The Conformational Stability and Biophysical Properties of the Eukaryotic Thioredoxins of Pisum Sativum Are Not Family-Conserved

摘要: Thioredoxins (TRXs) are ubiquitous proteins involved in redox processes. About forty genes encode TRX or TRX-related plants, grouped different families according to their subcellular localization. For instance, the h-type TRXs located cytoplasm mitochondria, whereas f-type have a plastidial origin, although both types of an eukaryotic origin as opposed other TRXs. Herein, we study conformational and biophysical features TRXh1, TRXh2 TRXf from Pisum sativum. The modelled structures three show well-known fold. While sharing similar pH-denaturations features, chemical thermal stabilities different, being PsTRXh1 (Pisum sativum thioredoxin h1) most stable isoform; moreover, follow three-state denaturation model, during chemical-denaturations. These differences thermal- chemical-denaturations result changes, broad sense, several ASAs (accessible surface areas) proteins. Thus, strong relationship can be found between primary amino acid sequence structure among TRXs, that residue stability properties is not. We discuss how these determine unique functions pea, residues described (pH-titrations, dimerizations chemical-denaturations) belong regions interaction with Our results suggest demands protein-protein function relatively rigid, protein-binding pockets (some common) for each proteins, but per se (as long there maintained core), less so.