BIOCHEMISTRY ASSIGNMNET Scholarship Essay Example | Topics and Well Written Essays - 2750 words

BIOCHEMISTRY ASSIGNMNET - Scholarship Essay ExampleSci-Tech Encyclopedia information ab give away ion exchange McGraw-Hill Encyclopedia of Science and Technology. copyright 2005 by The McGraw-Hill Companies, IncCarl R. Kemnitz and Mark J. Loewen J. Am. Chem. Soc. 2007 129(9) pp 2521 - 2528 http//www.expasy.ch/http//www.brenda.uni-koeln.dehttp//www.genome.ad.jp/dbget-bin/www_bgetec1.5.1.34Biochemistry Manual from http//mcb.berkeley.edu/UniProtKB/TrEMBL Release 35.5 of 15-May-2007UnitProt Taxonomy Browser. http//www.ebi.ac.uk/newt/displayProtein Spotlight, 2004. Swiss Institute of BioinformaticsQ1. (30 marks) The following peptide, substance Z, was isolated from whale intestinal mucosa GAKKIYPRVSACMIHGGAVIAIDMDGTDA The industrious peptide is amidated on the C-terminal amino dose. Draw the structure of the amidated amino acid residue. (5) The following reagents act on this peptide. Write out the products for each treatment, using the one-letter amino acid abbreviations. (6) a. Trypsi n GAK---K---IYPR---VSACMIHGGAVIAIDMDGTDA b. Dansylchloride (first products) GAK---KIYPRVSACMIHGGAVIAIDMDGTDAc. Cyanogen bromide. GAKKIYPRVSACM---IHGGAVIAIDM---DGTDAPeptide Z is an inactive precursor. It is converted to the active peptide by hydrolysis with chymotrypsin. The larger product of the hydrolysis is the active peptide. Draw the structure of the active peptide. (8) GAKKIYPRVSACM---IH---GGAVIAIDM---DGTDAQ2. (30 marks) a) Read up about leucine secure proteins and answer the following questions. Keep answers brief. - What is the characteristic structural feature of these proteins What forces elapse the zipper zipped up These proteins are characterized by two helices that look like a zipper with leucine residues lining on the inside of the zipper. The hydrophobic interactions of the branched range of mountains of the...In this way, the larger molecules of the inactive peptide would not be able to bind to the stationary frame and therefore, will be eluted first. And after th is, a strong acid exchanger can be used to facilitate the dissociation of the active peptide with the stationary phase.Enzyme employment at 5 hours was measured as DA min-1 = 0.15. The protein concentration of the stock enzyme solution used for the checkout of activity was 50 mg ml-1. Details of the assay are given in Q4. Assume e for the product was 800 L mol-1 cm-1 at the wavelength used, and measurements were made in a cuvette of 1 cm light path. head the specific activity of the enzyme after it had been treated for 5 hours at 25o. Express your answer as mmoles product produced per minute per mg protein. Set all your calculations out clearly.Peptide Z is an inactive precursor. It is converted to the active peptide by hydrolysis with chymotrypsin. The larger product of the hydrolysis is the active peptide. Draw the structure of the active peptide. (8)- What is the characteristic structural feature of these proteins What forces keep the zipper zipped up These proteins are charac terized by two helices that look like a zipper with leucine residues lining on the inside of the zipper. The hydrophobic interactions of the branched chain of the leucine residues keep the helices in place.- What is the role of the zipper in these proteins - In pri