Abstract
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: cofactor-binding protein, azurin, flavodoxin, ferredoxin, flavin mononucleotide, iron-sulfur cluster, folding speed, folding pathway
Protein & Peptide Letters
Title: How Do Cofactors Modulate Protein Folding?
Volume: 12 Issue: 2
Author(s): Catherine L. Higgins, B. K. Muralidhara and Pernilla Wittung-Stafshede
Affiliation:
Keywords: cofactor-binding protein, azurin, flavodoxin, ferredoxin, flavin mononucleotide, iron-sulfur cluster, folding speed, folding pathway
Abstract: 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.
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Cite this article as:
Higgins L. Catherine, Muralidhara K. B. and Wittung-Stafshede Pernilla, How Do Cofactors Modulate Protein Folding?, Protein & Peptide Letters 2005; 12 (2) . https://dx.doi.org/10.2174/0929866053005782
DOI https://dx.doi.org/10.2174/0929866053005782 |
Print ISSN 0929-8665 |
Publisher Name Bentham Science Publisher |
Online ISSN 1875-5305 |

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