Micro- and macro-stabilities of globular proteins View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1979-08

AUTHORS

P. L. PRIVALOV, T. N. TSALKOVA

ABSTRACT

PROTEIN stability is usually expressed in terms of the energies required for the micro- and macro-unfolding of its structure, determined from hydrogen exchange and denaturation experiments. Both these characteristics represent qualitatively different properties of a protein macromolecule which can be classified as the rigidity of the structure and the stability of the macroscopic state. In this report, the dependence of these properties on the parameters specifying protein structure is analysed. More... »

PAGES

693-696

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/280693a0

DOI

http://dx.doi.org/10.1038/280693a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1020154825

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/224319


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