How Do Cofactors Modulate Protein Folding?
Cofactors are essential components of many proteins for biological activity. Characterization of several cofactor-binding proteins has shown that cofactors often have the ability to interact specifically with the unfolded polypeptides. This suggests that cofactor-coordination prior to polypeptide folding may be a relevant path in vivo. By binding before folding, the cofactor may affect both the mechanism and speed of folding. Here, we discuss three different cofactors that modulate protein-folding processes in vitro.
Keywords: azurin; cofactor-binding protein; ferredoxin; flavin mononucleotide; flavodoxin; folding pathway; folding speed; iron-sulfur cluster
Document Type: Review Article
Affiliations: Biochemistry & Cell Biology Department, Rice University, Houston, Texas 77251 USA.
Publication date: 01 February 2005
- Protein & Peptide Letters publishes short papers in all important aspects of protein and peptide research, including structural studies, recombinant expression, function, synthesis, enzymology, immunology, molecular modeling, drug design etc. Manuscripts must have a significant element of novelty, timeliness and urgency that merit rapid publication. Reports of crystallisation, and preliminary structure determinations of biologically important proteins are acceptable. Purely theoretical papers are also acceptable provided they provide new insight into the principles of protein/peptide structure and function.
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