(Q44009825)

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Salts and glycine increase reversibility and decrease aggregation during thermal unfolding of ribonuclease-A.

scientific article published in April 2002

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Europe PubMed Central

PubMed publication ID

12036068

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28 November 2017

title

Salts and glycine increase reversibility and decrease aggregation during thermal unfolding of ribonuclease-A. (English)

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Europe PubMed Central

PubMed publication ID

28 November 2017

Tsutomu Arakawa

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Europe PubMed Central

PubMed publication ID

28 November 2017

Yoshiko Kita

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Europe PubMed Central

PubMed publication ID

12036068

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28 November 2017

publication date

1 April 2002

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Europe PubMed Central

PubMed publication ID

12036068

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28 November 2017

published in

Bioscience, Biotechnology, and Biochemistry

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Europe PubMed Central

PubMed publication ID

28 November 2017

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Europe PubMed Central

PubMed publication ID

28 November 2017

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Europe PubMed Central

PubMed publication ID

12036068

retrieved

28 November 2017

page(s)

880-882

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Europe PubMed Central

PubMed publication ID

12036068

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28 November 2017

cites work

Thermal unfolding of ribonuclease A in phosphate at neutral pH: deviations from the two-state model.

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Crossref

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https://api.crossref.org/works/10.1271%2FBBB.66.880

retrieved

21 January 2018

The observed change in heat capacity accompanying the thermal unfolding of proteins depends on the composition of the solution and on the method employed to change the temperature of unfolding

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Crossref

reference URL

https://api.crossref.org/works/10.1271%2FBBB.66.880

retrieved

21 January 2018

Identifiers

DOI

10.1271/BBB.66.880

1 reference

stated in

Europe PubMed Central

PubMed publication ID

12036068

retrieved

28 November 2017

PubMed publication ID

12036068

1 reference

stated in

Europe PubMed Central

PubMed publication ID

12036068

retrieved

28 November 2017

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