Anatomy and Physiology
9th Edition
ISBN: 9781260256000
Author: SALADIN
Publisher: MCG
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Textbook Question
Chapter 2, Problem 8TYR
The arrangement of a polypeptide into a fibrous or globular shape is called its
- a. primary structure.
- b. secondary structure.
- c. tertiary structure.
- d. quaternary structure.
- e. conjugated structure.
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Students have asked these similar questions
The level of protein structure that describes all aspects of the three-dimensional folding of a polypeptide is referred to as the
A. quaternary structure.
B. secondary structure.
C. primary structure.
D. tertiary structure.
Both alpha-helices and beta-sheets (select any/all answers that apply):
A.
are examples of secondary structure.
B.
are stabilized by hydrogen-bonds between backbone atoms.
C.
are examples of tertiary structures.
D.
never contain proline residues.
E.
are commonly found in proteins.
A. A macromolecule composed of one or more
polypeptides
B. The monomer of polypeptides.
C. The specific sequence of amino acids in a
polypeptide.
D. Structure of coils and/or folds of a
polypeptide strueture.
E. Structure of polypeptide resulting from
interactions between R-groups. Contributes to
unique 3D shape of molecule.
F. Two or more polypeptides interacting to form
a single functional unit.
1. Protein
2. amino acid
3. primary structure
4. secondary structure
5. tertiary structure
6. quaternary structure
Chapter 2 Solutions
Anatomy and Physiology
Ch. 2.1 - Prob. 1BYGOCh. 2.1 - Prob. 2BYGOCh. 2.1 - Prob. 3BYGOCh. 2.1 - Prob. 4BYGOCh. 2.1 - Prob. 5BYGOCh. 2.1 - The definition of chemical element; the six most...Ch. 2.1 - The structure of an atom and the special...Ch. 2.1 - Prob. 3AYLOCh. 2.1 - Prob. 4AYLOCh. 2.1 - Prob. 5AYLO
Ch. 2.1 - Prob. 6AYLOCh. 2.1 - Prob. 7AYLOCh. 2.1 - Prob. 8AYLOCh. 2.1 - Hew isomers resemble and differ from each otherCh. 2.1 - Prob. 10AYLOCh. 2.1 - Prob. 11AYLOCh. 2.2 - Prob. 6BYGOCh. 2.2 - Prob. 7BYGOCh. 2.2 - Prob. 8BYGOCh. 2.2 - Prob. 9BYGOCh. 2.2 - Prob. 10BYGOCh. 2.2 - Prob. 11BYGOCh. 2.2 - How the biologically important properties of water...Ch. 2.2 - Prob. 2AYLOCh. 2.2 - The differences between solutions, colloids, and...Ch. 2.2 - Prob. 4AYLOCh. 2.2 - The action and physiological function of buffersCh. 2.2 - Prob. 6AYLOCh. 2.3 - Prob. 12BYGOCh. 2.3 - Prob. 13BYGOCh. 2.3 - Prob. 14BYGOCh. 2.3 - Prob. 15BYGOCh. 2.3 - The definition of energy, and the two basic forma...Ch. 2.3 - Prob. 2AYLOCh. 2.3 - Prob. 3AYLOCh. 2.3 - Prob. 4AYLOCh. 2.3 - Prob. 5AYLOCh. 2.3 - Prob. 6AYLOCh. 2.4 - Prob. 16BYGOCh. 2.4 - Prob. 17BYGOCh. 2.4 - Prob. 18BYGOCh. 2.4 - Prob. 19BYGOCh. 2.4 - Prob. 20BYGOCh. 2.4 - Prob. 21BYGOCh. 2.4 - Prob. 22BYGOCh. 2.4 - Prob. 23BYGOCh. 2.4 - Prob. 24BYGOCh. 2.4 - The criterion for considering a compound to be...Ch. 2.4 - Prob. 2AYLOCh. 2.4 - The structures of hydroxyl, methyl, carboxyl,...Ch. 2.4 - The difference between monomer and polymera; how...Ch. 2.4 - The defining characteristics of carbohydrates end...Ch. 2.4 - Prob. 6AYLOCh. 2.4 - Prob. 7AYLOCh. 2.4 - Prob. 8AYLOCh. 2.4 - Prob. 9AYLOCh. 2.4 - Prob. 10AYLOCh. 2.4 - Prob. 11AYLOCh. 2.4 - Differences between a dipeptide, oligopeptide,...Ch. 2.4 - Prob. 13AYLOCh. 2.4 - Prob. 14AYLOCh. 2.4 - What defines a conjugated protein; the general...Ch. 2.4 - Prob. 16AYLOCh. 2.4 - How enzymes differ from ether proteins, and the...Ch. 2.4 - Prob. 18AYLOCh. 2.4 - Prob. 19AYLOCh. 2.4 - The term for a chain of linked enzymatic...Ch. 2.4 - The basic structural components of adenosine...Ch. 2.4 - Prob. 22AYLOCh. 2.4 - Prob. 23AYLOCh. 2.4 - Prob. 24AYLOCh. 2 - A substance that ____ is considered to be a...Ch. 2 - Prob. 2TYRCh. 2 - Prob. 3TYRCh. 2 - Prob. 4TYRCh. 2 - Prob. 5TYRCh. 2 - Prob. 6TYRCh. 2 - Prob. 7TYRCh. 2 - The arrangement of a polypeptide into a fibrous or...Ch. 2 - Prob. 9TYRCh. 2 - Prob. 10TYRCh. 2 - Prob. 11TYRCh. 2 - Dietary antioxidants are important because they...Ch. 2 - Prob. 13TYRCh. 2 - Prob. 14TYRCh. 2 - A chemical reaction that joins two organic...Ch. 2 - Prob. 16TYRCh. 2 - Prob. 17TYRCh. 2 - Prob. 18TYRCh. 2 - Prob. 19TYRCh. 2 - Prob. 20TYRCh. 2 - Prob. 1BYMVCh. 2 - Prob. 2BYMVCh. 2 - Prob. 3BYMVCh. 2 - Prob. 4BYMVCh. 2 - Prob. 5BYMVCh. 2 - Prob. 6BYMVCh. 2 - Prob. 7BYMVCh. 2 - Prob. 8BYMVCh. 2 - Prob. 9BYMVCh. 2 - Prob. 10BYMVCh. 2 - Prob. 1WWTSCh. 2 - Prob. 2WWTSCh. 2 - Prob. 3WWTSCh. 2 - Prob. 4WWTSCh. 2 - Prob. 5WWTSCh. 2 - Prob. 6WWTSCh. 2 - Prob. 7WWTSCh. 2 - The higher the temperature is, the faster an...Ch. 2 - Prob. 9WWTSCh. 2 - Prob. 10WWTSCh. 2 - Suppose a pregnant women with serve morning...Ch. 2 - Prob. 2TYCCh. 2 - Prob. 3TYCCh. 2 - How would the bodys metabolic rate be affected if...Ch. 2 - Prob. 5TYC
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- Large globular proteins frequently are comprised of two or more recognizable structures that often confer unique functions or properties. These structures are termed: a quatemary structure b. domains c. heterotropic d. multimeric e à andearrow_forwardWhich of the following statements is/are TRUE for globular proteins? A. sensitive to changes in pH & heat B. regular amino acid sequence C. soluble in water D. structural rolearrow_forwardThis structure of a protein comes from the further bending and folding of pleated sheets and helices: A. primary B. secondary C. tertiary D. quaternaryarrow_forward
- Indicate which of the following are present in the primary, secondary, tertiary, and quaternary structures ofproteins: a. peptidebonds b. hydrogen bonds between adjacentpeptides c. hydrogen bonds within a singlepeptide d. hydrophobic interactions e. association of four polypeptide chainsarrow_forwardWhich of the following is incorrect? a. The overall shape of an entire polypeptide including all its side chains is called its tertiary structure b. Only multimeric proteins have quaternary structure C. The amino acid sequence of a protein is called its primary structure d. None; all the other choices are correctarrow_forwardIn order to study protein structures and functions, many protein techniques have been developed for specific applications. Which of the following pair of technique: application is INCORRECT? a. Mass Spectrometry: protein molecular weight b. SDS-PAGE: protein structure c. X-ray crystallography: protein structure d. NMR: protein structure e. Peptide mass fingerprinting: protein presence and identificationarrow_forward
- Proteins often have regions that show specific, coherent patterns of folding or function. These regions are called: a. domains. b.oligomers. c. peptides. d. sites. e. subunits.arrow_forwardMatch the level of protein structure to its description: Primary Secondary Tertiary Quaternary A. Folding due to interactions among the peptide backbone B. Interactions among multiple polypeptide chains C. Sequence of amino acids D. Folding due to interactions among side chainsarrow_forwardIn proteins, which of the following are the characteristic patterns that arise when hydrogen bonds form between amino acids? A. Quaternary structure. B. Tertiary structure C. Primary structure D. Secondary structurearrow_forward
- The tangled shape of a polypeptide is its ________ structure, which gives it maximum stability. A. primary B. secondary C. tertiary D. quaternary E. denaturalizedarrow_forwardThe three-dimensional conformation of a protein may be strongly influenced by amino acid residues that are very far apart in sequence. This relationship is in contrast to secondary structure, where the amino acid residues are: a. always side by side. b. generally near each other in sequence. c. invariably restricted to about 7 of the 20 standard amino acids. d. often on different polypeptide strands. e. usually near the polypeptide chain's amino terminus or carboxyl terminus.arrow_forwardWhich of the following describes the tertiary structure of proteins? A. Helices and sheets formed from hydrogen bonds between the amino acids of polypeptides B. The functional domains that form from interactions between different parts of the polypeptide C. The association of multiple polypeptides D. The linear sequence of amino acids making up the polypeptidearrow_forward
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