folding

11 November 2019

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Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model

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Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy

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Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin

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Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues

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Kinetic mechanism of folding and unfolding of Rhodobacter capsulatus cytochrome c2

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Amide protection in an early folding intermediate of cytochrome c

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An early intermediate in the folding reaction of the B1 domain of protein G contains a native-like core

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Further evidence on the equilibrium "pre-molten globule state": four-state guanidinium chloride-induced unfolding of carbonic anhydrase B at low temperature

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Ultrafast signals in protein folding and the polypeptide contracted state

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Fast events in protein folding initiated by nanosecond laser photolysis

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Protein folding triggered by electron transfer

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Submillisecond events in protein folding

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A continuous-flow capillary mixing method to monitor reactions on the microsecond time scale.

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Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR.

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Kinetic mechanism of cytochrome c folding: involvement of the heme and its ligands

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The barriers in protein folding

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Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding

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31 March 2020

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31 March 2020

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31 March 2020

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Diffusion-limited contact formation in unfolded cytochrome c: estimating the maximum rate of protein folding

31 March 2020

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31 March 2020

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Protein folding: the endgame

31 March 2020

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Kinetic intermediates in the formation of the cytochrome c molten globule

31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0598-385

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9587001%20AND%20SRC:MED&resulttype=core&format=json

11 November 2019

1 reference