Concept explainers
To draw: The structural formula of a simple amino acid.
Introduction: A
To determine: The importance of the carboxyl group, amino group, and R group.
Introduction: An organic compound is defined as a chemical compound that has carbon and another element. A
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EBK BIOLOGY
- Find a protein of your choice (rcsb.org), choose a part of it (containing at least 30 amino acid residues), find the amino acid sequence (sequence in it), identify what functional groups the amino acid substitutes contain (carboxyl group and 2-position the Nitro group will form amide bonds, forming the covalent basic structure of the protein). What different interactions can occur between these functional groups? How will it relate to the spatial structure of the protein?arrow_forward01 Description Please draw the structure of the 19 L-a-amino acids and proline in any form, as you prefer. You may want to use a letter-size sheet or larger, it's up to you. Guiding principle: You want to understand the differences among amino acids. Although you may want to only draw the R-group it's preferable to draw it along with the rest of the molecule (i.e., the Ca, the amino group and the carboxyl group). Here are some examples (your drawings should not limited to the following styles): NH₂ OH Alanine H H O OH Proline lysine alarmy stock płwłos Tryptophan OH COOH | H₂N-C-H CH₂ Phenylalanine argininearrow_forwardPlease, need help with the explanation and diagram. The structure and properties of poly peptides: A) Describe the type of bonding that would occur when three amino acid monomers (include a diagram of the amino acids) form a tripeptide and describe how such bonds could be formed. B) During the period of Chemical Evolution, what is the significance of the structure of the polymer formed? (Include a diagram)arrow_forward
- use one-letter code for amino acid if needed what is the overall amino acid sequence?arrow_forward* Draw the tripeptide FTQ, making sure to care for stereochemistry.* Identify the N-terminus and the C-terminus of the peptide.* Identify what type of stabilizing interactions the amino acid side chains could employ in the tertiary andquaternary structure of a protein.arrow_forwardDraw the structural formula of a simple amino acid. What is the importance of the carboxyl group, amino group, and R group?arrow_forward
- Show the chemical structure of all 20 amino acids ?arrow_forwardMacmillan Learning Consider the structure of methionine in its +1 charge state. H₂N CH₂ CH₂ CH3 -OH Give the pK, value for the a-amino group of methionine. An answer within ±0.5 units is acceptable. Give the pK, value for the a-carboxyl group of methionine. An answer within +0.5 units is acceptable. Determine the isoelectric point (pl) for methionine. Give your answer to two decimal places. pK (−NH ) = pK₂ (-COOH) = pl = 5.74 2.28 Incorrect 9.21 Incorrect Attemptarrow_forwardGive the names of the 20 Common Amino Acids and draw the structure of each.arrow_forward
- What are the similarities and differences of intermolecular interactions that stabilize secondary versus tertiary structure? Think about types of interactions, side-chain versus backbone interactions, and proximity of the residues involved. The molecule considered is a protein: pancreatic amylase.arrow_forwardWhat is amphoterism? Show using chemical equations the amphoteric property of protein.arrow_forwardConsider the oligopeptide whose structure is shown below: How many peptide bonds are there? Give the complete name of the oligopeptide What is the net charge of the oligopeptide at pH 7? Explain. If you were asked to fragment the oligopeptide with just one enzyme or one chemical reagent, what enzyme or chemical reagent will you use to give the most number of fragments? Show where the peptide bond cleavage will occur.arrow_forward
- Biology (MindTap Course List)BiologyISBN:9781337392938Author:Eldra Solomon, Charles Martin, Diana W. Martin, Linda R. BergPublisher:Cengage Learning