Number 3 answer. I think its the amino acids that dont belong in 20 major amino acids. I hope you can help me. Thank you.
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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?Many bioactive compounds are derived from amino acids. This compound, found in trace amounts in mammalian brains and hypothesized to play a role as a neuromodulator or neurotransmitter, is derived from an amino acid through removal of the backbone carboxylic acid group. The amino acid from which it is derived must be: (Write out the entire name; Spelling matters, but case does not; Do not include L- or D- in the name; For acidic amino acids write the full name, e.g. “so-and-so acid”)Non-standard amino acids are derived from common amino acids by biochemical modifications. Please identify the chiral centers of given non-standard amino acids.
- Please ASAP. Thank you. How does the mutation change/affect the structure of the Hb heterotetramer (ie how is quaternary protein structure affected)?GABA (B) protein Need help answering questions about the GABA(B) protein. What is the primary structure Describe secondary structure (alpha-helix, beta sheet, and how many of each and what percent of the total protein)What is the tertiary structure (which should also show secondary structure)Does the protein have a quaternary structure, if so what is it?I was given an amino acid position 564 with the PDC code 2V1X. Would it be possible to describe why this position in the protein is important and outline the effects the mutation will have on the structure / function of the protein? Thank you.
- Consider the peptide Trp-Arg-Glu-Cys-Gly-Tyr. For the drawings requested below, please show them in zig-zag style, from amino to carboxy terminus, with correct stereochemistry Draw the predominant form at pH = 2 Draw the predominant form at pH = 5 Draw the predominant form at pH = 7 Draw the predominant form at pH = 12Asp-Gly-Lys-Glu-Ile-Phe Draw its full chemical structure as it would exist at pH = 7.0. Draw an arrow pointing to each peptide bond. Identify the net charge of the peptide and briefly explain how you arrived at this answer.How many carbon atoms are present in the R group in each of the following standard amino acids? Please see picture. Thank you!
- A small protein has a sequence ACNCKAAPMLCARYCAMLH. The structure of this single peptide is stabilized by the formation of two separate disulfide bonds, but the locations of those disulfide bonds are unknown. In order to determine the location, you purify this peptide and treat it with trypsin (cleaves peptide bond at long, positively-charged side chains). Tryptic digestion generated two peptides. Based on this result, determine the location of the –S-S– bonds. Show them in a diagram on the sequence by connecting the corresponding residues. Explain your reasoning.Topic: ISOLATION AND CHARACTERIZATION OF PROTEINS 1. Which amino acids contains the following:a. Sulfur/sulfhydryl groupb. Aromatic groupc. Imidazole ringd. Guanidine groupe. Indole ring2. Classify the following proteins to their biological functions (casein, albumin, gluten, andmyoglobin) 3. Which level of protein structure organization are lost hydrolysis and denaturation?4. What is the Beer-Lambert’s Law? Why is it relevant to the quantitative analysis of proteins?Using the biosynthesis of aminolevulinate (ALA) as an example, describe at least two techniques that can be used to elucidate detail of a biosynthetic pathway. Please keep brief - 5 sentences/dot points max.