(Q44019108)

English

pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9.

scientific article published in April 2002

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scholarly article

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Europe PubMed Central

29 November 2017

pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. (English)

1 reference

Europe PubMed Central

29 November 2017

protein folding

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Daniel P Raleigh

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Daniel P Raleigh

2

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author name string

Satoshi Sato

1

1 reference

Europe PubMed Central

29 November 2017

language of work or name

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publication date

1 April 2002

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Europe PubMed Central

29 November 2017

Journal of Molecular Biology

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Europe PubMed Central

29 November 2017

318

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Europe PubMed Central

29 November 2017

2

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Europe PubMed Central

29 November 2017

571-582

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Europe PubMed Central

29 November 2017

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Ph-dependent interactions and the stability and folding kinetics of the N-terminal domain of L9. electrostatic interactions are only weakly formed in the transition state for folding 1 1Edited by C. R. Matthews

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Ribosomal Protein L9: A Structure Determination by the Combined Use of X-ray Crystallography and NMR Spectroscopy

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pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain

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Protein Denaturation

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Identifiers

10.1016/S0022-2836(02)00015-3

1 reference

Europe PubMed Central

29 November 2017

1 reference

Europe PubMed Central

29 November 2017

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