Anatomy & Physiology: An Integrative Approach
2nd Edition
ISBN: 9780078024283
Author: Michael McKinley Dr., Valerie O'Loughlin, Theresa Bidle
Publisher: McGraw-Hill Education
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Question
Chapter 2.8, Problem 38WDYL
Summary Introduction
To determine:
The reason that the amino acid Leucine classified as a non polar amino acid.
Concept introduction:
The Leucine is the amino acid which is used in the biosynthesis of proteins. The leucine consists of α – amino group and α – carboxylic acid.
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Are all the amino-acids soluble in water? Explain why?
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Note: Reference the Naturally occurring amino acids data table for additional information.
Identify the amino acids contained in each of the following tripeptides.
Chapter 2 Solutions
Anatomy & Physiology: An Integrative Approach
Ch. 2.1 - What subatomic particles determine the mass of an...Ch. 2.1 - Diagram the atomic structure of chlorineatomic...Ch. 2.1 - Do isotopes represent the same element? Do they...Ch. 2.1 - Prob. 4WDYLCh. 2.2 - List the common cations and anions of the human...Ch. 2.2 - Prob. 6WDYLCh. 2.2 - Explain how and why ions form based on the octet...Ch. 2.3 - Could an ionic bond form between two cations or...Ch. 2.3 - Prob. 9WDYLCh. 2.3 - What is an isomer?
Ch. 2.3 - Explain covalent bond formation in terms of...Ch. 2.3 - Assign the partial charges between nitrogen and...Ch. 2.3 - Why are some covalent bonds nonpolar and others...Ch. 2.3 - Are O2, and CO2 nonpolar or polar molecules?Ch. 2.3 - What is the name of the intermolecular attraction...Ch. 2.4 - What is the intermolecular bond that is...Ch. 2.4 - Which property of water contributes to the need to...Ch. 2.4 - How does the interaction of a nonelectrolyte and...Ch. 2.4 - How do phospholipid molecules interact with water...Ch. 2.5 - Explain why water is neutral.Ch. 2.5 - Which type of substance releases H+ when added to...Ch. 2.5 - What is the general relationship of [H+] and pH?Ch. 2.5 - Why are buffers important and how do they function...Ch. 2.6 - Prob. 24WDYLCh. 2.6 - Why is blood also considered the other two types...Ch. 2.6 - What are four ways solution concentration may be...Ch. 2.7 - Prob. 27WDYLCh. 2.7 - What functional groups may act as an acid?Ch. 2.7 - What defines a polymer? List the three...Ch. 2.7 - Do lipid molecules typically dissolve in water?...Ch. 2.7 - Which class of lipids forms cell membranes? What...Ch. 2.7 - What is the repeating monomer of glycogen? Where...Ch. 2.7 - For each of the following, indicate if it is a...Ch. 2.7 - What is the general function of nucleic acids?Ch. 2.7 - What are the structural differences between RNA...Ch. 2.7 - What are the monomers of proteins and the name of...Ch. 2.7 - Prob. 37WDYLCh. 2.8 - Prob. 38WDYLCh. 2.8 - What distinguishes the tertiary and quaternary...Ch. 2.8 - What happens to a protein when it denatures? How...Ch. 2 - Prob. 1DYKBCh. 2 - _____ 2. Substances that dissolve in water include...Ch. 2 - _____ 3. Temperature stabilization is dependent...Ch. 2 - _____ 4. All of the following are accurate about...Ch. 2 - _____ 5. Blood is a mixture that is more...Ch. 2 - Prob. 6DYKBCh. 2 - _____ 7. Glucose is stored as which molecule...Ch. 2 - _____ 8. All of the following are common ions of...Ch. 2 - _____ 9. Intermolecular attractions between polar...Ch. 2 - _____ 10. When a protein permanently unfolds, it...Ch. 2 - List the common ions of the human body by name,...Ch. 2 - Describe a polar bond and a polar molecule.Ch. 2 - Diagram two water molecules and label the polar...Ch. 2 - Compare and contrast what occurs when a substance...Ch. 2 - Define the terms acid, base, PH, and buffers.Ch. 2 - Explain the units for expressing a concentration...Ch. 2 - List the four organic biomolecules and the...Ch. 2 - Which two organic biomolecules contain nitrogen...Ch. 2 - Describe how phospholipid molecules form the...Ch. 2 - Explain protein denaturation, including bow it...Ch. 2 - Which property of water is significant in children...Ch. 2 - Prob. 2CALCh. 2 - Prob. 3CALCh. 2 - The condition of rickets involves bones that have...Ch. 2 - The hormone insulin is a __________ composed of...Ch. 2 - An individual is exposed to high-energy radiation....Ch. 2 - The lab results from a diabetic patient show a...Ch. 2 - Prob. 3CSL
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- The following are structural diagrams of a selection of newly discovered amino acids. OH -の-CHs NH HO C-OH NH, AN-CH CH2 CH2 OH Ho NH, C=0 a) Select 1 amino acid. Redraw it. Label the alpha carbon and circle/highlight the entire backbone of the amino acid. b) The amino acids are part of a channel protein embedded in the cell membrane. Choose 2 amino acids (from above) that you would expect to find within the interior/middle of the cell membrane. Draw the formation of the dipeptide using the 2 amino acids you selected. Identify the other products formed in the reaction.arrow_forwardIn each of the following pairs of amino acids, identify which amino acid would be more soluble in water: (a) Ala, Leu; (b) Tyr, Phe; (c) Ser, Ala; (d) Trp, Hisarrow_forwardWhy is it important to specify the three-dimensional structure of amino acids?arrow_forward
- Glycine is an amino acid whose side group does not participate in any of the types of side group interactions we discussed in class. Briefly explain why this amino acid's side group does not interact with the side groups of other amino acids.arrow_forwardWhy is methionine (Met) not found on the inside of a protein even though it is hydrophobic?arrow_forwardDespite being hydrophobic, why is methionine (Met) not located within a protein?arrow_forward
- Porcine dynorphin is a neuropeptide having 17 amino acid residues. Its structure is shown below. Tyr-Gly-Gly-Phe-Leu-Arg-Arg-Ile-Arg-Pro-Lys-Leu-Lys-Trp-Asp-Asn-Gln How does trypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C-terminal end. List down the different fragments that would result if dynorphin were cleaved by trypsin. . How does chymotrypsin catalyze the hydrolysis of peptides? You can answer this question by identifying the amino acids involved and whether the hydrolysis is at their amino side or the carboxyl side or if particular amino acids end up at the N-teminal end or at the C- terminal end. List down the different fragments that would result if dynorphin were cleaved by chymotrypsin. . Cyanogen bromide is a chemical reagent which also cleaves peptide bonds. What is/are…arrow_forwardWhich functional group(s) shown above is (are) present in all amino acids?arrow_forwardAll L amino acids have an S absolute configuration except L - cysteine, which has the R configuration. Explain why L - cysteine is designated as having the R absolute configuration.arrow_forward
- The peptide cys-leu-glu-ala-cys-lys is at pH 7 in oxidizing conditions. Part a) Draw the peptide's titration curve. Part b) What would the pI of the peptide be around?arrow_forwardTwo of the 20 common amino acids have two chiral carbon atoms in their structures. Identify these amino acids and their chiral carbon atoms.arrow_forwardWhich among the 20 standard amino acids has more than one chiral carbon? Draw its structure and indicate with asterisk the second chiral carbon. Is it polar or non-polar? Is it essential or non-essential?arrow_forward
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