Chapter 5: Q18CP (page 126)
Explain the origin of orthologous proteins, paralogous proteins, and multidomain proteins.
Short Answer
Orthologous and paralogous protein origin is gene duplication, and multidomain protein origin is sequence variation.
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Chapter 5: Q18CP (page 126)
Explain the origin of orthologous proteins, paralogous proteins, and multidomain proteins.
Orthologous and paralogous protein origin is gene duplication, and multidomain protein origin is sequence variation.
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(a) In what order would the amino acids Arg, His, and Leu be eluted from a carboxymethyl column at pH6 ?
(b) In what order would Glu, Lys, and Val be eluted from a diethylaminoethyl column at pH 8?
Identify the first residue obtained by Edman degradation of cytochrome c from (a) Drosophila, (b) baker’s yeast, and (c) wheat germ (see Table 5-6).
Electrospray ionization mass spectrometry (ESI-MS) of proteins involves creating positively charged ions of the protein and separating them according to their mass-to-charge ratio (m/z).
(a) What causes the different positive charges on different particles of the protein?
(b) The amino acid composition (in numbers of residues per chain) of hen egg-white lysozyme (HEWL) is as follows:
P 2 Y 3 N 14 H 1
D 7 M 2 L 8 E 2
C 8 R 11 G 12 F 3
A 12 I 6 K 6 V 6
S 10 W 6 T 7 Q 3
What is the maximum positive charge that can be present on a HEWL ion?
You wish to determine the sequence of a short peptide. Cleavage with trypsin yields three smaller peptides with the sequences Leu–Glu, Gly–Tyr– Asn–Arg, and Gln–Ala–Phe–Val–Lys. Cleavage with chymotrypsin yields three peptides with the sequences Gln–Ala–Phe, Asn–Arg–Leu–Glu, and Val–Lys–Gly–Tyr. What is the sequence of the intact peptide?
Explain how you could use a column containing carboxymethyl groups to separate serum albumin and ribonuclease A(see Table 5-3).
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