• encode
  • The genomes of higher plants, including Arabidopsis thaliana , Glycine max (soybean), Oryza sativa (rice), and Zea mays (maize), encode approximately 10 to 20 members of the PDI family, which show wide variation in the organization of their thioredoxin (TRX)-fold domains [ 4 , 5 ]. (hindawi.com)
  • It is estimated that 20-30% of all genes in most genomes encode membrane proteins. (wikipedia.org)
  • conformations
  • and amino acid composition but with different folding conformations. (bio.net)
  • Kinetical accessibility: means that the path in the free energy surface from the unfolded to the folded state must be reasonably smooth or, in other words, that the folding of the chain must not involve highly complex changes in the shape (like knots or other high order conformations). (wikipedia.org)
  • Prions are stable conformations of proteins which differ from the native folding state. (wikipedia.org)
  • dynamics
  • The targets are moving, and as predictions become more sophisticated with each passing tournament, so does our appreciation of the intricacies of protein structure, function, and dynamics. (mdpi.com)
  • The correct three-dimensional structure is essential to function, although some parts of functional proteins may remain unfolded, so that protein dynamics is important. (wikipedia.org)
  • aggregation
  • The familial amyloid neuropathies (or familial amyloidotic neuropathies, neuropathic heredofamilial amyloidosis, familial amyloid polyneuropathy) are a rare group of autosomal dominant diseases wherein the autonomic nervous system and/or other nerves are compromised by protein aggregation and/or amyloid fibril formation. (wikipedia.org)
  • The aggregation of one precursor protein leads to peripheral neuropathy and/or autonomic nervous system dysfunction. (wikipedia.org)
  • analyze the protein
  • Covering experiment and theory, bioinformatics approaches, and state-of-the-art simulation protocols for better sampling of the conformational space, this volume describes a broad range of techniques to study, predict, and analyze the protein folding process. (springer.com)
  • Gel electrophoresis was used to analyze the protein complex, the complex formed a single band that was excised and ran on an SDS gel. (wikipedia.org)
  • biogenesis
  • TC# 5.A.1.1.1) (2) the cytochrome c-type biogenesis proteins, CcdA (TC# 5.A.1.2.1) of Paracoccus pantotrophus and Bacillus subtilis. (wikipedia.org)
  • amyloid
  • Several neurodegenerative and other diseases are believed to result from the accumulation of amyloid fibrils formed by misfolded proteins. (wikipedia.org)
  • In Bovine spongiform encephalopathy (Mad Cow Disease), native proteins re-fold into a different stable conformation, which causes fatal amyloid buildup. (wikipedia.org)
  • electron
  • Disulfide bond formation involves electron transfer from the substrate to a disulfide carrier protein (e.g. (hindawi.com)
  • These methods include: Mass spectrometry Macromolecular crystallography Proteolysis Nuclear magnetic resonance spectroscopy of proteins (NMR) Electron paramagnetic resonance (EPR) Cryo-electron microscopy (cryo-EM) Multiangle light scattering Small angle scattering Ultrafast laser spectroscopy Dual-polarization interferometry and circular dichroism Most often researchers use them to study the "native states" of macromolecules. (wikipedia.org)
  • This dithiol pair attacks the periplasmic N-terminal disulfide bridge at C103 and C109 (C1 and C2, respectively) which transfers electrons to DsbC and other protein electron acceptors as noted above. (wikipedia.org)
  • In order to reverse the reaction, electrons are transferred from dithiol proteins in the periplasm to an electron acceptor in the cytoplasm as follows: reduced proteinperiplasm → DsbAperiplasm → DsbBmembrane → quinonesmembrane → reductasemembrane→ terminal electron acceptorcytoplasm (e.g. (wikipedia.org)
  • newly synthesized
  • The endoplasmic reticulum (ER) is the first organelle in the secretory pathway, and this dynamic and highly specialized organelle contains enzymes and chaperones that mediate the folding and assembly of newly synthesized proteins [ 1 ]. (hindawi.com)
  • cytochrome
  • For cytochrome c and some other proteins, it has been shown that the molten globule state is a "thermodynamic state" clearly different both from the native and the denatured state, demonstrating for the first time the existence of a third equilibirum (i.e., intermediate) state. (wikipedia.org)
  • bovine
  • The drug aprotinin (Trasylol, previously Bayer and now Nordic Group pharmaceuticals), is a small protein bovine pancreatic trypsin inhibitor (BPTI), or basic trypsin inhibitor of bovine pancreas, which is an antifibrinolytic molecule that inhibits trypsin and related proteolytic enzymes. (wikipedia.org)
  • matrices
  • The roles of such proteins include protection and support, forming Connective tissue, tendons, bone matrices, and muscle fiber. (wikipedia.org)
  • globules
  • IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. (wikipedia.org)
  • Misfolding
  • The mechanisms by which protein misfolding leads to disease remains a challenging and medically important problem. (mdpi.com)