Anatomy & Physiology: The Unity of Form and Function (Standalone Book)
7th Edition
ISBN: 9780073403717
Author: Kenneth S. Saladin Dr.
Publisher: McGraw-Hill Education
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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.
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
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.
Chapter 2 Solutions
Anatomy & Physiology: The Unity of Form and Function (Standalone Book)
Ch. 2.1 - Prob. 1BYGOCh. 2.1 - Prob. 2BYGOCh. 2.1 - Prob. 3BYGOCh. 2.1 - Prob. 4BYGOCh. 2.1 - Prob. 5BYGOCh. 2.1 - Prob. 1AYLOCh. 2.1 - Prob. 2AYLOCh. 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 - Prob. 9AYLOCh. 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 - Prob. 1AYLOCh. 2.2 - Prob. 2AYLOCh. 2.2 - Prob. 3AYLOCh. 2.2 - Prob. 4AYLOCh. 2.2 - Prob. 5AYLOCh. 2.2 - Prob. 6AYLOCh. 2.3 - Prob. 12BYGOCh. 2.3 - Prob. 13BYGOCh. 2.3 - Prob. 14BYGOCh. 2.3 - Prob. 15BYGOCh. 2.3 - Prob. 1AYLOCh. 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 - Prob. 1AYLOCh. 2.4 - Prob. 2AYLOCh. 2.4 - Prob. 3AYLOCh. 2.4 - Prob. 4AYLOCh. 2.4 - Prob. 5AYLOCh. 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 - Prob. 12AYLOCh. 2.4 - Prob. 13AYLOCh. 2.4 - Prob. 14AYLOCh. 2.4 - Prob. 15AYLOCh. 2.4 - Prob. 16AYLOCh. 2.4 - Prob. 17AYLOCh. 2.4 - Prob. 18AYLOCh. 2.4 - Prob. 19AYLOCh. 2.4 - Prob. 20AYLOCh. 2.4 - Prob. 21AYLOCh. 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. 1TFCh. 2 - Prob. 2TFCh. 2 - Prob. 3TFCh. 2 - Prob. 4TFCh. 2 - Prob. 5TFCh. 2 - Prob. 6TFCh. 2 - Prob. 7TFCh. 2 - The higher the temperature is, the faster an...Ch. 2 - Prob. 9TFCh. 2 - Prob. 10TFCh. 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_forwardIndicate 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_forward
- This structure of a protein comes from the further bending and folding of pleated sheets and helices: A. primary B. secondary C. tertiary D. quaternaryarrow_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_forwardThe structure of a protein results from the folding ofthe pleated sheets or helices.a. primary c. tertiaryb. secondary d. quaternaryarrow_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_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_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_forward
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