LLNSAMSRLYSLRSS 1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6? 2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein? 3. at ph7 which amino acid side chain can form ionic bonds.
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LLNSAMSRLYSLRSS
1.Assuming this sequnce is enitrely alpha helical what is the hydrogen bond donor to the carbonyl oxygen of Met6?
2.what amino acids in the sequnce above would most likely face the hydrophoic core od a protein?
3. at ph7 which amino acid side chain can form ionic bonds.
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- The first and major effect in denaturation of proteins is that: a. peptide bonds break. b. helices unwind. c. sheet structures unfold. d. tertiary structure is changed. e. quaternary structures disassemble.N. HN H3N Where on this amino acid does it attach to a primary sequence of a protein and where is the ionizable position of the R group?8) The figure shows an unfolded polypeptide consisting of six amino acids. Describe how cooperativity will drive protein folding of the polypeptide chain into an alpha-helixe- 10EEHOW is AG changed as each amino acid is incorporated into the secondary structure - s)? O H O H 3 H. H. 5 CH-C H. 6 -N-CH-C- OH O H,N CH-C -N CH C-N CH CH CH2 CH2 CH2 CH2 CH OH CH H;C CH3
- -100 100 8. This is a helical wheel projection. The following amino acids of your protein were predicted to participate in an alpha helix: DRMVEHACKSI. a. Plot these amino acids in the helical wheel projection below. b. Is the alpha helix in your protein hydrophobic, amphipathic or hydrophobic? c. Would you expect this helix to be on the interior of the protein, exposed, or partially exposed?Tt O 8. What are the driving forces that promotes tertiary -3D and quaternary -4D structure formation of proteins. Provide specific examples of the interactions that drive the formation of 3D and 4D structures?1 Draw a general sketch ( backbone only ) of a protein alpha- helix and a beta shet. 2 why do heat and acid denature protein 3 what rae the forces tha drive the formation of secondary and tertiary protein structure. Using your amino acid table, draw two of th epossible interactions. 4 what are enzyme and how they work? Discuss one example of how enzyme catalyze reactions. Also, provide an example of inhibition NOTE- PLEASE DO NOT EXPLAIN TOO MUCH EXPLAIN TO THE POINT EXPLAIN IN SHORT GIVE ANSWER TO THE STRAIGHT POINT.
- 1 Draw the following polypeptide: Met- Tyr-Val-Ser-Asn 2A Draw the hydrolysis of a dipeptide consisting of phenylaline and glutamic acid. 2B What are the fuctional group present in the side chains of the amino acids.( phenylalanine and glutamic acid) 2C are the sidechains in part 2B hydrophobic or polar 2D where would you expect to find them ( surface or interior of a protein) ? why ?. In glycoproteins, what are the three amino acids to whichthe carbohydrate groups are most frequently linked? Towhat functional group is the glycan linked in each case?A protein has been sequenced after cleavage of disulfide bonds. The protein is known to contain 3 Cys residues, located as shown below. Only one of the Cys has a free –SH group and the other two are involved in an -S-s- bond.
- 0ミレーNレ NH geometry on both cand N. Torigonal plannes CH - C-N o=), HN CH2 CH-C-OH (a- carbon) CH2 HooC Aspaxagine - Toline - Valine - Arginine - phenylalcmine - Glutamic ocid. 1.Give the name and three letter code for each amino acid in the peptide. e 2. At pH 7, approximately what charge would be on your peptide? Explain your answer. 3. Can your peptide form intra/interchain disulfide bonds? Explain why/why not. e 4. Will your peptide absorb UV and is it fluorescent? Explain why/why not. e 5. What is the probability that your peptide contains a cis peptide bond? Explain your answer.3. Amino Acid Sequence and Protein Structure Our growing understanding of how proteins fold allows researchers to make predictions about protein structure based on primary amino acid sequence data. Consider the following amino acid sequence. 1 3 5 6 7 8 9 10 Ile - Ala - His - Thr - Tyr - Gly - Pro - Phe-Glu – Ala- - 11 12 13 14 15 17 20 Ala - Mat - Cys- Lys - Trp - Glu-Ala-Gln-Pro - Asp- 16 18 19 21 22 23 24 25 26 27 28 Gly - Met-Glu - Cys - Ala - Phe - His - Arg (a) Where might bends or ß turns occur? (b) Where might intrachain disulfide cross-linkages be formed? (c) Assuming that this sequence is part of a larger globular protein, indicate the probable location (external surface or interior of the protein) of the following amino acid residues: Asp, lle, Thr, Ala, Gln, Lys. Explain your reasoning.S1.What functional group (pictured below) is used in the formation of ATP, the backbone of DNA, and the plasma membrane? R. - HO- asluolom OgH 910m ansa obyd to inuoms adisi69 101 P- Hnedenoi HO 9tom anisinos H 19w 1639 eniv blut viend ou nontel:oceansied bol-ngtsl s19 1591 a. Amino b. Carbonyl c. Ester d. Phosphate e. Alcohol Sabios onime Tertio of bensemoo Insietib ti aolem tsrll blas onims ns to neg at to quang ly snodibod for ogh quotg
