Folding and stability of human carbonic anhydrase II

descriptionPublicationkeyboard_double_arrow_right Part of book or chapter of book , Article , Other literature type 01 Jan 2000Publisher:Birkhäuser Basel

Authors: U, Carlsson; B H, Jonsson;

doi: 10.1007/978-3-0348-8446-4_13

pmid: 11268519

Folding and stability of human carbonic anhydrase II

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Abstract

Knowledge of various dynamic aspects of the structure of carbonic anhydrase is important for comprehension of the structural integrity and function of the enzyme. Therefore, characterization of the folding pathway will contribute to a deeper understanding of the structure-function relationship and will provide clues to help solve the protein folding problem.

Related Organizations

Linköping University
Sweden
Umeå University
Sweden

Keywords

Protein Denaturation, Protein Folding, Protein Conformation, Protein Structure, Secondary, Recombinant Proteins, Isoenzymes, Kinetics, Amino Acid Substitution, Enzyme Stability, Mutagenesis, Site-Directed, Humans, Carbonic Anhydrases

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