(Q74030954)

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427010%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

title

Strain in the folding nucleus of chymotrypsin inhibitor 2 (English)

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8 November 2019

2

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8 November 2019

author name string

Ladurner AG

series ordinal

1

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8 November 2019

Fersht AR

series ordinal

3

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8 November 2019

publication date

1 January 1997

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8 November 2019

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8 November 2019

volume

2

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8 November 2019

issue

6

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8 November 2019

page(s)

363-368

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Folding of chymotrypsin inhibitor 2. 1. Evidence for a two-state transition

8 November 2019

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The Structure of the Transition State for Folding of Chymotrypsin Inhibitor 2 Analysed by Protein Engineering Methods: Evidence for a Nucleation-condensation Mechanism for Protein Folding

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Conformational Pathway of the Polypeptide Chain of Chymotrypsin Inhibitor-2 Growing from its N Terminusin vitro. Parallels with the Protein Folding Pathway

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Following co-operative formation of secondary and tertiary structure in a single protein module

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7 January 2021

Identification and characterization of the unfolding transition state of chymotrypsin inhibitor 2 by molecular dynamics simulations

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Effect of active site residues in barnase on activity and stability

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Hydrophobic core repacking and aromatic-aromatic interaction in the thermostable mutant of T4 lysozyme Ser 117-->Phe

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7 January 2021

The native strains in the hydrophobic core and flexible reactive loop of a serine protease inhibitor: crystal structure of an uncleaved alpha1-antitrypsin at 2.7 A

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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7 January 2021

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Identifiers

DOI

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:9427010%20AND%20SRC:MED&resulttype=core&format=json

8 November 2019

1 reference