Ch2 Flashcards
Most of an atom’s mass is
In the nucleus
Atoms come together to form
Every atom was made
Molecules
In a star
What makes the world 3Dimensional
Atoms, since they are 3D structures. They make up molecules that have specific shapes.
FORM=FUNCTION
Covalent Bond
Strongest bond-Not broken by dissolving in water
A bond where electrons are shared in pairs
Polar Covalent Bonds
Electrons are NOT equally shared
Regions have partial charges
Hydrophilic
Non Polar covalent bonds
Electrons are equally shared. Do not dissolve easily in water (lipids)
Hydrophobic
Ionic bond and what 2 kinds
Phillic or phobic
Results from electron transfer
Electron lost-Cation +
Electron gained- Anion -
Dissolves in polar solutions
Hydrophilic
Hydrogen Bonds
Hydrophillic or phobic?
Weaker bond
+ - Attraction between polar molecules
Formed when H bonds with a highly electronegative atom
Hydrophilic
Cohesion
Attraction of H20 molecules to each other
(Hydrogen bonding)
Adhesion
Property of water to stick to other substances through Hydrogen bonds
What allows for surface tension
Cohesion
Solute
Dissolves in a liquid
Solvent
Dissolves solute
Solution
A solute dissolved in a solvent.
Precipitate
A solid that is seperate from the solution
Solubility
How easy/difficult something is to dissolve
Large molecules are ______ because ______.
Water soluble because their outer surface attracts water
Covalent bonds and ionic bonds occupy
Opposite ends of a continuous spectrum, from nearly equal (c) to completely unequal(i) sharing of electrons
How many bonds can an atom have
Multiple
Kinetic energy
Energy of motion
Heat
The measure of total kinetic energy for a given body of matter
Calorie
Unit of heat
Amount of energy needed to raise 1g OF WATER 1C
Specific Heat
Amount of heat that must be absorbed/lost for 1g to change temperature by 1C
Acid
H+ Hydrogen Proton/cation donator
A molecule that DONATES a proton to a solution.
Base
OH-
(H+ acceptor)
Takes H ion from solution and makes it part of the molecule
Salt
Substance that neither donates nor accepts H+
PH is a measure of
The molar concentration of H+ as a whole number.
(Hydrogen ions in a solution )
More H more Acidic
PH formula
pH = Log(1/H+)
Buffer
Substance that prevent drastic change in pH when acids/bases are added
What do buffers do
Replaces strong acids/bases with weak ones that produce less H+/OH-
H+ and OH- are ____ and can
Highly reactive - drastically affect biomolecules (protein shape)
Van der waals interaction
Help reinforce
Attraction/repulsion between molecules
Cause by fluctuations of electron distribution
Help reinforce 3D shape of large molecules
Hydrophobic interactions
Forms the
The tendency of non polar molecules in a polar solvent (like water) to interact with one another
Phospholipid billayer
Hydroxyl Group
-OH
Polar
Hydrophilic
Carbonyl group
> C=O
Polar
Hydrophilic
Carboxyl Group
-COOH
Polar
Forms ionic bonds
Acidic Hydrophilic
Amino group
-NH2
Polar
Hydrophilic
Sulfhydryl Group
-SH
Polar
Hydrophilic
Part of proteins
Phosphate group
-OPO^2- 3 subscript
Polar
Hydrophilic
Methyl group
-CH3
Non polar
Hydrophobic
4 Biomolecules
Carbohydrates
Lipids
Proteins
Nucleic Acids
Carbohydrates are ___ due to ____.
They are classified _______.
What are the types?
Used as a
Polar/Hydrophillic
Abundant hydroxyl groups
By size
Mono,di,and polysaccharides(3+)
Source of energy
Dehydration Reaction
3 steps?
Forms a covalent bond and a water molecule as a product
(Pulls components from both the short polymer and unlinked monomer-forms H20 molecule-Bonds chain)
Hydrolysis Reaction
Adds a water molecule breaking a covalent bond
Linked chain separates into monomer and polymer- An H20 is used- H goes to the polymer, HO to monomer.
For every 1 carbon in a carbohydrate
There is 2H and 10
(And H20)
Saturated fat
If all the Carbon Carbon bonds are SINGLE BONDS
Unsaturated Fat
1 or more C = C double bond present
Healthier
A covalent bond between sugars
Glycosidic bond
Glycosidic bonds are ______. It forms
Dehydration reactions. Forms covalent bond and a H20 molecule.
Glycogen
The sugar storage of polysaccharides
What form do plants store polysaccharides in
Starch
Cellulose
Structural polysaccharides in plants that make up cell walls.
Can not be broken down by the stomach
Chitin
Polysaccharide that provides structural support/creates the exoskeleton of anthropoids
Lipids are composed
They are
Primarily of hydrogen and carbon atoms
Non polar covalent bonds
most hydrophobic
Classes of lipids and their purposes
- Structure- Phospholipids
- Energy source- Triglycerides
- Messengers-Steroids
Triglyceride is made up of
Fatty acid chains make them
Glycerol + 3 Fatty acids
Hydrophobic
Phospholipids are made up of
They make up our
They are
Glycerol and 2 fatty acids
Make up our biological membranes
Amphipathic
(Head-Hydrophillic Tail-Hydrophobic)
What is glycerol
What is a fatty acid
Glycerol- a 3 carbon alcohol
Fatty acid-Long carbon chain (16-18)
Steroids are based off. They act as. They are classified
The cholesterol molecule- chemical messengers. As lipids.
Protein
Polymer of amino acids
There are 20 amino acids
Amino acid Structure
Looks like lungs. Amino group on left, Carboxyl group on right, attached by central carbon. Side chain/R group on top.
R group
Residual groups that have different chemical properties
Differs between each amino acid
Determines if hydrophilic/phobic
Catalyst
Speeds up reaction and remains unchanged
Enzymes
Protein that catalyzes a chemical reaction and remain unchanged
All _____ are ______ but not all ______ are _______
All Enzymes are catalysts but not all catalysts are enzymes
8 Functions of Proteins
- Acceleration of chemical reactions
- Protection against disease (Antibodies)
- Storage of amino acids
- Transport channels
- Hormones
- receptor Proteins
- Motor/contractile proteins
- Structural support
Peptide bond and how is it formed
Covalent bond between amino acids
Formed by dehydration reaction
Peptide vs Protein
Generally 2-50 amino acids (shorter polymer)
Greater than 50 amino acids (larger polymer)
4 structural models
Space filling model
Ribbon model
Wire-frame model
Simplified diagrams
Levels of protein structure
Primary
Secondary
Tertiary
Quaternary
Primary structure
Every protein….
It
The sequence of an amino acids
Has a unique amino acid sequence
Determines other levels of structure
Secondary structures
What 2 shapes
Hydrogen bonding between amino hydrogen of one amino acid + the Carboxyl oxygen of another
alpha helix or Beta pleated sheets
Tertiary stage is the….due to….
Folding occurs in a way that
Formation of bends/loops of polypeptide chain due to interaction between R groups
Amino acids are brought together properly
Quaternary
Brings..
Proteins w more than 1 polypeptide chain
Together 2+ proteins work as a functional unit
Many proteins stay at the
Tertiary level of structure
Myoglobin
What evolved from it
An ancestral protein that makes muscle red. Bonds to oxygen.
Hemoglobin evolved from myoglobin.
Mutations that change Primary Structure
May affect structure and therefore function
Denaturation
What 4 things can cause it
When proteins lose their 3D shape
pH, temperature, salt concentration, an organic solvent
Since proteins renature independently
We determined structure is determined by the amino acid sequences.
The information for how to fold is contained within the PS.
Every covalent bond
Is stored energy.
A proteins 3D shape can
Can change if necessary to fulfill its functions.
Nucleic Acids 2 uses
Polymer or monomer
Form the genetic material of the cell
Aids the transfer of energy in the cell
Polymer of nucleotides
Polymers of nucleic acids
DNA and RNA
Structure of Nucleic acids
- Phosphate group(s)
- 5 Carbon Carbohydrate (ribose/dioxiribose)
- Base containing carbon-nitrogen ring (Nitrogenous base)
Phosphate attached to sugar phosphate backbone
What are the 2 kinds of nitrogenous bases and what goes in each
Pyrimidine Cytosine Thymine Uracil
Purines Adenine Guanosine
How are Nitrogenous bases put together
Polar or non polar
Covalent bonds between the phosphates and sugars
Hydrogen bonds between 2 strands
Non polar
ATP
Monomer or polymer
Adenosine Triphosphate
Adenosine- Adenine+ribose
Monomer and nucleotide
NAD and FAD
Monomers or polymers
Nucleotides. Electron acceptors that carry electrons and energy
Two ends of a nucleic acid polymer
5’ prime beginning of polymer
3’ end
Glucose is the
It is classified as a
Simplest sugar Monosaccharide(carb)
DNA structre
2 polymer chains in an alpha helix.
Antiparrellel arrangement- One 5’ 3’ down the other opposite.
What bases are paired
What holds them together
C-G A-T DNA
C-G A-U RNA
Weak hydrogen bonds-leads to definite 3D shape
RNA vs DNA
Single strand
Ribose not dioxiribose
Uracil is used
Metabolism
All the chemical reactions in a cell
2 kinds of metabolic pathways
They can be
Anabolic - building complex molecules from simple ones
Catabolic- Breaking down complex molecules into simpler ones
Can be interlinked
Potential energy
The energy matter possesses based on its location or structure
(Covalent bonds)
Anytime HC one place LC another-PE
Thermodynamics
Study of energy transformations that occur in a collection of matter
1st law of thermodynamics
Energy can not be created nor destroyed only transformed
2nd law of thermodynamics
Energy transfers/transformations increases the entropy of the universe
Living systems produce entropy->requires energy input to stay ordered
Entropy
Measure of disorder within a system
Delta G definition and formula?
Change in amount of free energy between substrates and products
G(FS)-G(IS)=🔺G
More energy=
In spontaneous change=
Less energy=
Less stable/greater work capacity
Free energy of system released/ can be harnessed for work
More stable/less work capacity
Exergonic Reaction
Energy is released
Favors/Inc entropy due to heat release
Can occur spontaneously
Reactants have more energy than products
Endergonic reactions
Energy is required
Not spontaneous
Reactants have less energy than products
Hydrophillic or Phobic
Lipids
Carbohydrates
Nucleic acids
Proteins
Phobic
Phillic
Phillic
Phillic
There are ___ naturally occurring elements. _____ are essential for human life
92
25
How are radioactive isotopes useful in research
They can be used as tracers to follow particular particles through metabolic pathways
Enzyme activity
4 possible influences
How efficiently an enzyme functions
Temperature, pH, cofactors, inhibitors
International unit of enzyme activity
Amount of enzyme that catalyzes the conversion of 1 micro mole of substrate per minute
Cofactor
Non protein molecule that aids catalysts
Generally metals (zinc, iron, copper)
Coenzyme
Cofactor that is an organic molecule (vitamins)
Helps enzyme
Affinity
The strength of interaction between 2 things
Competitive inhibitor
Blocks the active site and prevents the substrate from binding
Non competitive inhibitor
What is it also called
Changes the structure of the active site leading to weaker bonding affinity
Does not attach to the AS
Allosteric
GFP
Green Florescent Protein
Can be connected to proteins to see where they go in metabolic pathways
