By Engelbert Buxbaum
Textbook for classes at either graduate and undergraduate point. additionally for similar classes in biochemistry, biochemistry lab, and techniques. comprises entire analytical description of constitution, biophysics, and serve as of proteins. additionally summarizes the options used to represent protein and protein interactions.
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Extra resources for Fundamentals of Protein Structure and Function
9). This brings the catalytic aspartate residues (D25 in each subunit) together, thus forming the catalytic site of the enzyme. 9. Top: Dimerisation of HIV-protease (PDB-code 1DAZ) occurs by the formation of an antiparallel β-sheet from the ends of both subunits. This brings the 2 catalytic aspartate residues (D25 and D25 ’) close together. Middle: Space ﬁlling model of HIV-Protease. Bottom: Substances with two peptides linked by a stiﬀ backbone can interdigitate into the dimerisation site of a monomer and prevent dimerisation.
Very little is known about the function of such methyl-groups. sulphhydryl-groups to form methyl thioesters. this has been observed on structural proteins, functional signiﬁcance is unknown. No methylation of hydroxy-groups has ever been observed. 34 2 Protein structure ADP-ribosylation using NAD+ as donor. g. pertussis toxin (see ﬁg. 11 on page 258). glucosylation is the binding of single sugar molecules to proteins. 3 on page 115 for a discussion of the medical relevance of this reaction). Similar to ATP-ribosylation it may also be caused by bacterial toxins (produced especially by the genus Clostridium) on Thr-residues of Rho-type small G-proteins, using UDP-glucose as substrate.
Proteins contain a variable amount of hydrophobic amino acids which leads to diﬀerent binding strength to hydrophobic groups (for example butyl- or phenyl-groups) attached to a support matrix. 5 to several M), to maximise interactions with the support. They are eluted with a gradient of decreasing salt concentration, until even very hydrophobic proteins leave the column. In organic chemistry columns with octadecyl-groups (C18 , “reverse phase chromatography”) are used, but it would not be possible to elute proteins from such columns without denaturing them.