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Central Dogma Theory
- Every cell in the body has the same DNA
- Different cells express different subset
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What determines all rxns in the cell?
Plasma Membrane
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Simplest eukaryote:
yeast
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Rough ER differences from smooth
- Ribosomes
- protein synthesis
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Smooth ER differences from Rough
- no ribosomes
- lipid synthesis
- Ca2+ storage
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Cytosol:
Solutions with dissolved substances such as glucose, CO2, O2, ect.
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Cell fractionation:
- takes cells apart and separates the major organelles from one another
- -centrifuges and enables scientists to determine the functions of organelles
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Structure/Function Paradigm:
the shape dictates the function
-
Bioenergetics
- Order and work requires energy
- external energy must be converted into usable forms
-
Central DOgma of Molecule Biology
DNA->RNA->Proteins
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Plasma Membrane Comp and Func:
- Phospholipid bilayer with embedded proteins
- Selective passage of molecules into and out of cell
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Nucleus comp and func:
- Nuclear envelope surrounding nucleoplasm, chromatin, and nucleolus
- Storage of genetic information
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Nucleolus comp and func:
- Located within nucleus
- Concentrated area of chromatin, RNA, and proteins
- Site for ribosome synthesis
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Ribosome comp and func:
- Protein and RNA in two subunits
- Protein synthesis
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Endoplasmic reticulum comp and func:
- Membranous saccules and canals
- Synthesis and/or modification of proteins and other substances, and transport by vesicle formation
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Smooth ER comp and func:
- Having no ribosomes
- Various; lipid synthesis in some cells
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Golgi apparatus comp and func:
- Stack of membranous saccules
- Processing, packaging, and distribution of molecules
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Vacuole and vesicle comp and func:
- membranous sacs
- Storage and transport of substances
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Lysosome comp and func:
- Membranous vesicle containing digestive enzymes
- Intracellular digestion
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Mitochondrion comp and func:
- Inner membrane(with cristae) within outer membrane
- Cellular respiration
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Cytoskeleton comp and func:
- Microtubules, actin filaments, and intermediate filaments
- Shape of cell and movement of its parts
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Cilia and flagella comp and func:
- pattern of microtubules
- Movement of cell
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Centriole comp and func:
- pattern of microtubules
- Formation of basal bodies
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Magnification
the ratio of an object's image size to its real size
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Resolution
The measure of the clarity of the image or the minimum distance of two distinguishable points
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Contrast
Visible differences in parts of the sample
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Total surface area equation:
(height x width) x sides x number of boxes
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Total volume equation:
Height x width x length x number of boxes
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Surface to volume ratio equation
surface area / volume
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Differential Interference Contrast
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Who came up with the term cells and when?
Robert Hook 1665
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First person to see "animalcules" under the microscope and when?
Van Leeuwennhoek, 1674
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Acid
A molecule that releases a proton when dissolved in water; this dissociation generates hydronium(H30+) ions, thereby lowering the pH.
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Amino Acid
- Functional group (-NH2)
- Can accept a proton and carry a positive charge in aqueous solution.
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Atom
The smallest particle of an element that still retains its distinctive chemical properties; consists of a positively charged nucleus surrounded by a cloud of negatively charged electrons
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ATP
- Adenosine 5-triphosphate
- Molecule that serves as the principal carrier of energy in cells; this nucleoside triphosphate is composed of adenine, ribose, and three phosphate groups
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Avogadro's number
The number of molecules in a mole, the quantity of a substance equal to its molecular weight in grams; approximately 6x10^23
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base
Molecule that accepts a proton when dissolved in water; also used to refer to the nitrogen-containing purines or pyrimidine's in DNA and RNA
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buffer
Mixture of weak acids and bases that maintains the pH of a solution by releasing and taking up protons
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chemical bond
An exchange of electrons that holds two atoms together. Types found in living cells include ionic bonds, covalent bonds, and hydrogen bonds.
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Chemical group
Combination of atoms, such as a hydroxyl group (-OH) or an amino group (-NH2), with distinct chemical and physical properties that influences the behavior of the molecule in which it resides
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Condensation reaction
Chemical reaction in which a covalent bond is formed between two molecules as water is expelled; used to build polymers, such as proteins, polysaccharides, and nucleic acids.
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Conformation
Precise, three-dimensional shape of a protein or other macromoluecule, based on the spatial location of its atoms in relation to one another
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Covalent bond
Stable chemical link between two atoms produced by sharing one or more pairs of electrons
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DNA
- Deoxyribonucleic Acid
- Double-stranded polynucleotide formed from two separate chains of covalently linked deoxyribonucleotide units. It serves as the cell's store of genetic information that is transmitted from generation to generation.
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Electron
Negatively charged subatomic particle that occupies space around an atomic nucleus
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Electrostatic attraction
Force that draws together oppositely charged atoms. Examples include ionic bonds and the attractions between molecules containing polar covalent bonds
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fatty acid
Molecule that consists of a carboxylic acid attached to a long hydrocarbon chain. Used as a major source of energy during metabolism and as a starting point for the synthesis of phospholipids.
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hydrogen bond
A weak noncovalent interaction between a positively charged hydrogen atom in one molecule and a negatively charged atom, such as nitrogen or oxygen, in another; these interactions are key to the structure and properties of water
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hydrolysis
Chemical rxn that involves cleavage of a covalent bond with the accompanying consumption of water
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Hydronium IOn
The form taken by a proton (H+) in aqueous solution
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Hydrophilic
Molecule or part of a molecule that readily forms hydrogen bonds with water, allowing it to dissolve; literally, "water loving"
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Hydrophobic
Nonpolar, uncharged molecule or part of a molecule that forms few or no hydrogen bonds with water molecules and therefore does not dissolve; "water fearing"
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Hydrophobic interactions
Type of noncovalent bond that forces together the hydrophobic portions of dissolved molecules to minimize their disruption of the hydrogen-bonded network of water; helps push together membrane phospholipids and fold proteins into a compact, globular shape
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Inorganic molecule
Not composed of carbon and hydrogen
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Ion
An atom carrying an electrical charge, either positive or negative
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Ionic bond
Interaction formed when one atom donates electrons to another; this transfer of electrons causes both atoms to become electrically charged
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Lipid
Organic molecule that is insoluble in water but dissolves readily in nonpolar organic solvents; typically contains long hydrocarbon chains or multiple rings.
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Lipid bilayer
Thin pair of closely juxtaposed sheets, composed mainly of phospholipid molecules, that forms the structural basis for all cell membranes
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Macromolecule
Polymer built from covalently linked subunits; includes proteins, nucleic acids, and polysaccharides with a molecular mass greater than a few thousand daltons
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Molecule
Group of atoms joined together by covalent bonds
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Molecular weight
Sum of the atomic weights of the atoms in a molecule; as a ratio of molecular masses, it is a number without units.
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Monomer
Small molecule that can be linked to others of a similar type to form a larger molecule (polymer)
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Noncovalent bond
Chemical association that does not involve th sharing of electrons; singly are relatively weak, but can sum together to produce strong, highly specific interactions between molecules. Examples are hydrogen bonds and van der Waals attractions
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Nucleotide
Basic building block of the nucleic acids, DNA and RNA; includes a nucleoside with a series of one or more phosphate groups linked to its sugar
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Organic molecule
Chemical compound that contains carbon and hydrogen
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pH scale
Concentration of hydrogen ions in a solution, expressed as a logarithm. Thus, an acidic solution with pH3 will contain 10^-3 M hydrogen ions
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polar
In chemistry, describes a molecule or bond in which electrons are distributed unevenly
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Polymer
Long molecule made by covalently linking multiple identical or similar subunits (monomers).
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Protein
Polymer built from amino acids that provides cells with their shape and structure and performs most of their activities
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Proton
Positively charged particle found in the nucleus of every atom; also, another name for a hydrogen ion (H+)
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RNA
- Ribonucleic Acid
- Molecule produced by the transcription of DNA
- usually single-stranded, it is a poluculeotide composed of covalently linked ribonucleotide subunits.
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Sequence
The linear order of monomers in a large molecule, for example amino acids in a protein or nucleotides in DNA; encodes info that specifies a macromolecules's precise biological func.
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Subunit
A monomer that forms par of a larger molecule, such as an amino acid residue in a protein or a nucleotide residue in a nucleic acid.
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Sugar
A substance made of carbon, hydrogen, and oxygen with a general formula(CH20)n.
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van der Waals attractions
Weak noncovalent interaction, due to fluctuating electrical charges, that comes into play between two atoms within a short distance of each other
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Acetyl CoA
Activated carrier that donates the carbon atoms in its readily transferable acetyl group to many metabolic rxns, including the citric acid cycle and fatty acid biosynthesis; the acetyl group is linked to coenzyme A by a thioester bond that releases a large amount of energy when hydrolyzed
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Activated carrier
A small molecule that stores energy or chemical groups in a form that can be donated to many different metabolic rxns.
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Activation Energy
The energy that must be acquired by a molecule to undergo a chemical rxn
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ADP, ATP
- Adenosine diphosphate
- Adenosine triphosphate
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anabolism
Set of metabolic pathways by which large molecules are made from smaller ones
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Biosynthesis
An enzyme-catalyzed process by which complex molecules are formed from simple substances by living cells; also called anabolism
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Catabolism
Set of enzyme-catalyzed reactions by which complex molecules are degraded to simpler ones with release of energy.
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Catalysis
Substance that accelerates a chemical rxn brought about by the action of a catalyst; virtually all rxns in a cell require such assistance to occur under conditions present in living organisms
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Catalyst
Substance that accelerates a chemical rxn by lowering its activation energy; enzymes perform this role in cells
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Condensation Rxn
Chemical reaction in which a covalent bond is formed between two molecules as water is expelled; used to build polymers, such as proteins, polysaccharides, and nucleic acids
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Coupled reaction
Linked pair of chemical rxns in which free energy released by one rxn serves to drive the other rxn
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diffusion
Process by which molecules and small particles move from one location to another by random, thermally driven motion
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Entropy
- Thermodynamic quantity that measures the degree of disorder in a system
- All transfers increase disorder to the universe
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Enzyme
A protein that catalyzes a specific chemical rxn
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Equilibrium
State in which the forward and reverse rates of a chemical rxn are equal so that no net chemical change occurs
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Equilibrium constant, K
For a reversible chemical rxn, the ratio of substrate to product when the rates of the forward and reverse rxns are equal
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Free energy, G
Energy that can be harnessed to do work, such as driving a chemical rxn
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free-energy change, changeG
- in a chemical rxn, the difference in free energy between reactant and product molecules.
- Large neg vaule of G = strong tendency to occur
- Measurement of concentration, temperature and pressure
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Hydrolysis
Chemical rxn that involves cleavage of a covalent bond with the accompanying consumption of water
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Metabolism
The sum total of the chemical rxns that take place in the cells of a living organism
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Michaelis constant
Concentration of substrate at which an enzyme works at half its maximum velocity; serves as a measure of how tightly the substrate is bound
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Oxidation
Removal of electrons from an atom, as occurs during the addition of oxygen to a carbon atom or when a hydrogen is removed from a carbon atom
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Photosynthesis
The process by which plants, algae, and some bacteria use the energy of sunlight to drive the synthesis of organic molecules from carbon dioxide and water
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Reduction
Addition of electrons to an atom, as occurs during the addition of hydrogen to a carbon atom or the removal of oxygen from it
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Respiration
General term for any process in a cell in which the uptake of molecular oxygen is coupled to the production of CO2
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Standard free-energy change
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substrate
A molecule on which an enzyme acts
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turnover number
The number of substrate molecules an enzyme can convert into product per second
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The process of making polymers
polymerication
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what creates order to the universe?
Thermal Dynamic
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What do you call a polysaccharide linkage?
Glycosidic Linkage
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Amino Acids make?
Proteins
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Fatty acids make:
- Lipids
- glycerol
- steroids
- cholesterol
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What is a lipid linkage called?
Ester Linkage
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What is the special bond in phospholipids?
Phosphate bond
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What are the two ways a phospholipid form?
-
Name for when something is both hydrophobic and hydrophilic
Ampaphatic
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What prevents our cells from freezing in the winter?
- monosaturated fatty acid
- Cholesterol signalers
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Special structure of steriods
4 fused rings
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Nucleotide linkage:
Phosphodiester Linkage
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Why is ATP such a great energy source?
Because it has 3 negative energies, readily wants to repel them
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Nonpolar Amino acids
- Alanine
- Leucine
- Isoleucine
- Proline
- Cysteine
- Methionine
- Phenylalanine
- Tryptophan
- Glycine
- Valine
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Uncharged polar amino acids
- Asparagine
- Serine
- Threonine
- Tyrosine
- Glutamine
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Positively charged amino acids
-
Negatively charged amino acids
- Aspartic Acid
- Glutamic Acid
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Amino acids form what type of bond?
Peptide bond
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Amino acid functions
- * proteins
- * Peptide bonds
- * Bacterial cell walls
- * Antibiotics
- * Signal molecule in brain
-
Amino Acids Bond Types:
- Peptide Bond
- Polar Covalent
- Condensation
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Amino Acid structure
N-C-COOH
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Amino Acids Polymer
Proteins
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Nucleotides Bond Types
- Phosphodiester Linkage
- Covalent
- Hydrogen bonding
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Monosaccharides bonding type
- Glycosidic Linkage
- Covalent
- Hydrogen Bonding
-
Saccharides structure
- (CH(2)O)n
- N=3,4,5,6
- Isomers
- Ring formations
-
Monosaccharides polymers
- Carbohydrates
- Disaccharides
- Oligosaccharides
- POlysaccharides
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Carbohydrates Functions
- Production & storage of energy
- Plant cell walls
- insect exoskeletons
- slime & mucus
- Plasma Membrane
-
Fatty Acids polymers, but not a polymer
- Fats
- membrane lipids
- phospholipids
- triacylglycerols
- Steroids
- Cholesterol
-
Fatty Acids function
- primary building block of all membranes
- energy source
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Cell Wall
Composed of Carbohydrates: cellulose or chitin
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Peroxisome
Involved in hydrogen peroxide synthesis and degradation
-
Chloroplast
site of photosynthesis
-
Schromoplast
non-green pigments
-
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Metabolism
Series of chemical rxns involved in storing (anabolism) or releasing (catabolism) energy
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Glycolysis
Anaerobic process in cytoplasm in which glucose, a 6 carbon compound, is oxidized to two pyruvates, which are both three carbon chains
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Krebs cycle
Aerobic process that oxidizes pyruvates to CO2
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Gene functions
- 1. to be preserved and transmitted
- 2. to control various biological functions through the production of proteins and RNA
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Nucleotides
- the components of nucleic acids, three subunits
- 1. Sugar
- 2. Phosphate
- 3. Nitrogenous base
-
How many different proteins are there?
over 30,000
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Endogonic
- Anabolic
- creates order
- requires energy
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dehydrogenase
an enzyme that oxidizes a substrate by a reduction rxn that transfers one or more hydrides (H-) to an electron acceptor
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Closed system
a physical system which doesn't exchange any matter with its surroundings, and isn't subject to any force whose source is external to the system
-
Open system
a system which continuously interacts with its environment or surroundings
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Bioenergetics
the study of how organisms manage their energy resources
-
The Chemistry of Lie is organized into Metabolic Pathways
Metabolism: totality of an organisms chem rxns
Metabolic Pathway: begins w/a specific molecule and ends w/a product
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3 kinds of kinetic energy
- -movement
- -thermal energy
- -light energy
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Energy is:
the capacity to cause change
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Potential energy is:
energy that matter possesses because of its location or structure
-
Types of potential energy:
- -Chemical energy
- -Positional energy
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The 5 Laws of Energy Transformation
- 1. Thermodynamics
- 2. Isolated system
- 3. Open system
- 4. Organisms are open systems
- 5. These laws apply to the universe as a whole
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2 Laws of Thermodynamics
1. Law of Conservation of Energy
-
Law of Conservation of Energy
- 1. The energy of the universe is constant
- -energy can be transferred and transformed from one form to another, cannot be created or destroyed
2. Implication-must account for source and fate of all energy in biological systems
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Law of Entropy
- During every energy transfer or transformation, some energy becomes unusable, often lost as heat.
- -Every transfer or transformation increases disorder(entropy)
- -Entropy tends to increase in closed systems
- -for a process to occur spontaneously, it must increase the entropy of the universe
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Energy flows into an ___________ in the form of _________ and exits in the form of _________
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Cells create ordered __________ from less ordered ______
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Organisms replace ordered forms of ________ and _______ with less ordered forms
-
The evolution of more complex organisms does not violate the ____ ___ __ ___________
second law of thermodynamics
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Oxidation/Reduction Rxn Definition:
The transfer of partial transfer of an electron from one atom to another
-
Photosynthesis energy input and output
- Sunlight->Heat
- H20->O2
- CO2->glucose
-
Cellular Respirations energy inputs and outputs
- Glucose->CO2 & heat
- O2->H2O
- ADP->ATP
-
What does ATP do after created from cellular respiration?
Cellular work and heat
-
What products become oxidized and reduced in this equation:
CH4 + 2O2 = CO2 + energy + 2H2O
- Oxidized: CH4 -> CO2
- Reduced: 2O2 ->2 H2O
-
2 of the most stable molecules(as in oxidization/reduction)
-
How does a exergonic rxn proceed?
with a net release of free energy and is spontaneous
-
How does an endergonic rxn proceed?
absorbs free energy from its surroundings and is nonspontaneous
-
Free energy chemical rxns proceed.....
in direction that causes a loss in free energy which increases in net disorder
-
Gibbs Free energy is
a measure of a system's total energy available to do work, w/o reference to the surroundings
-
Endergonic=positive G=is the rxn spontaneous or not
no
-
Exergonic=negative G=is the rxn spontaneous or not
yes
-
Coupled rxns
When the net change of G is negative, the rxns are spontaneous
-
In a Na Cl rxn what gets oxidized and what gets reduced. Also which is negative ion and which is the positive ion?
- Na+ is the positive ion that gets oxidized
- Cl- is the negative ion that gets reduced
-
Rxns in a ______ system eventually reach _______ and then do _ _____
- closed system
- equilibrium
- no work
-
Cells are ___ in ________; they are ____ systems experiencing a constant flow of materials
-
A defining feature of life is that ________ is never at __________
-
A ________ pathway in a cell releases ______ _______ in a series of rxns
-
ATP powers cellular work by coupling __________ rxns to __________ rxns
-
3 main kinds of work a cell does
- -chemical
- -transport
- -mechanical
-
To do work, cells manage energy resources by ________ _________
energy coupling
-
Most energy coupling in cells is mediated by ___
ATP
-
Why is there so much energy in ATP?
the negative charges don't like being so close
-
What can break the phosphate bonds in ATP?
Hydrolysis
-
WHen is energy released from ATP?
when the terminal phosphate bond is broken
-
Where does the energy come from when the phosphate bond in ATP is broken?
chemical change to a state of lower free energy
-
What happens when change in G=0?
no energy
-
3 high energy electron carriers:
- 1. NAD+ -> NADH
- 2. NADP+ -> NADPH
- 3. FAD -> FADH2
-
________ speed up metabolic rxns by __________ energy barriers
-
A chemical agent that speeds up a reaction without being consumed by the reaction
Catalyst
-
A catalytic protein
Enzyme
-
The initial energy needed to start a chemical rxn is called:
activation energy
-
__________ ___________ is often supplied in the form of thermal energy that the reactant molecules absorb from their surroundings
Activation Energy
-
Nonprotein enzyme helpers
cofactors
-
An organic cofactor is called a:
coenzyme
-
What randomness does coenzymes include?
vitamins
-
What binds to the active site of an enzyme, competing with the substrate?
Competitive inhibitors
-
What binds to ANOTHER part of an enzyme to change shape and make the active site less effective?
Noncompetitive inhibitors
-
What are some examples of inhibitors?
toxin, poisons, pesticides and antibiotics
-
________ _____ store, transmit, and help express hereditary information
Nucleic acids
-
The amino acid sequence of a polypeptide is programmed by a unit of inheritance called a:
gene
-
______ are made of DNA
Genes
-
Nucleic acid made of monomers called:
nucleotides
-
_____ provides directions for its own replication
DNA
-
DNA directs synthesis of ______ and through _____ controls protein synthesis
mRNA
-
What do nucleic acids do?
- store & transmit hereditary information
- regulate gene expression
-
What are the two super charged molecules in DNA & RNA that repel each other?
Phosphate group & Nitrogenous base
-
Enzymatic Protein func and ex
- Selective acceleration of chem rxns
- EX: digestive enzymes catalyze the hydrolysis of bonds in food molecules
-
Defensive proteins func & ex
- Protection against disease
- ex: antibodies inactivate and help destroy viruses and bacteria
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Storage proteins func & ex
- Storage of amino acids
- ex: Plants of storage proteins in their seeds
-
Transport proteins func & ex:
- Transport of substances
- ex: hemoglobin, iron protein->oxygen from lungs to body
-
Hormonal Protein func & ex
- Coordination of an organism's activities
- ex: insulin, causes other tissues to up take glucose which regulates blood sugar concentration
-
Receptor Proteins func & ex
- Response of cell to chemical stimuli
- Ex: built into membrane of nerve cell detect signaling molecules released by other nerve cells
-
Contractile and motor proteins func & ex
- Movement
- ex: actin and myosin proteins are responsible for the contraction of muscles
-
Structural proteins func & ex:
- Support
- Keratin, collagen, elastin and silk fibers
-
What do you call a polysaccharide(carbohydrates) linkage?
Glycosidic LInkage
-
What do you call a lipid linkage?
Ester LInkage
-
What do call a nucleic acid linkage?
phosphodiester
-
What do you call a amino acid linkage?
Peptide Linkage
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4 basic monomers
- amino acid
- fatty acid
- nucleic acid
- monosaccharides
-
How do you form a peptide bond?
OH and H of two amino acids and connect the C and N together
-
The four bonds involved in the folding and maintence of proteins:
- Hydrogen bonds
- Electrostatic attractions
- Van der Waals
- Hydrophobic interaction
-
The final folded structure of a protein is called:
conformation
-
When a protein refolds spontaneously to its original conformation after its been denatured
renaturation
-
Molecule that steers proteins along productive folding pathways, helping them to fold correctly and preventing them from forming aggregates inside the cell
chaperone protein
-
The primary structure of a protein:
Amino acid sequence
-
Secondary Structure of a protein:
Folds that form in certain segments of the polypeptide chain
-
Tertiary Structure of the protein:
full, three-dimensional conformation of the entire polypeptide chain
-
Quarternary Structure of a protein:
More than one polypeptide chain
-
regions of polypeptide chain lacking any definite structure
intrinsically disordered sequences
-
Shape name in which the polypeptide chain folds up into a compact shape like a ball with an irregular surface
Globular Proteins
-
Shape name for protein that have a relatively simple, elongated three-dimensional structure
fibrous proteins
-
Most abundant fibrous protein
collagen
-
A substance that is bound by a protein
ligand
-
Region of a protein that associates with a ligand
binding site
-
Enzymes that catalyze a hydrolytic cleavage rxn
hydrolase
-
Enzyme class that breaks down nucleic acids by hydrolyzing bonds btwn nucleotides
nuclease
-
Enzyme class that breaks down proteins by hydrolyzing peptide bonds btwn amino acids
protease
-
Enzyme class that joins two molecules together
Ligase
-
Enzyme class that catalyzes the rearrangement of bonds within a single molecule
Isomerase
-
Enzyme class that catalyzes polymerization reactions such as the synthesis of DNA and RNA
Polymerase
-
Enzyme class that catalyzes the addition of phosphate groups to molecules
Kinase
-
Enzyme class that catalyzes the hydrolytic removal of a phosphate group from a molecule
Phosphatase
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Enzyme class tha catalyze rxns in which one molecule is oxidized white the other is reduced
oxido-reductase
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Enzyme class that hydrolyzes ATP
ATPase
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