Publications by authors named "Kevin Sforza"
Article Synopsis
- The text presents programs for analyzing the thermodynamics of linear repeat proteins using a 1D Ising model, focusing on intrinsic folding and interfacial coupling free energies.
- These programs are applicable to both homopolymeric and heteropolymeric constructs, allowing researchers to study the impact of mutations on folding behavior and free energies.
- A bootstrap analysis is included to assess parameter uncertainty and correlations, highlighting the importance of rigorous statistical methods in the interpretation of results from complex models.
Designed helical repeats (DHRs) are modular helix-loop-helix-loop protein structures that are tandemly repeated to form a superhelical array. Structures combining tandem DHRs demonstrate a wide range of molecular geometries, many of which are not observed in nature. Understanding cooperativity of DHR proteins provides insight into the molecular origins of Rosetta-based protein design hyperstability and facilitates comparison of energy distributions in artificial and naturally occurring protein folds.
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- The study reveals direct NMR evidence for a unique bifurcated H-bonding arrangement that involves nitrogen as an acceptor, specifically between histidine and threonine within ankyrin repeat proteins.
- The findings show that the internal H-bonds are stronger than those exposed on the protein's surface, which is supported by pKa values indicating lower acidity in hidden histidines.
- Additionally, substituting threonine with valine disrupts the H-bonding network, leading to increased H-bond scalar coupling, thus highlighting the crucial role of these interactions in protein stability and structure.