Chapter 2 Flashcards
What is the monomer for polysaccharides?
Sugars
What is the monomer for nucleic acids?
Nucleotides
What is the monomer for proteins?
Amino Acids
What is the monomer for lipids?
Fatty acids
What are Cis fats?
Type of double bond found in nature and leads to bending
What are trans fats?
Straighter fatty acids that are solid at room temperature
What is hydrogenation?
A process that results in double bonds in the trans orientation
What is a saturated fat?
Fatty acids with only single bonds
What is an unsaturated fat?
Fatty acids with double bonds
What do cholesterol and steroids function as?
Signaling molecules
How can cholesterol and steroids move through membranes?
Because they have no charge
What does cholesterol do?
Functions as a buffer for membranes
What is an amphipathic and what is an example?
Molecules that have both charged and uncharged portions.
Ex: detergents
What is a micelle?
Simplest structure in which water surrounds a single layer of phospholipids
What is a liposome and how do they assemble?
Bilayer structure used for delivery of small molecules or drugs assembled based on hydrophobic forces
What 3 components make up a Nucleic Acid?
Phosphate group, sugar, and nitrogenous base
What is a nucleic acid without the phosphate group called?
Nucleoside
Cytosine, thymine, uracil
Prymides
Adenine, guanine
Purines
What is the difference between prymides and purines?
Prymides are single ringed while purines have two rings
NAD+
Electron carrier for Kreb’s cycle
FAD
Secondary electron carrier
What are the components of an amino acid?
Amino group, carboxyl group, and a side chain
What is a polypeptide?
Long chain of amino acids
Describe polar charged.
1) Can form ionic bonds
2) Hydrophillic side chain can act as acids or bases
3) Active sites of enzymes
Which amino acids are in the polar charged group?
Aspartic Acid Glutamic Acid Lysine Arginine Histidine
Describe polar uncharged.
1) Form H- bonds
2) Associate with water
3) Hydrophillic side chains tend to have a partial (-) or (+) charge which allows for chemical reactions
Which amino acids are polar uncharged?
Serine Threonine Glutamine Asparagine Tryosine
Describe non polar.
1) Hydrophobic side chain consists of C and H’s
2) Act as the inner core of soluble proteins
3) Associate with the lipid bilayer
Which amino acids are non polar?
Alanine Valine Leucine Isoleucine Methionine Phenylalanine Tryptophan
Which amino acids are the only proteins that phosphate groups can bind to?
Serine, Threonine, and Tryosine
Which amino acids have side chains with unique properties?
Glycine
Cysteine
Proline
Alanine
Ala, A
Valine
Val, V
Aspartic Acid
Asp, D
Glutamic Acid
Glu, E
Lysine
Lys, K
Arginine
Arg, R
Histidine
His, H
Leucine
Leu, L
Isoleucine
lIe, I
Methionine
Met, M
Phenylalanine
Phe, F
Tryptophan
Try, W
Serine
Ser, S
Threonine
Thr, T
Glutamine
Gln, Q
Asparagine
Asn, N
Tryosine
Try, Y
Glycine
Gly, G
Cysteine
Cys, C
Proline
Pro, P
What is a protein?
Large macromolecules that can contain 1 or more polypeptide chain
Who developed the primary structure for amino acids?
Frederick Sanger
Who was one of the only people who has won 2 individual noble prizes and developed the secondary structure for proteins?
Linus Pauling
What is the tertiary structure of proteins?
The organization of alpha helices and beta sheets into complex structures
What is the primary structure of proteins?
The sequencing of amino acids
What is the secondary structure of amino acids?
Alpha Helices, Beta sheets, and a combination of both
Give an example of a protein that only contains alpha helices
Myoglobin
Give an example of a protein that only contains beta sheets
Green fluorescent protein
Give an example of a protein containing both beta sheets and alpha helices
RAS
What is the quaternary structure of proteins?
Made up of multiple polypeptide chains
What are molecular machines and give an example.
Multi-protein interactions
Ex: ATP Synthase
What hold protein domains together?
Intermolecular forces
What are the characteristics of protein domains?
1) Proteins are modular
2) Proteins independently fold
3) Domains are associated with a function
What is an interactome?
The entire collection of all interactions in the cell
How are interactions within the cell described?
By a network map
What are hub genes and why are they important?
In a network map, they are the genes that most of the arrows point to. They are important because a lot of theses genes are crucial to essential functioning within the cell
What is a proteome?
The entire inventory of all proteins in the cell
What are proteomics?
The study of all proteins in a cell by high computer assisted techniques
What are thermodynamics?
The study of changes in energy in relation to events in the universe
What are bioenergetics?
Specific to the transformation of energy within the cell
What is the 1st Law of Thermodynamics?
Energy is conserved, energy cannot be created or destroyed
What is the 2nd Law of Thermodynamics?
The tendency towards disorder (entropy)
How is energy conserved at a cellular level?
Through catalysts
What are catalysts?
Substances that stress chemical bonds and accelerates reactions in the forward or reverse reactions
What are the biological catalysts?
Enzymes
What did the Romans do and when?
In the first century, they used glass lenses as magnifiers
What did Hans and Zaccharias do and when?
In the 1590s, they built the first microscope
What did Anton Van Leeuwenhoek do and when?
In the mid 1600s, he improved lens grinding and increased magnification from 50 x to 270x
What is the interacome?
The entire collection of all interactions in the cell.
Name the three ways enzymes work.
1) Aligning the reactants to decrease activation entropy
2) Changing the reactivity of the substrate
3) Stress or alter the conformation of the substrate
Why does thermodynamics matter in life?
Because cells are highly organized, therefore a lot of energy is needed to keep the organization
Who came up with the graph used to measure enzyme activity?
Leonor Michaelis and Maud Menten
How do reactions want to proceed?
To the lowest state of energy (entropy)
Enzymes remain_________________after reactions.
The same
What do enzymes sometimes require?
Cofactors such as metals to act as proton donors
What are irreversible inhibitors?
Work by binding to an enzyme and reducing or eliminating its ability to catalyze a reaction
What are Competitive Inhibitors?
They depend on the substrate and inhibitor to determine the velocity
What are noncompetitive inhibitors?
Concentration of inhibitors determine reaction
What is anabolism?
The synthesis of macromolecules
What is catabolism?
The disassembly of macromolecules. ——>
What does a negative delta G mean?
The reaction will occur spontaneously
What does a positive delta G mean?
The reaction needs energy to occur
