Four melanocyte-stimulating hormones have the following amino acid sequences:
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1 Assignment 14: Melanocyte-stimulating hormone belongs to a group called the melanocortins. This group includes ACTH, alpha-msh, beta-msh and gamma-msh; these peptides are all cleavage products of a large precursor peptide called pro-opiomelanocortin (POMC). Alpha-MSH is the most important melanocortin for pigmentation. Four melanocyte-stimulating hormones have the following amino acid sequences: alpha-msh: Ac-Ser-Tyr-Ser-Met-Glu-His-Phe-Arg-Trp-Gly-Lys-Pro-Val-NH 2 beta-msh (human): Ala-Glu-Lys-Lys-Asp-Glu-Gly-Pro-Tyr-Arg-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro- Pro-Lys-Asp beta-msh (porcine): Asp-Glu-Gly-Pro-Tyr-Lys-Met-Glu-His-Phe-Arg-Trp-Gly-Ser-Pro-Pro-Lys-Asp gamma-msh: Tyr-Val-Met-Gly-His-Phe-Arg-Trp-Asp-Arg-Phe-Gly Conserved sequence: parts of the sequence that remain same between species or over time, and therefore probably have more importance to the protein s biological activity. 1. Find the conserved portions of sequences between the two beta-msh hormone peptides. 2. What amino acid residue is different in the middle of this conserved sequence? Does this substitution probably make an important difference in its function why or why not? 3. What would be the expected overall charge on gamma-msh at physiological ph? *note: Sometimes proteins get modified on their ends, as in alpha-msh. A two-carbon acyl unit as been attached to one end, and an NH 2 group to the other end.
2 Growth hormone (GH) is a hormone that stimulates growth and cell reproduction in humans and other animals. It is a 191-amino acid, single chain polypeptide hormone which is synthesized, stored, and secreted by the somatotroph cells within the lateral wings of the anterior pituitary gland. The major isoform of the human growth hormone is a protein of 191 amino acids and a molecular weight of about 22,000 daltons. The structure includes four helices necessary for functional interaction with the GH receptor. GH is structurally and apparently evolutionarily homologous to prolactin and chorionic somatomammotropin. Despite marked structural similarities between growth hormone from different species, only human and primate growth hormones have significant effects in humans. 1. how long is the amino acid chain for the major isoform of GH? 2. what is the class of function of this protein? 3. what levels of protein structure does this writeup indicate? 4. how important is the degree of conservation between species for biological function?
3 Cathepsin (Cathepsin G): cysteine proteases, a type of protein that breaks apart other proteins, found in many types of cells including those in all animals. There are approximately a dozen members of this family, which are distinguished by their structure and which proteins they cleave. Most of the members become activated at the low ph found in lysosomes. Thus, the activity of this family lies almost entirely within those organelles. 1. Just looking at this picture, what can you say about the levels of protein structure? 2. Is this a globular or fibrous protein? 3. The amino acids at the active site are shown in green: what is one residue that is evident? 4. Can you find the N-terminal and the C-terminal? 5. If this a protein that eats up the primary structure of other proteins, what would you say about its danger factor?
4 Cytochrome C551, Pseudomonas aeruginosa 1. Protoporphyrins are related to heme groups. What can you say about the protein structure illustrated here? 2. Is this a globular or a fibrous protein? 3. A residue is shown in yellow. What is the charge on this residue? 4. Where are the N-terminal and the C-terminal?
5 Ranatuerin-2csa: Broad spectrum antibacterial peptide Description ranatuerin-2csa Chain Type polypeptide(l) Length 32 residues DSSP secondary structure 78% helical (4 helices; 25 residues) 1. What features are evident from this information about the peptide shown? 2. What would be the predicted charge on this peptide at physiological ph? 3. Does the amino acid sequence listed seem reasonably consistent with so much alpha helix structure? On the following page: 1. What can be said about the levels of protein structure evident for this protein? 2. How many amino acid residues are there in each chain? 3. How many disulfide links are indicated? 4. Can you identify any N- or C-terminals?
6 Another member of the cathepsin family of proteases. Chain A (polymer 1) Description Chain Type Length CATHEPSIN D polypeptide(l) 97 residues DSSP secondary structure 5% helical (1 helices; 5 residues) 38% beta sheet (9 strands; 37 residues) Chain B (polymer 2) Description Chain Type Length PDP domain assignment CATHEPSIN D polypeptide(l) 241 residues 1LYWBa 54 residues 1LYWBb 187 residues DSSP secondary structure 15% helical (8 helices; 38 residues) 42% beta sheet (22 strands; 102 residues)
Copyright 2008 Pearson Education, Inc., publishing as Pearson Benjamin Cummings
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