Molecular Cloning and Chaperone Activity of DnaK from Cold-adapted Bacteria, KOPRI22215
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چکیده
منابع مشابه
Role of Molecular Interactions and Oligomerization in Chaperone Activity of Recombinant Acr from Mycobacterium tuberculosis
Background: The chaperone activity of Mycobacterium tuberculosis Acr is an important function that helps to prevent misfolding of protein substrates inside the host, especially in conditions of hypoxia. Objectives: The aim of this study was to establish the correlation of structure and function of recombinant Acr proteins both before and after ge...
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Institute of Evolutionary Biology and Environmental Studies, University of Zurich, Zurich, 4 Switzerland 5 Swiss Institute of Bioinformatics, Lausanne, Switzerland 6 Department of Genetics, Smurfit Institute of Genetics, University of Dublin, Trinity College Dublin, 7 Dublin, Ireland 8 Instituto de Biología Molecular y Celular de Plantas (CSIC-UPV), Valencia, Spain 9 Department of Biology, Univ...
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Objective(s):Brucellosis is a well-known domestic animal infectious disease, which is caused by Brucella bacterium. GroEL antigen increases Brucella survival and is one of the major antigens that stimulates the immune system. Hence, the objective of the present study was cloning and bioinformatics analysis of GroEL gene. Materials and Methods: The full-length open reading frame of this gene was...
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The molecular chaperone DnaK prevents intracellular protein misfolding and aggregation by transiently binding with newly synthesized polypeptides and protein folding intermediates. DnaK preferentially binds to peptides with basic residues (Arg/Lys) present on the outside of a hydrophobic core. The electrostatic contribution toward DnaK/peptide binding was determined by measuring the dissociatio...
متن کاملThe Molecular Chaperone DnaK Is a Source of Mutational Robustness
Molecular chaperones, also known as heat-shock proteins, refold misfolded proteins and help other proteins reach their native conformation. Thanks to these abilities, some chaperones, such as the Hsp90 protein or the chaperonin GroEL, can buffer the deleterious phenotypic effects of mutations that alter protein structure and function. Hsp70 chaperones use a chaperoning mechanism different from ...
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ژورنال
عنوان ژورنال: Bulletin of the Korean Chemical Society
سال: 2011
ISSN: 0253-2964
DOI: 10.5012/bkcs.2011.32.6.1925