Oligomerization affects the kinetics and thermodynamics of the interaction of a Bowman-Birk inhibitor with proteases

Author:

Brand G.D.,Pires D.A.T.,Furtado J.R.,Cooper A.ORCID,Freitas S.M.,Bloch C.

Funder

Coordenação de Aperfeiçoamento de Pessoal de Nível Superior

Conselho Nacional de Desenvolvimento Científico e Tecnológico

Fundação de Amparo à Pesquisa do Distrito Federal

Financiadora de Estudos e Projetos

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference26 articles.

1. Protein proteinase inhibitors - molecular aspects;Laskowski,1971

2. Bowman-Birk protease inhibitor from the seeds of Vigna unguiculata forms a highly stable dimeric structure;Rao;Biochim. Biophys. Acta,2007

3. Kinetics of a-chymotrypsin dimerization;Gilleland;J. Biol. Chem.,1976

4. Double-headed protease inhibitors from black-eyed peas. V. Analysis of the energetics of protease-inhibitor interactions;Gennis;J. Biol. Chem.,1976

5. Crystal structure of cancer chemopreventive bowman-birk inhibitor in ternary complex with Ê resolution. Structural basis bovine trypsin at 2. 3 a of Janus-faced serine protease inhibitor specificity;Koepke;J. Mol. Biol.,2000

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