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noncovalent interactions are
weak but collectively strong enough to define the folded structure of a protein
in a folded polypeptide, nonpolar side chains
tend to cluster at the core of the protein and away from the aqueous surrounding, leaving the polar and charged side chains at the surface
polar and charged amino acids tend to be at the
regions of proteins that are exposed to the aqueous surrounding
hydrogen bonds in polypeptides
can be formed to the polar side chains on the outside of the molecule
maturation of proteins involves
correct folding, proteolytic cleavage, chemical modifications, formation of quaternary structures, association with co-factors
elastin fibers allow tissues such as skin, arteries and lungs to
stretch and recoil without tearings
TSEs are a family of
fatal brain diseases characterized by lesions that appear as small cavities (spongy appearance)
Ex. of TSEs
scrapie (sheep), mad-cow disease (cattle), and Creutzfeldt-Jakod disease (CJD), or kuru ("to tremble with fear") (humans)
TSEs protein only hypothesis
diseases are caused by incorrectly folded versions of the prion protein
several strains of prions exist
variations of the prion protein tertiary structure that are also infectious
insulin protein: connecting polypeptide is removed after
disulfide bonds are made, result = mature insulin
two levels of protein regulation:
regulation of gene expression (determines the amount of protein produced by the cell by limiting transcription and or translation), control of protein function (the protein is synthesized by its activity is restricted according to the needs of the cell
what activates PKA by binding to the regulatory subunits, causing the release of the catalytic subunits?
the kinase activity of the released catalytic subunits (in PKA) do what?
phosphorylate multiple effector proteins
feedback inhibition: allosteric regulation:
a change in the conformation of a protein that affects its activity due to the binding of regulatory molecule
feedback inhibition: the end product of a biosynthetic pathway does what?
inhibits the enzyme that catalyzes the first step of its synthesis, causing the entire pathway to shut down
a small protein that is attached to a target protein and is a label for regulation or destruction
ubiquitylation and proteasomal degradation: a ubiquitin ligase enzyme attaches several
ubiquitins to the target protein
ubiquitylation and proteasomal degradation: a cap domain of the proteasome (a protease complex)
recognizes the polyubiquitylated target protein
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