Protein Structure Worksheet PartI Complete the following tasks- be sure to bring your completed work to class as we will continue to work on this question in class. A. Locate the parts of the amino acids that participate in the chemical reaction that links the amino acids together in a covalent bond. Lysine Cysteine Serine Н H. H 11 N-C-C он сн, =0 N-C-C I Н OH H ҫH, Он Cн, 2 2 SH ҫн, OH сн, ҫн, NH2 2 2 I I - C- N I-C-CIC- I I O- I I /\
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Locate the parts of the amino acids that participate in the
Serine
Cysteine
Lysine
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- GABA (B) Need help answering these questions about the GABA(B) protein. What class (globular, fibrous, membrane) protein is the protein Identify the organism (or organisms that have this protein) Identify the cellular location of this protein Describe the function Find the primary structure (list it on a slide) Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein) Find a picture of the tertiary structure (which should also show secondary structure) Does the protein have a quaternary structure, if so what is it?Solve only the specific amino acid number and percent (%) Difference. Thank you so much♥[Ten - Biomolecules] INSTRUCTIONS — Answer the following multiple-choice questions and EXPLAIN in 3-5 sentences why you chose that answer. — Answer properly Questions; Thomas was purifying an enzyme from a homogenate of muscle cells. He went through seven steps of purification and found that the enzyme activity was the same as the homogenate value. On the eighth step, when the protein washighly pure, the enzyme activity rose to five times that of the homogenate value. Can you suggest a possible reason? A. the homogenate assay was wrong B. step eight has co-purified an activator of the enzyme. C. the enzyme has an inhibitor present in the muscle cell homogenate D. the temperature at step eight was just right for the enzyme activity.
- Question 1Predicting Secondary Structure Which of the following peptides is more likely to take up an -helical structure, and why? (a) LKAENDEAARAMSEA (b) CRAGGFPWDQPGTSNPlease ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?Question for protein crystallography- 1. While performing a routine protein crystallization screening, you observe that one of your well drops has doubled in size compared to the remaining wells. Note: the drop in question was set up by taking 1 µL of the protein solution (10 mg/mL LDH in 20 mM TRIS pH 7.5, 0.5 M NaCl and 10% PEG 4000K) and adding it to 1 µL of the crystallization solution (10% PEG 4000K, 50 mM NaCl and 20 mM TRIS pH 8.0). Why did this drop grow larger in size compared to when you initially set it up?
- PLEASE HELP 1. How many chirality centers does ribose have? Identify them.Biomaterial question: Give a brief and clear answer, please a. Briefly describe the structural differences between the three major types of biomaterials, including their chemical structure, bonding characteristics, crystal structures, etc. b. Explain briefly the working principle and the information provided by the spectroscopic and chromatographic characterization techniques . Give an example to each of them.Text:QUESTION 16 Protein maturation in the ER includes. A Disulfide bond formation B. proteolytic cleavage C attachment of oligosaccharide d. Prolyl isomertzation
- based on this oligopeptide (KEQSCMV) would someone be able to help me on the following questions? What moieties within oligopeptide are those mainly responsible for the formation of an alpha-helix? Name the process that leads to the unfolding of the alpha helix to yield a random coil. State and justify, for oligopeptide, which amino acid side chains will be involved in: hydrophilic interactions, hydrophobic interactions, disulphide bridges and salt bridges. In each case, briefly justify your choice.Good day can you please help me with the question below. Your assistance will be highly appreciated. Explain how the spectroscopic properties of amino acids can be used to quantify protein using UV light.What are different kind of forces present in primary , secondary and Tertiary structure of protein . what are different kinds of amio acid or side chain involve in protein folding and how they work. ( please answer both plzzzz , in detail simple language plzz)