STABILIZING INTERACTIONS IN THE H2A-H2B MONOMERIC AND DIMERIC KINETIC INTERMEDIATES
Guyett, Paul J.
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The long-standing goal of protein folding studies is to understand how the amino acid sequence encodes the folding of a peptide from an extended conformation to the biologically active, three-dimensional structure. Theoretically, evolution should have smoothed the folding landscapes of proteins to reduce any intermediates or deviation from the most direct and rapid trajectory of folding, i.e. kinetic traps. However, transiently populated intermediates are common features in the folding landscapes of large proteins. Previous comparison of homologous dimeric histone proteins, H2A-H2B, hMfB, hPyA1, and hFoB, identified that transient population of intermediates correlated with rapid association, suggesting intermediates are not kinetic traps, but may accelerate folding. Understanding the structural features of kinetic intermediates will help elucidate their role in the folding landscape. The folding mechanism of H2A-H2B is multi-state, with transient population of a dimeric ensemble (I