The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin (Q30165217)

9 June 2017

title

The temperature dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin (English)

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9 June 2017

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Sadqi M

1

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9 June 2017

Casares S

series ordinal

2

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López-Mayorga O

series ordinal

3

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9 June 2017

Conejero-Lara F

series ordinal

4

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9 June 2017

language of work or name

English

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publication date

1 September 2002

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9 June 2017

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9 June 2017

volume

527

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9 June 2017

issue

1-3

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9 June 2017

page(s)

86-90

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Protein folding intermediates and pathways studied by hydrogen exchange

9 June 2017

cites work

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Pressure Dependence of Amide Hydrogen−Deuterium Exchange Rates for Individual Sites in T4 Lysozyme

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pH dependence of the hydrogen exchange in the SH3 domain of alpha-spectrin.

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Low energy of activation for amide hydrogen exchange reactions in proteins supports a local unfolding model

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Hydrogen exchange in chymotrypsin inhibitor 2 probed by denaturants and temperature

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Hydrogen exchange of the tetramerization domain of the human tumour suppressor p53 probed by denaturants and temperature

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The folding transition state between SH3 domains is conformationally restricted and evolutionarily conserved.

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Temperature and pH dependences of hydrogen exchange and global stability for ovomucoid third domain

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Predicting the equilibrium protein folding pathway: structure-based analysis of staphylococcal nuclease

7 January 2021

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7 January 2021

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7 January 2021

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Identifiers

DOI

10.1016/S0014-5793(02)03172-1

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9 June 2017

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