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CHAPTER   4   Myoglobin and Hemoglobin: A Study of Protein Structure and Function
 
1.
The ________ is the end of a polypeptide that has a free carboxylate group.

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2.
________ is the asymmetry or "handedness" of a molecule such that it cannot be superimposed on its mirror image.

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3.
A segment of a polymer in which the backbone adopts a regularly repeating conformation is called a/an ________.

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4.
R state and T state are the two conformations of a/an ________.

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5.
A/An ________ is the formation of a covalent bond between two molecules during which the elements of water are lost.

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6.
An accumulation of certain types of insoluble protein aggregates in tissues is a/an ________.

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7.
A loop is a segment of a/an ________, usually found on the protein surface, that joins two elements of secondary structure.

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8.
________ is an enzyme that catalyzes the hydrolysis of peptide bonds.

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9.
________ is a procedure for the stepwise removal and identification of the N-terminal residues of a polypeptide.

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10.
Irregular secondary structure is a segment of a polymer in which each residue has a different ________ conformation.

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11.
The record of the radiation scattered from an object, for example in X-ray crystallography, is called a/an ________.

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12.
A/An ________ is a protein that binds to unfolded or misfolded proteins in order to promote their normal folding.

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13.
In a heteropolymer, the ________ are not all identical.

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14.
________ is the local spatial arrangement of a polymer's backbone atoms without regard to the conformations of its substituent side chains.

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15.
A stretch of polypeptide residues that fold into a globular unit with a hydrophobic core is called a/an ________.

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16.
An ion pair is an electrostatic interaction between two ionic groups of ________ charge.

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17.
________ is the refolding of a denatured macromolecule so as to regain its native conformation.

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18.
An allosteric protein is a protein in which the binding of a/an ________ at one site affects their binding at other sites.

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19.
A group's ________ is determined by the chemical properties of the group's immediate neighbors.

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20.
The fully folded conformation of a macromolecule is its ________.

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21.
In ________ binding, the binding of a ligand at one site on a macromolecule affects the affinity of other sites for the same ligand.

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22.
A/An ________ is an essential organic group that is permanently associated with an enzyme.

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23.
A change of an amino acid residue in a protein to one with similar properties is a/an ________.

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24.
A/An ________ residue in a protein is the same in all evolutionarily related proteins.

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25.
________ is hemoglobin that does not contain bound oxygen or is not in the oxygen-binding conformation.

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26.
The decrease in O2 binding affinity of hemoglobin in response to a decrease in pH is called the ________.

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