|Name||Mr. Alfredo Peguero-Tejada|
|Organization or Institution||University of South Florida|
Assessing the intrinsic secondary structure propensity of chameleon sequences
Alfredo Peguero-Tejada, Arjan van der Vaart
University of South Florida
Chameleon sequences can adopt both α-helical and β-sheet conformations depending on the protein in which they are found. The extent to which this polymorphism is intrinsic or context driven is not fully understood. Characterizing the relative stability between the different structural states of these sequences would allow for more intelligent drug design and shed light on the observed structural plasticity of sequences. The present study addresses this issue by calculating the conformational free energy difference between α-helical and β-sheet conformations via the confinement method, which links thermodynamic states of interest by transforming them into sets of independent harmonic oscillators. The results of this study will yield a library of conformational free energy differences as a function of various chameleon peptide sequences.