pH-dependent stability and folding kinetics of a protein with an unusual alpha-beta topology: the C-terminal domain of the ribosomal protein L9. (Q44019108)

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scientific article published in April 2002

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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

1 reference

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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Formation of electrostatic interactions on the protein-folding pathway

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Titration properties and thermodynamics of the transition state for folding: comparison of two-state and multi-state folding pathways.

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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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The stability and dynamics of ribosomal protein L9: investigations of a molecular strut by amide proton exchange and circular dichroism

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Global analysis of the effects of temperature and denaturant on the folding and unfolding kinetics of the N-terminal domain of the protein L9.

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The anatomy of protein beta-sheet topology

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Folding of the Multidomain Ribosomal Protein L9: The Two Domains Fold Independently with Remarkably Different Rates†

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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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Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding

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The origin of pH-dependent changes in m-values for the denaturant-induced unfolding of proteins

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On the pH dependence of protein stability.

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MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures

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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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