(Q56999466)

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Metastable states and folding free energy barriers

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title

Metastable states and folding free energy barriers (English)

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David Baker

1

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publication date

December 1998

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published in

Nature structural biology

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volume

5

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issue

12

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page(s)

1021-1024

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exact match

https://scigraph.springernature.com/pub.10.1038/4130

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cites work

Unfolded conformations of alpha-lytic protease are more stable than its native state

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21 January 2018

Structure of alpha-lytic protease complexed with its pro region

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21 January 2018

Pro region C-terminus:protease active site interactions are critical in catalyzing the folding of alpha-lytic protease

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21 January 2018

The role of pro regions in protein folding.

1 reference

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21 January 2018

Catalysis of a protein folding reaction: thermodynamic and kinetic analysis of subtilisin BPN' interactions with its propeptide fragment.

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21 January 2018

A protein-folding reaction under kinetic control

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21 January 2018

A soluble domain of the membrane-anchoring chain of influenza virus hemagglutinin (HA2) folds in Escherichia coli into the low-pH-induced conformation

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21 January 2018

Prodomain mutations at the subtilisin interface: correlation of binding energy and the rate of catalyzed folding

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21 January 2018

The prosegment-subtilisin BPN' complex: crystal structure of a specific 'foldase'

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21 January 2018

Protease pro region required for folding is a potent inhibitor of the mature enzyme.

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Three-dimensional structure of porcine pancreatic procarboxypeptidase A. A comparison of the A and B zymogens and their determinants for inhibition and activation.

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21 January 2018

The sequences of small proteins are not extensively optimized for rapid folding by natural selection

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21 January 2018

Kinetically controlled folding of the serpin plasminogen activator inhibitor 1

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retrieved

7 January 2021

based on heuristic

inferred from DOI database lookup

Energetics of folding subtilisin BPN'

1 reference

stated in

Crossref

reference URL

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7 January 2021

based on heuristic

inferred from DOI database lookup

Pro-peptide as an intramolecular chaperone: renaturation of denatured subtilisin E with a synthetic pro-peptide [corrected]

1 reference

stated in

Crossref

reference URL

https://api.crossref.org/works/10.1038%2F4130

retrieved

7 January 2021

based on heuristic

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Identifiers

DOI

10.1038/4130

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Dimensions Publication ID

1004038218

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PubMed publication ID

9846867

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(Q56999466)

Metastable states and folding free energy barriers

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