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Transcript
Name__________________________ (1 pt) CH 110 Partners Name _______________________(1 pt) 120 pts T A _______________________________ April 22/25, 2008 50 minutes Work Shop 04 YOU ARE FREE TO COLLABORATE WITH YOUR PARTNER AND MAY ASK QUESTIONS OF YOUR TEACHING ASSISTANT. ANSWER EACH OF THE QUESTIONS IN THE SPACE PROVIDED. 12 pts 1) Diagram the general steps in an enzyme mechanism, then explain generally but in some detail how an enzyme converts a free substrate molecule into a free product molecule: 44 pts 2) A protein will be least soluble in water when the pH = _____. The interaction of a protein side group which is acidic with one which is basic will form a ___________. Cysteine residues stabilize tertiary protein structure by forming: _______________________ . A group of hydrophobic side-groups on a protein will cause the chain to _____________________________________. A group of hydrophylic side-groups on a protein will cause the chain to ______________________________________. The secondary structure of a protein has hydrogen bonds between what two entities in the peptide grouping: __________________________________________________________. An a-helix has the hydrogen bond between which aminoacid residues? _____________________________________ (circle) lipids carbohydrates Enzymes are proteins . A cofactor is _________________________________ . The name of an enzyme tells _________________________ . The following are enzyme names, what do these enzymes do? Isomerase ____________________ Hydrolase ________________________ Transferase ________________________ Lyase _________________________ What specifically does an acetylcholineesterase enzyme do? ______________________________________________ . Explain in terms of structure why enzymes work best over very narrow ranges of pH and temperature: __________________________________________________________________________________ __________________________________________________________________________________ __________________________________________________________________________________ . Explain briefly the “lock & key” mechanism of enzyme specificity: ____________________________ _________________________________________________________________________________ _________________________________________________________________________________ __________________________________________________________________________________ . Workshop 04 Page 2 30 pts 3) a) Digest the tetrapeptide below into its component amino acids using strong ACID (HCl(aq), form!!): b) Name each of the amino acids and indicate whether the side groups are nonpolar, polar neutral, acidic, basic. O O O O H3NCHCNHCHCNHCHCNCHCO CH2 CH2 CH2 CH2 CH2 CH2 CH3 C CNH2 O O O CH2 HO CH HCl H2O c) What will be the likely pI of the above tetrapeptide? _____ Is this tetrapeptide predominately hydophylic hydrophobic (circle)? Will this peptide give a positive: Biuret test? ______ ; Xanthopoetic test? ______ 32 pts 4) Describe or define each of the following: a) Primary structure of a protein: b) Secondary structure of a protein:: c) Tertiary structure of a protein: d) Quaternary structure of a protein: e)How does a competitive enzyme inhibitor work? f) How does an allosteric enzyme inhibition/stimulation (regulation) work? g) Make a β-glycosidic linkage with the aminoacid residue: HO H2COH O OH HO HN O C CH3 O + C O H N C CH2 C H H NH h) Draw and explain the general features of tertiary structure of a protein (taking a random coil shape) when it consists of five approximately equal length regions in which three regions are hydrophobic and the other two region is hydrophilic in nature when placed in contact with water: H2O hydrophobic hydrophylic hydrophobic hydrophylic hydrophobic