Unit 1 Test Flashcards
(55 cards)
1
Q
Hydrogen Bonds
A
Attractive force between a partially positive atom and a partially negative atom. Either N, O, or F
2
Q
Chemical Reactions
A
Changing the arrangements of atoms and ions by breaking and forming chemical bonds
3
Q
Dehydration
A
- AKA Condensation reaction.
- OH from one molecule and H from another break apart while the remaining atoms join together.
- Results in one big molecule and water
4
Q
Hydrolysis
A
- Reverse condensation
- H2O is added to one large molecule to break it apart
- Water is added and two products are created
5
Q
Neutralization
A
- Acid and base added together.
- Produce a water and a salt
6
Q
Redox
A
- Involves reduction and oxidization
- Oxidization: Losing electrons
- Reduction: Gaining electrons
- No electrons=oxidized
- Receives electrons=reduced
7
Q
Properties of water
A
Water is a universal solvent
8
Q
Water form
A
H molecules are closer together
9
Q
Ice form
A
H molecules are further
10
Q
Heat capacity
A
- Amount of energy needed to raise the temperature.
11
Q
Cohesion
A
What allows animals to walk on water
12
Q
Adhesion
A
Allows water to stick to thinks (i.e. xylem)
13
Q
Hydrophobic
A
Not attracted to water (non-polar)
14
Q
Hydrophilic
A
Attracted to water (polar)
15
Q
Amphipathic
A
Contains both polar and non-polar properties
16
Q
Carbs
(monomer, functional group, bond)
A
Monomer: Monosaccharide
Functional group: Carbonyl and Hydroxyl
Bond: Glycosidic linkage
17
Q
Alpha vs beta bonds
A
Alpha: OH is below the plane
Beta: OH is above the plane
18
Q
Carb storage molecules
A
Starches
- Glycogen ans Cellulose
19
Q
Lipids
A
- Do not have a monomer
- Non-polar
- Fatty acids, fats, phospholipids, steroids, and waxes
20
Q
Saturated vs Unsaturated
A
Saturated: All single bonds, unhealthy
Unsaturated: Some double bonds, healthy
21
Q
Proteins
A
Monomer: Amino Acids
Functional groups: Amino group, carboxyl, and an R group
Bonds: Peptide bonds
22
Q
Protein Structure
A
- Primary: Different amino acids are arranged accordingly to form a polypeptide chain
- Secondary: Chains are folded or coiled (alpha helix or beta pleated)
- Tertiary: 3D structure is determined based on the bonds and repulsion of the molecules composition
- Quaternary: Merging of 2 or more polypeptides
23
Q
Denaturation
A
Temperature and pH can impact /alter a protein
24
Q
Nucleic acids
A
Monomer: Nucleotides
Structure: Nitrogenous base, phosphate group, and pentose
Functional group: Phosphate
Bond: Phosphodiester bond
25
Pentose
RNA: Pentose is called Ribose (Ribonucleic acid)
DNA: Pentose is called deoxyribose
(deoxyribonucleic acid)
26
Nitrogen Bases
Adenine, Thymine, Guanine, Cytosine, and Uracil
Thymine is only DNA
Uracil is only RNA
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Families of Nitrogen Bases
Pyrimidines: 6 membered and single ringed
(Cytosine, Thymine, and Uracil)
Purines: 5 and 6 membered joint together, double ringed (Adenine and Guanine)
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Enzymes
Biological catalyst, usually a protein, that changes the rate of a chemical reaction without being changed itself
Purpose: To speed up chemical reactions
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What is the activation energy for enzymes?
Typically it is heat, but too much can lead to denaturation
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Allosteric Inhibitor
(competitive vs non)
Competitive: Bind to the active site and prevent enzyme activity
Non-competitive: Bind somewhere else on the cell which changes the shape, also preventing enzyme activity
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Allosteric Activator
Binds to cell, changes its shape, enhancing enzyme activity (allows the substrate to attach)
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Feedback Inhibition
Prevention of wasting cellular resources being wasted by using excess product of an enzyme inhibitor to slow down production
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Substrate
Reactant substance that is recognized and binds to an enzyme. Tends to be small
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Active site
Specific pocket, grove, or indent in the enzyme where the substrate enters
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E.S complex
Process of an enzyme and substrate binding together
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Activation energy
Minimum amount of energy required to complete a chemical reaction
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Conformation
Enzymes are flexible molecules that change shape to better bind to substrates
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Co factor
Non protein group that binds to an enzyme such as Zn, Cu, or Fe and helps with chemical reactions
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Co enzymes
Organic co factors with similar jobs. Usually derived from water soluble vitamins
40
Saturation level
Enzymes are saturated with substrates and new ones cannot bind to the active site until more enzymes become available
41
Fluid Mosaic Model
Description used to explain the characteristic of the cellular membrane
42
Lipid molecules
sat. vs. unsat.
Saturated: Fatty acids are closer together and the membrane becomes more rigid
Unsaturated: Fatty acids have kinks which make more space available in the membrane and makes it more fluid
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Sterols
AKA cholesterol
They are INSIDE the membrane
High temp: Restrain movement
Low temp: Occupy space to avoid forming a semisolid gel
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Main Molecules in Membrane
Glycolipid: Membrane lipid bound to a carb
Glycoprotein: Membrane component that contains a sugar and is bound to an amino acid
Phospholipid: 2 fatty acid tails linked to a glycerol, phosphate, and a compound
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Membrane Proteins
Help determine the specific function of the membrane
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4 types of membrane protein
1. Transport
2. Enzyme Activity
3. Receptor
4. Anchor
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The two types of membrane protein (in terms of placement on membrane)
1. Transmembrane/integral: Embedded inside the membrane and interacts with the hydrophobic part
2. Peripheral: Only on the surface, interacts with the hydrophilic part
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Passive Transport
Movement of molecules in biological systems that do NOT require energy
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3 Types of Passive Transport
1. Simple diffusion: Substance moves across membrane unassisted
2. Facilitated diffusion: Requires help from transmembrane proteins
3. Osmosis: Movement of water in/out of cells
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Osmosis
Diffusion of water across a semipermeable membrane based on demand and concentration since the solute cannot move
51
Explain Hypotonic, Hypertonic, and Isotonic
Hypotonic: Solution has less solute than the cell-causes the cell to swell
Hypertonic: Solution has more solute than cell-causes cell to shrivel
Isotonic: Equal solute, equal water. Perfect equilibrium
52
Active Transport
Transportation across the membrane with the help of the cell's energy to move materials in and out of the cell
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Exocytosis
Large molecules transported out of the cell with the help of the surrounding phospholipid bilayer engulfing the substances.
Exo=exit
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Endocytosis (and the 3 types)
Importing large molecules from the exterior of the cell to the cytosol
Pinocytosis: Cell brings in water or liquid (think pinot grigio)
Phagocytosis: Cell brings in solid particles (think "f" for food)
Receptor-mediated endocytosis: Outer cell contains surface receptor proteins that recognize and bind to specific molecules, bringing them into the cell
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