(Q72033203)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7664063%20AND%20SRC:MED&resulttype=core&format=json

23 October 2019

title

Molten globular characteristics of the native state of apomyoglobin (English)

1 reference

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23 October 2019

4

Rose GD

1 reference

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23 October 2019

author name string

Lin L

1

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23 October 2019

Pinker RJ

2

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23 October 2019

Forde K

3

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23 October 2019

Kallenbach NR

5

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23 October 2019

publication date

1 July 1994

1 reference

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Nature structural biology

23 October 2019

published in

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23 October 2019

volume

1

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23 October 2019

page(s)

447-452

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23 October 2019

issue

7

1 reference

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Structural and genetic analysis of protein stability

23 October 2019

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Protein folding studied using hydrogen-exchange labeling and two-dimensional NMR

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The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure.

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An early immunoreactive folding intermediate of the tryptophan synthease beta 2 subunit is a 'molten globule'.

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Thermodynamic puzzle of apomyoglobin unfolding

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Structure and stability of the molten globule state of guinea-pig alpha-lactalbumin: a hydrogen exchange study

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The phase transition between a compact denatured state and a random coil state in staphylococcal nuclease is first-order

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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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31 March 2020

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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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31 March 2020

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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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31 March 2020

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31 March 2020

Identifiers

DOI

10.1038/NSB0794-447

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:7664063%20AND%20SRC:MED&resulttype=core&format=json

23 October 2019

1 reference