Ch. 2 Biomolecules Flashcards
List the 4 major classes of Biomolecules
Carbohydrates
Lipids
Proteins
Nucleic Acids
List the monomer, covalent bond and the functions for Carbohydrates
Monomer = Monosaccharides
Covalent bond = glycosidic bond
Functions = energy storage, cell structure and communication
List the monomer, covalent bond and the functions for Lipids
Monomer = there is none
Covalent bond = Ester bonds
Functions = stores energy, membrane structure, signaling molecules
List the monomer, covalent bond and the functions for Proteins
Monomer = Amino acids
Covalent bond = Peptide bond
Functions = enzymes are proteins that help chemical reactions happen faster in living things
List the monomer, covalent bond and the functions for Nucleic Acids
Monomer = Nucleotides
Covalent bond = Phosphodiester bond
Functions = helping to make proteins and control cell activities
Describe the ratio of carbon, hydrogen, and oxygen atoms within any monosaccharide
Carbon & Oxygen = for every carbon atom there is one oxygen atom
Hydrogen = roughly twice the number of carbon atoms plus two
Explain why phospholipids are considered amphipathic
Due to the fact they have one part that likes water (head) and one part that avoids water (tails)
Explain why amphipathic phospholipids are important for cell membranes
It creates a flexible protective layer in cell membranes that controls what enter and leaves, keeping the cell safe
Diagram (“block diagram”) the parts of a phospholipid and state whether each part is hydrophilic or hydrophobic
[ Hydrophilic Head ] (water loving)
|
[Hydrophobic Tails] [Hydrophobic Tails] (water repelling)
Describe how many different amino acids are used to make proteins in human cells
20 different kinds of amino acids
Describe the essential properties of the primary structures of proteins
the sequence of amino acids in a protein chain
Describe the essential properties of the secondary structures of proteins
This is how the chain folds into shapes
Describe the essential properties of the tertiary structures of proteins
This is the overall 3D shape of a single protein molecule, formed by the interactions between different parts of the chain
Describe the essential properties of the quaternary structures of proteins
This is how multiple protein chains (subunits) come together to form a larger functional unit
Diagram the parts of a nucleotide (“block diagram”)
+——–+
| Base |
+——–+
|
|
v
+——–+
| Sugar |
+——–+
|
|
v
+——–+
| Phosphate |
+——–+
Describe the chemical bonds that hold the 2 strands of DNA together
Hydrogen Bonds: Hold the base pairs together between the two strands.
Covalent Bonds: Connect the sugar and phosphate along each strand
Which part(s) of a nucleotide interact to form 2 stranded molecules
Nitrogenous Bases: Pair across the two strands.
Sugar-Phosphate Backbone: Forms the structural support on each strand
Compare and contrast the properties of DNA and RNA
DNA: Double-stranded, stores genetic information, has thymine, and mostly stays in the nucleus.
RNA: Single-stranded, helps make proteins, has uracil, and moves around the cell.
Define the essential properties of disaccharides
simple sugars made of two monosaccharides, which is used for quick energy
Define the essential properties of polysaccharides
complex sugars made of many monosaccharides, used for long term energy storage
Which molecule is needed to make steroid lipids?
cholesterol
Be able to identify a steroid ring structure
3 1/2
Define denaturation of protein
Denaturation of a protein is when it loses its normal shape due to changes in conditions like heat, pH, or chemicals
List some of the chemical bond types that help a protein’s tertiary structure to be stabilized
Hydrogen, Disulfide. and Ionic bonds
