3 documents found, page 1 of 1
Lessons on protein structure from interleukin‐4: All disulfides are not created...
Vaz, Daniela C.; Rodrigues, J. Rui; Loureiro‐Ferreira, Nuno; Müller, Thomas D.; Sebald, Walter; Redfield, Christina; Brito, Rui M. M.Interleukin-4 (IL-4) is a hematopoietic cytokine composed by a four-helix bundle stabilized by an antiparallel beta-sheet and three disulfide bonds: Cys3-Cys127, Cys24-Cys65, and Cys46-Cys99. IL-4 is involved in several immune responses associated to infection, allergy, autoimmunity, and cancer. Besides its physiological relevance, IL-4 is often used as a “model” for protein design and engineering. Hence, to un...
Potentially amyloidogenic conformational intermediates populate the unfolding l...
Rodrigues, J. Rui; Simões, Carlos J. V.; Silva, Cândida G.; Brito, Rui M. M.Protein aggregation into insoluble fibrillar structures known as amyloid characterizes several neurodegenerative diseases, including Alzheimer's, Huntington's and Creutzfeldt-Jakob. Transthyretin (TTR), a homotetrameric plasma protein, is known to be the causative agent of amyloid pathologies such as FAP (familial amyloid polyneuropathy), FAC (familial amyloid cardiomiopathy) and SSA (senile systemic amyloidosi...
Enthalpic and entropic contributions mediate the role of disulfide bonds on the...
Vaz, Daniela C.; Rodrigues, J. Rui; Sebald, Walter; Dobson, Christopher M.; Brito, Rui M. M.The role of disulfide bridges in the structure, stability, and folding pathways of proteins has been the subject of wide interest in the fields of protein design and engineering. However, the relative importance of entropic and enthalpic contributions for the stabilization of proteins provided by disulfides is not always clear. Here, we perform a detailed analysis of the role of disulfidesin the conformational ...