Analyzing Protein Disorder with IUPred2A

Algorithms for Analyzing Protein Conformational Flexibility with Noisy Data

Many proteins undergo changes in their structure during biochemical processes such as binding and transport. Such conformational changes are crucial to the functioning of proteins, and by extension, to most biological processes. This thesis describes algorithms for detecting conformational changes from protein structure data. Conformational changes may be determined by comparing protein structu...

Analyzing Disease-Associated Protein Structures with Visual Analytics

Protein function is related to protein structure, and understanding disease-associated structural changes is critical both to understanding protein-mediated illness and to developing clinical therapies. We have developed a visual analytics tool called ContactWalker that uses molecular dynamics simulations to investigate the structural and physical differences between wild type and disease-assoc...

Disorder-Based Protein-Protein Interactions

Intrinsic Protein Disorder and Protein-Protein Interactions

Intrinsically disordered proteins often bind to more than one partner. In this study, we focused on 11 sets of complexes in which the same disordered segment becomes bound to two or more distinct partners. For this collection of protein complexes, two or more partners of each disordered segment were selected to have less than 25% amino acid identity at structurally aligned positions. As it tur...

Analyzing leukocyte telomere length in bipolar disorder: Authors' reply.

Our original study adds important information to the evidence base for bipolar disorder (BD) pathology. We show, for the first time, that shorter leukocyte telomere length (LTL) is already present in individuals with the early stages of BD and is comparable to LTL from individuals in the late stages of the disease. This result is at least surprising. We might speculate that, in BD, LTL would be...