(Q51278144)

2 April 2018

title

Unveiling a hidden folding intermediate in c-type cytochromes by protein engineering. (English)

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2 April 2018

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4

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Maurizio Brunori

5

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2 April 2018

author name string

Alessandro Borgia

1

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2 April 2018

Daniele Bonivento

2

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2 April 2018

Carlo Travaglini-Allocatelli

3

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2 April 2018

language of work or name

English

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publication date

1 February 2006

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2 April 2018

Journal of Biological Chemistry

number of pages

6

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based on heuristic

inferred from page(s)

published in

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2 April 2018

volume

281

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issue

14

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2 April 2018

page(s)

9331-9336

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2 April 2018

The folding of an enzyme. I. Theory of protein engineering analysis of stability and pathway of protein folding

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Snapshots of protein folding. A study on the multiple transition state pathway of cytochrome c(551) from Pseudomonas aeruginosa

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Expression and characterization of Pseudomonas aeruginosa cytochrome c-551 and two site-directed mutants: role of tryptophan 56 in the modulation of redox properties.

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Parallel pathways in cytochrome c(551) folding.

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Structure of cytochrome c551 from Pseudomonas aeruginosa refined at 1.6 Å resolution and comparison of the two redox forms

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Structural differences between mesophilic, moderately thermophilic and extremely thermophilic protein subunits: results of a comprehensive survey

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21 January 2018

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An Obligatory Intermediate in the Folding Pathway of Cytochromec552fromHydrogenobacter thermophilus

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Folding mechanism of Pseudomonas aeruginosa cytochrome c 551 : role of electrostatic interactions on the hydrophobic collapse and transition state properties 1 1Edited by P. E. Wright

21 January 2018

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21 January 2018

Identifiers

DOI

10.1074/JBC.M512127200

1 reference

2 April 2018

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2 April 2018