Which of the following pairs of amino acids can have intermolecular hydrogen bonding between the functional groups in their side chains? Select all that apply. phenylalanine and tyrosine two tyrosine residues serine and threonine alanine and threonine
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Which of the following pairs of amino acids can have intermolecular hydrogen bonding between the
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phenylalanine and tyrosine
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two tyrosine residues
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serine and threonine
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alanine and threonine
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- Compare the molecular property of amino acids and their roles in protein folding. Hydrophilic acids Arginine Asparagine Aspartic Acid Cysteine Glutamic acid Glutamine Glycine Histidine Lysine Serine Threonine hydrophobic acids Alanine Isoleucine Leucine Methionine Phenylalanine Proline Tryptophan Tyrosine ValineWhich of the following statements best describes the hydrophobic character of bacteriorhodopsin (2BRD)? Both the interior and exterior of the protein are hydrophobic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, including the central core of the trimer. Both the interior and exterior of the protein are hydrophilic, but the central core of the trimer is hydrophobic. Both the interior and exterior of the protein are hydrophobic, but the central core of the trimer is hydrophilic.Exercise A: Amino Acid Functional Groups Figure 1 below shows one of the 20 amino acids that make up proteins. Recall that carbon can form four covalent bonds. Amino acids consist of a central carbon, called the a-carbon, that is bonded to four different chemical groups. H + CH2 OH Figure 1. Structure of an amino acid Answer the below questions in your own document. • On the amino acid shown in Figure 1, label the a-carbon. • The a-carbon of each of the 20 amino acids is bonded to one hydrogen atom, one amino group, one carboxyl group, and one R group (more on that below). You should recognize the amino and carboxyl groups from our discussion of functional groups in organic molecules. Circle and label* the amino group and the carboxyl group in Figure 1. *Note: our goal in this question, and in similar questions throughout this lab, is for you to be able to identify specific structures. You can do this circling/labeling in whatever way is easiest for you. You might want to draw the…
- Drag each of the following items into the corresponding boxes to indicate the protein structural level that is predominantly affected by the chemical interactions listed. Some items may be placed in more than one box. Reset Help Hydrogen bonds between polar groups in amino acid side chains Hydrophobic interactions between amino acid side chains lonic bonds between positively- charged and negatively-charged amino acid side chains Peptide bonds Hydrogen bonds between carbonyl oxygens and amino nitrogens within a polypeptide backbone Disulfide bonds Primary structure Seconday structure Tertiary structure Quaternary structureT/F: The titration curve for serine will have 2 inflection points. T/F: The Amino Acid D-selenocysteine has an R-Configuration T/F: Each water molecule can form H bonds with 4 other water molecules T/F: In a buffer system, decreasing the concentration of the conjugate base relative to acid makes the buffer more acidic T/F: Glycine forms good interactions in a protein structure True or false?Please clearly identify each numbered amino acid side chain, below. Your description should include the name or 3 letter code for the amino acid and the type (i.e., chemical class) of the amino acid. 1 4 OH OH CH, CH, CH2 CH2 CH, "H,N-C-C-0 "H,N-C-C-0 "H,N-C-C-0 _0-5-5-N H. H O H O HO но
- Each ionizable group of an amino acid can exist in one of two states, charged or neutral. The electric charge on the functional group is determined by the relationship between its pKa and the pH of the solution. This relationship is described by the Henderson-Hasselbalch equation. Lysine has three ionizable functional groups. The pKa for these groups are pK1 = 3.1, pK2 = 8.3 and pKR = 10.8. 1. Draw the structures of the predominant ionization state of Lysine at pH 1, 4, 8, and 12. Calculate also the net charge of each of these ionized molecules. Show your work. 2. Calculate the isoelectric point (pI) of Lysine in aqueous solution using the pKa values given above. Explain the rationale of your calculations and show your work.Amino acids are the building blocks for proteins in the cell. The structures of the amino acids glutamate (or glutamic acid), glycine, and leucine are provided below in the same order from left to right. Map any chiral centers with a 1.Aspartic acid has a side chain bearing a carboxylic acid group; its pK, is ~4. The alpha-carboxylic and alpha-amino groups have pk, values similar to those of alanine, - 2 and ~9, respectively. Determine the net charge on an aspartic acid molecule at the following pH values (match each pH to the best choice). pH = 1 [ Choose ] pH = 2 [ Choose ] pH = 4 [ Choose ] pH = 7 [ Choose ] pH = 9 [ Choose ] pH = 13 [ Choose ] > > >