draw the structure of the tripeptife Pro-Ser-Cys as it would appear at physiological PH with its C-terminal amino acid residue protected as its methyl ester

What would the order of migration be (bottom to top in the gel) in a SDS-PAGE for the following proteins? Concanavalin A (ConA) (a homotetramer of 106 kDa), lysozyme (a monomer of 14.3 kDa) & horse liver alcohol dehydrogenase (ADH) (a homodimer of 80 kDa). a. ADH, ConA, lysozyme b. ConA, ADH, lysozyme c. Lysozyme, ADH, ConA Od. Lysozyme, ConA, ADH

You are studying how your Lys-Val-Thr tripep de interacts with another pep de, which places an Asp in close proximity to the Lys on your pep de. How would the presence of an Asp side chain affect the pKa of the Lys side chain? Briefly explain your reasoning. (remember pKas are rela ve, pKa=log([H+][A-]/[HA])

The enzyme creatine kinase catalyzes the ATP-dependent phosphorylation of creatine. Propose a mechanism for the reaction described using the curved arrow convention. Show the complete structure of the nucleotide.

Draw the structure of a phosphonamidite monomer suitable for SPPS of adenosine RNA Nucleosides. Circle all protecting groups and identify their canonical deprotection conditions.

EF-G is a macromolecular mimic of EF-tu. It's role in translation is to To cause the large subunit of the ribosome to disassociate with the small subunit of the ribosome Bind to the vacant A-site subsequent to peptide bond formation and resolve the hybrid state of the ribosome To recruit the signal recognition particle (SRP) to the ribosome and to facilitate synthesis of membrane proteins O To cause the large subunit to associate with the small subunit of the ribosome Shuttle an amino-acylated tRNA to the A site to initiate the peptidyl transfer reaction

What would the following sequence of dodecapeptide M be? My best guess would be option C

One of the most common features of anion binding sites is the presence of an a-helical structure. Using a schematic diagram of a helix, describe what you've observed. The direction of the dipole and the N-terminus of the helix should be clearly indicated. Show the (general) base structure of the glutamic acid functional group side chain.

The diagram to the right illustrates the inter-actions of the amino acid side chains of two a-helical polypeptide strands in a coiled-coil, viewed end-on and projected along the helix axes from the N-terminal to the C-terminal end. Are the macrodipoles of the two a- helices oriented parallel or anti-parallel? For this projec- tion is the positive end of the macro-dipole in the sur- face of the paper or below the surface? f C b g e d a' a d' g b' f'

The folding of intrinsically disordered proteins is prevented by the presence of Ser, Lys, and Glu residues. What do these amino acids have in common? Why do they disrupt IDPs?