(Q46092446)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:19277727%20AND%20SRC:MED&resulttype=core&format=json

23 January 2020

title

A single mutation induces molten globule formation and a drastic destabilization of wild-type cytochrome c at pH 6.0. (English)

1 reference

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23 January 2020

4

1 reference

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23 January 2020

Faizan Ahmad

7

1 reference

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23 January 2020

author name string

Md Khurshid Alam Khan

1

1 reference

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23 January 2020

Utpal Das

2

1 reference

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23 January 2020

Md Hamidur Rahaman

3

1 reference

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23 January 2020

A Srinivasan

5

1 reference

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23 January 2020

Tej P Singh

6

1 reference

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23 January 2020

publication date

10 March 2009

1 reference

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Journal of Biological Inorganic Chemistry

23 January 2020

published in

1 reference

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23 January 2020

volume

14

1 reference

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23 January 2020

issue

5

1 reference

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23 January 2020

page(s)

751-760

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https://scigraph.springernature.com/pub.10.1007/s00775-009-0488-6

23 January 2020

exact match

0 references

cites work

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Equilibrium studies of the effect of difference in sequence homology on the mechanism of denaturation of bovine and horse cytochromes-c

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Determinants of a protein fold. Unique features of the globin amino acid sequences

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Protein folding and protein evolution: common folding nucleus in different subfamilies of c-type cytochromes?

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A unique molten globule state occurs during unfolding of cytochrome c by LiClO4 near physiological pH and temperature: structural and thermodynamic characterization

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Solvent isotope effect and protein stability

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Characterization of horse cytochrome c expressed in Escherichia coli.

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Stable submolecular folding units in a non-compact form of cytochrome c

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12 December 2020

A native tertiary interaction stabilizes the A state of cytochrome c

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12 December 2020

The relation between the divergence of sequence and structure in proteins

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12 December 2020

Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c

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From Levinthal to pathways to funnels

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8-anilino-1-naphthalene sulfonic acid (ANS) induces folding of acid unfolded cytochrome c to molten globule state as a result of electrostatic interactions.

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Nucleation mechanisms in protein folding

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Conformation of ferricytochrome c. IV. Relationship between optical absorption and protein conformation

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New Perspectives on c-Type Cytochromes

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Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process

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Binding of naphthalene dyes to the N and A conformers of bovine alpha-lactalbumin

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Anion size modulates the structure of the A state of cytochrome c.

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High-resolution three-dimensional structure of horse heart cytochrome c

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12 December 2020

Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants

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12 December 2020

Unfolding free energy changes determined by the linear extrapolation method. 1. Unfolding of phenylmethanesulfonyl alpha-chymotrypsin using different denaturants

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12 December 2020

The Soret circular dichroism spectrum as a probe for the heme Fe(III)-Met(80) axial bond in horse cytochrome c.

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12 December 2020

Classification of acid denaturation of proteins: intermediates and unfolded states

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12 December 2020

A possible origin of differences between calorimetric and equilibrium estimates of stability parameters of proteins

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12 December 2020

Kinetic intermediates in the formation of the cytochrome c molten globule

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12 December 2020

Main-chain bond lengths and bond angles in protein structures

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12 December 2020