Chapter 3 Flashcards
Organic molecules
Carbon-containing molecules that are found in all forms of life
4 major classes of organic molecules
- Lipids
- Carbohydrates
- Proteins
- Nucleic acids
Of the 4 major classes of organic molecules, which of the three are macromolecules?
Carbohydrates, proteins, and nucleic acids
Organic Chemistry
The science of carbon-containing molecules
Condensation reaction
A chemical reaction that involves two or more molecules combining into a larger molecule by covalent bonding, with the loss of a small molecule
Dehydration reaction
A type of condensation reaction, where a water molecule is lost in the linkage process
Hydrolysis reaction
The process of breaking down a polymer, in which a water molecule is added back each time a monomer is released
How many shells of electrons does carbon have?
Two
Stereoisomers
Isomers that have identical bonding relationships but a different spatial arrangement of atoms
Carbohydrates such as ____, ____ and ____ are polymers of glucose.
cellulose; glycogen; starch
What are the functions of fats in living organisms?
- Support cushion for organs
- Energy storage
- Insulation
____ is a type of lipid that consists of a glycerol molecule attached to one ____ group and two ____ ____.
Phospholipid; phosphate; fatty acids
The polar hydrophilic region of a phospholipid molecule is composed of…
Glycerol backbone, phosphate group, and the charged nitrogen-containing region
The molecular structure of wax
A long hydrocarbon chain resembling a fatty acid attached by its carbonyl group to another long hydrocarbon chain
The tertiary structure of a polypeptide is predominantly determined by its ____ structure
Primary
For polypeptide chains, hydrogen bonds can form ____ a polypeptide and ____ different polypeptide chains
Within; between
Disulfide bridges are covalent bonds between ____ groups of cysteine side chains
Sulfhydryl (-SH)
Like hydrogen bonding in polypeptides, disulfide bonds can form between two cysteines located ____ the polypeptide chain or in ____ chains
Between; different
When a protein is denatured, ____, ____ and ____ bonds are broken, but the ____ bonds still remain intact for linking adjacent amino acids
Disulfide; Hydrogen; Ionic; peptide
Structural isomers
Isomers with the same atoms but with different bonding relationships
Cis-trans isomers
Isomers have identical bonding relationships but hydrogen atoms are positioned differently around a double bond
Enantiomers
Isomers have identical bonding relationships but the atoms are positioned differently, resulting in mirror images
What are isomers?
Molecules that have identical molecular formulas but different structures
What are isotopes?
Forms of the same atom that differ in the number of neutrons they contain
Triglycerides (fats) are composed of…
Glycerol covalently bound to three fatty acids
The composition of a phospholipid molecule
A head that is polar and hydrophilic, and two tails that are non-polar and hydrophobic
3 major structural components of an amino acid
- Amino group (single nitrogen atom bonded to 2 hydrogen atoms)
- Nitrogenous base (adenine, cytosine, guanine, thymine and uracil)
- Carboxyl group (combination of 2 functional groups attached to a single carbon atom, namely, hydroxyl (single-bonded OH) and carbonyl (double bonded O) groups)
What are the bonds and interactions that contributes directly to a protein’s tertiary structure?
- Ionic bonds
- Van der Waals forces
- Disulfide bonds
- Hydrogen bonds
- Hydrophobic effect
The chemical structure of a typical amino acid found in a protein
A central carbon atom bounded to an amino group, carboxyl group, a side chain, and a hydrogen atom
Proteins are made by ____ reactions
Dehydration
During a dehydration reaction, ____ bond forms between two sugars, while ____ bond forms between amino acids
Glycosidic; peptide
In a peptide bond, which parts of the two amino acids are joined together?
The amino group of one and the carboxyl group of the other
Primary structure of a protein
The sequence of amino acids in a polypeptide
Secondary structure of a protein
The repeating pattern of folding between regions
Tertiary structure of a protein
The three-dimensional shape of a single polypeptide chain
Quaternary structure of a protein
The interactions between two or more polypeptide chains
Ribozymes
RNA enzyme that catalyzes a chemical reaction
“Catalytic RNAs that cut things, make things, and do odd and useful jobs”