Human Physiology: An Integrated Approach (8th Edition)
8th Edition
ISBN: 9780134605197
Author: Dee Unglaub Silverthorn
Publisher: PEARSON
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Chapter 4.3, Problem 9CC
Summary Introduction
Introduction: Proteins are the polypeptide chains that are made up of amino acids which are linked by peptide bonds. The complexity in the chain of amino acids determines the structure of a protein. There are four levels of protein structures, namely primary, secondary, tertiary, and quaternary.
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Students have asked these similar questions
Select the term in column B which best matches the description in column A. There are more terms then
needed.
Column A
Column B
1. The pentose sugar found in DNA.
a) Cis fatty acid
b) Trans fatty acid
c) Coenzyme
d) Cofacipr
2. Commonly referred to as "insoluble fiber".
3. Considered to be an amphipathic molecule.
4. A molecule with the formula C18H3602 is probably a
e) Phospholipid
5. Bond created during the formation of the primary structure of a protein.
) Glycogen
6. A non-protein organic molecule needed for proper enzyme functioning.
g) Cellulose
7. Pyrimidine base found only in RNA.
h) Galactose
i) Fructose
8. Increasing the number of these molecules in the cell membrane would
increase the permeability of the cell membrane.
i) Thymine
k) Uracil
9. Bond which connects nucleotide monomers together.
1) Fatty acid
m) Disaccharide
n) Peptide bond
o) A-Helix
p) B-Pleated Sheet
q) Ribose
r) Deoxyribose
10.
(iii) Draw a structural diagram of a hydrogen bond between β-D-glucose and the side chain of any polar residue in a protein.
(iv) Name the type of bond that can occur between the axial hydrogens of glucose and the indole ring of tryptophan. Draw a structural diagram of this bond.
(v) Comment on the polar / apolar nature of the bond in part (iv) and explain why this type of interaction is prevalent in protein-sugar complexes.
Answer (iii) to (v) please.
The major secondary structure seen in collagen is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive
The major secondary structure seen in hemoglobin is: a) alpha helix b) beta sheet c) collagen helix d) random coil or nonrepetitive
Although all of these play a part in protein folding, the one which contributes the most is: a) salt bridges b) hydrogen bonds c) Van der Waals interactions d) hydrophobic effect
Chapter 4 Solutions
Human Physiology: An Integrated Approach (8th Edition)
Ch. 4.1 - Which biomolecules always include nitrogen in...Ch. 4.1 - Prob. 2CCCh. 4.1 - What is the difference between potential energy...Ch. 4.1 - Prob. 4CCCh. 4.2 - Prob. 5CCCh. 4.2 - Prob. 6CCCh. 4.2 - Prob. 7CCCh. 4.3 - Prob. 8CCCh. 4.3 - Prob. 9CCCh. 4.3 - Prob. 10CC
Ch. 4.3 - Prob. 11CCCh. 4.4 - Name five ways in which cells regulate the...Ch. 4.4 - Prob. 13CCCh. 4.4 - Prob. 14CCCh. 4.4 - Match each component on the left to the...Ch. 4.4 - Prob. 16CCCh. 4.4 - How is the separation of mitochondria into two...Ch. 4.4 - Prob. 18CCCh. 4.4 - Prob. 19CCCh. 4.4 - Prob. 20CCCh. 4.4 - What does the name RNA polymerase tell you about...Ch. 4.4 - Explain in one or two sentences the relationship...Ch. 4.4 - Prob. 23CCCh. 4.4 - List three general types of posttranslational...Ch. 4.4 - Prob. 25CCCh. 4 - List the three basic forms of work and give a...Ch. 4 - Prob. 2RQCh. 4 - Prob. 3RQCh. 4 - Prob. 4RQCh. 4 - Prob. 5RQCh. 4 - Prob. 6RQCh. 4 - Match each definition in the left column with the...Ch. 4 - Prob. 8RQCh. 4 - Organic molecules that must be present in order...Ch. 4 - In an oxidation-reduction reaction, in which...Ch. 4 - Prob. 11RQCh. 4 - Prob. 12RQCh. 4 - Prob. 13RQCh. 4 - Metabolic regulation in which the last product of...Ch. 4 - Prob. 15RQCh. 4 - Prob. 16RQCh. 4 - Create maps using the following terms.Ch. 4 - Prob. 18RQCh. 4 - Prob. 19RQCh. 4 - Prob. 20RQCh. 4 - Prob. 21RQCh. 4 - Briefly describe the processes of transcription...Ch. 4 - On what molecule does the anticodon appear?...Ch. 4 - Is the energy of ATPs phosphate bond an example of...Ch. 4 - Prob. 25RQCh. 4 - Prob. 26RQCh. 4 - Prob. 27RQCh. 4 - Prob. 28RQ
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Similar questions
- Disulfide bridges can form in proteins that are in an oxidizing environment. They form between what amino acid residues? a.) Between cysteine residues that are close in three-dimensional space, but not necessarily close in the primary structure b.) Always between cysteine residues between protein subunits c.) Between cysteine residues that are adjacent in the the primary structure d.)They will occur between any two cysteine residues in a protein e.) Between a methionine and a cysteine residuearrow_forwardThe difference between cholesterol molecule and the hopanoid molecule in bacteria is that the hopanoids are: a) hydrophobic b) hydrophilic c) hopanoids have five rings in their chemical structure d) cholesterol has 5 rings in their chemical structure e) c & darrow_forwardIn the peptide Ala – Gly – Val – Phe – Tyr, a carboxylate (-COO-) group would bound in which amino acid? A) Gly b) Ala c) Phe d) Tyr Which amino acid forms disulfide bonds? A) Met b) Cys c) Arg d) Pro The sequence Gly-Pro-Pro is often found in collagen. This would be a description of: a) primary structure b) secondary structure c) tertiary structure d) quaternary structurearrow_forward
- Which of the following membrane lipids have a direct glycosidic linkage between the head- group sugar and the backbone glycerol? a) Ether lipids b) Sphingolipids c) Glycolipids d) Phospholipids (Ctrl) - Tarrow_forwardWhich of these amino acids could be found in the transmembrane portion of a protein? a) asparticacid b) cysteine c) glycine d)isoleucine e) prolinearrow_forwardAlthough all of these may play a part, the major driving force in protein folding is: a) hydrogen bond formation b) salt bridge formation c) steric interactions d) the hydrophobic effect A partially folded protein is called a a) peptide template b) active domain c) molten globule d) precursor protein Which of these processed is NOT seen in protein denaturation? A) subunits are dissociated b) folding is unraveled c) alpha helix and beta sheets are unraveled d) peptide bonds are broken. A protein which has more than one stable conformation is called a: a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein If a denatured protein does not spontaneously renature upon removal of denaturing agents, it may require a ____ to renature. a) chaperone protein b) molten globule c) flexible protein d) inherently unstructured protein Prion protein and amyloid protein have which trait in common? A) They denature very easily…arrow_forward
- Describe the following levels of protein organization and give an example of each: A.) Primary B.) Secondary C.) Tertiary D.) Quarternaryarrow_forwardWater-soluble proteins such as myoglobin tend to fold such that: A) hydrophobic amino acids R-groups are on the interior of the protein and hydrophilic groups are on the outside OB) all peptides form hydrogen bonds with water. C) hydrophilic amino acid R-groups are on the interior of the protein and hydrophobic groups are on the outside. O D) hydrophilic and hydrophobic amino acid R-groups form hydrogen bonds with each other.arrow_forwardO-linked glycosylation occurs on ___ residues of proteins. a) Serine and Threonine b) Asparagine c) Methionine d) Acidic amino acid residuesarrow_forward
- Which of the following group of membrane lipids predominate in plant cells?a) Galactolipidsb) Sphingolipidsc) Glycerophospholipidsd) Archaebacterial ether lipidsarrow_forwardGlucose is stored as glycogen (a polymer) in some eukaryote cells (such as liver cells or muscle cells). This cellular storage is performed A) by an enzyme that causes dehydration synthesis in a specialized organelle, B) by a carbohydrate in a liposome, C) by a dehydration enzyme and stored as fat in an adipose cell, D) exocytosis of the glycogen, E) as glucose stored in the nucleus by special genes in the DNA.arrow_forwardIn the deoxy state, Histidine forms an ______ salt bridge with aspartate and an ______ salt bridge with lysine in the deoxidized state. a) Intra-chain; Intra-chain b) Intra-chain; inter-chain c) Inter-chain; Inter-chain d) Inter-chain; Intra-chainarrow_forward
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