Use LEFT and RIGHT arrow keys to navigate between flashcards;
Use UP and DOWN arrow keys to flip the card;
H to show hint;
A reads text to speech;
17 Cards in this Set
- Front
- Back
|
Enzymes |
A protein serving as a catalyst, a chemical agent that changes the rate of reaction without being consumed by the reaction |
|
|
Catalyst |
A chemical agent that changes the rate of a reaction without being consumed by the reaction |
|
|
Polypeptides |
A polymer (chain) of many amino acids linked together by peptide bonds |
|
|
Protein |
A three-dimensional biological polymer constructed from a set of 20 different monomers called amino acids |
|
|
Amino Acid |
An organic molecule possessing both carboxyl and amino groups. Amino acids serve as the monomers of proteins |
|
|
Peptide Bond |
The covalent bond between two amino acid units, formed by a dehydration reaction |
|
|
Primary Structure |
The level of protein structure referring to the specific sequence of amino acids |
|
|
Secondary Structure |
The localized, repetitive coiling or folding of the polypeptide backbone of a protein due to hydrogen bond formation between peptide linkages |
|
|
Alpha (α) Helix |
A spiral shape constituting one form of the secondary structure of proteins, arising from a specific hydrogen-bonding structure |
|
|
Beta (β) Pleated Sheet |
One form of the secondary structure of proteins in which the polypeptide chain folds back and forth. Two regions of the chain lie parallel to each other and are held together by hydrogen bonds |
|
|
Tertiary Structure |
Irregular contortions of a protein molecule due to interactions of side chains involved in hydrophobic interactions, ionic bonds, hydrogen bonds, and disulfide bridges |
|
|
Hydrophobic Interaction |
A type of weak chemical bond formed when molecules that do not mix with water coalesce to exclude the water |
|
|
Disulfide Bridges |
A strong covalent bon formed when the sulfur of one cysteine monomer bonds to the sulfur of another cysteine monomer |
|
|
Quaternary Structure |
The particular shape of a complex, aggregate protein, defined by the characteristic three-dimensional arrangement of its constituent subunits, each a polypeptide |
|
|
Denaturation |
In proteins, a process in which a protein unravels and loses its native conformation, thereby becoming biologically inactive. In DNA, the separation of the two strands of the double helix. Denaturation occurs under extreme conditions of pH, salt concentration, and temperature |
|
|
Chaperonin |
A protein molecule that assists the proper folding of other proteins |
|
|
X-ray Crystallography |
A technique that depends on the diffraction of an X-ray beam by the individual atoms of a molecule to study the three-dimensional structure of the molecule |
