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Life
Characterized by:
-the ability to grow
-reproduce
-respond to stimuli
-adapt to the environment
-carry out metabolic processes.
Science
A systematic enterprise that builds and organizes knowledge in the form of testable explanations and predictions about the universe.
What is science useful for?
-understanding natural phenomena
-solving problems
-making informed decisions
-advancing technology and medicine.
How is science different from other ways of knowing?
Science relies on empirical evidence, experimentation, and reproducibility, while other ways of knowing may include intuition, tradition, or personal experience, which are not always verifiable.
Archaea
Unicellular prokaryotes that lack a nucleus and membrane-bound organelles
Biological Evolution
the change over time in populations of related organisms (not only individuals)
Misconceptions about Biology
-Humans evolved from monkeys
-Survival of the Fittest = Strongest
-Evolution is a theory
-Individuals Evolve
-Evolution has a Goal
Overarching themes of Biology
1. law is subject to chemical and physical laws
2. structure determines funcitons
3. living systems transform energy and matter
4. living systems depend on information transactions
5. evolutions explains the unity and diversity of life
How can Isotopes be used in:
Biological Research/Medicine
Radioactive isotopes are a way to label/ "tag" a specific molecule and then it's progress, either in a chemical reaction or in living cells. This can be applied to cancer technology and research.However, it can damage living cells produce genetic mutation, and cell death.
Why do electrons occupy discrete, different energy levels?
To change energy levels
Relate position in the periodic table to atomic structure and the formation of ions.
A chemical element's position in the periodic table directly corresponds to its fundamental atomic structure
Metallic Bonds
a bond formed by the attraction between positively charged metal ions and the electrons around them
Polar Bonds
a covalent bond in which electrons are shared unequally
Nonpolar Bonds
a covalent bond in which electrons are shared equally
Predict how atoms such as C, H, O, and N share electrons in a covalent bond, the role of electronegativity, and the potential for hydrogen bonding between molecules
The nature of this sharing is determined by electronegativity, and the resulting polarity facilitates hydrogen bonding between molecules containing O-H and N-H bonds
Chemical Reaction
reactants contact each other, bonds between atoms in the reactants are broken, and atoms rearrange and form new bonds to make the products
Water Molecule
The bent shape and high electronegativity of the oxygen atom are what cause water to be a polar molecule
Cohesion
Attraction between (water) molecules of the same substance
Adhesion
An attraction between (water) molecules of different substances
High Specific Heat
The ability of water to absorb/release heat and resist changes in temperature.
High Heat of Vaporization
Amount of heat necessary to turn water into a gas
How can you tell if a molecule will dissolve easily in water?
Polar - Easily Dissolves
Ionic - Dissolves Well
Nonpolar - Insoluble
Carbohydrates
Broken down to glucose to provide energy.
Lipids
Energy-rich organic compounds, such as fats, oils, and waxes, that are made of carbon, hydrogen, and oxygen.
Nucleic Acids
DNA and RNA
Proteins
Nutrients the body uses to build and maintain its cells and tissues
Hydroxyl
(-OH) commonly found in alcohols and sugars.
Carboxyl
(-COOH), found in amino acids and fatty acids.
Amino
(-NH2), commonly found in amino acids and proteins.
Phosphate
(-PO4), found in nucleotides and nucleic acids.
Methyl
(-CH3), found in lipids and various organic compounds.
Types of Macromolecules
Proteins
Nucleic Acids
Carbohydrates
Lipids
Addition Polymerization
a type of polymerization in which the monomers simply add together to form the polymer, with no other products
Condensation Polymerization
a type of polymerization in which the formation of a small molecule, such as water, accompanies the extension of the polymer chain
Depolymerization Reactions
Reactions that break polymers into smaller monomers.
Hydrolysis
A chemical reaction where water is used to break down polymers into monomers by cleaving the bonds between the monomer units.
Glucose
A simple sugar with the molecular formula C6H12O6, commonly found in fruits and is a primary energy source for cells.
Fructose
A simple sugar with the molecular formula C6H12O6, found in many plants and is the sweetest natural sugar.
Galactose
A simple sugar with the molecular formula C6H12O6, primarily found in milk and dairy products.
Ribose
A simple sugar with the molecular formula C5H10O5, an essential component of RNA and important in cellular metabolism.
Deoxyribose
A simple sugar with the molecular formula C5H10O4, a component of DNA, differing from ribose by the absence of one oxygen atom.
Sucrose
A disaccharide composed of glucose and fructose, commonly known as table sugar, found in many plants.
Lactose
A disaccharide made up of glucose and galactose, primarily found in milk and dairy products.
Maltose
A disaccharide formed from two glucose units, produced during the digestion of starch.
Starch
A polysaccharide that serves as a storage form of energy in plants, composed of long chains of glucose units.
Glycogen
A polysaccharide that functions as a storage form of energy in animals, consisting of branched chains of glucose.
Cellulose
A polysaccharide that provides structural support in plant cell walls, made of long chains of glucose linked by beta-1,4-glycosidic bonds.
Chitin
A polysaccharide that forms the exoskeleton of arthropods and the cell walls of fungi, composed of N-acetylglucosamine units.
Primary functions of DSC (Deoxyribonucleic Acid)?
-to store genetic information
-provide instructions for protein synthesis (translation)
-ensure the transmission of hereditary traits.
Monomers that make up DSC
Nucleotides.
Bonds join the monomers in DNA
Phosphodiester Bonds.
Primary Functions of PSC (Proteins)
-Catalyze biochemical reactions (enzymes)
-Provide structural support
-Transport molecules
-Regulate biological processes.
Monomers that make up Proteins
Amino Acids
Bonds join the monomers in Proteins
Peptide Bonds
Triglycerides
A type of lipid formed from one glycerol molecule and three fatty acids, typically used for energy storage in the body.
Steroids
A class of lipids characterized by a carbon skeleton with four fused rings, playing roles in cell membrane structure and signaling.
Fatty Acids
Long hydrocarbon chains with a carboxylic acid group at one end, which can be saturated or unsaturated.
Saturated Fatty Acids
Contain no double bonds between carbon atoms, meaning they are fully 'saturated' with hydrogen atoms.
Unsaturated Fatty Acids
Contain one or more double bonds in their hydrocarbon chain, which can be classified as monounsaturated or polyunsaturated.
How do fatty acid variations affect triglycerides?
Variations in fatty acids affect the physical properties of triglycerides, such as melting point and fluidity, influencing their biological functions and roles in health.
Trans Fatty Acids
Trans fatty acids are a type of unsaturated fat that can increase the risk of heart disease by raising LDL cholesterol levels and lowering HDL cholesterol levels.
Nucleotides
Monomers that make up nucleic acids
Three components of Nucleotides
-A phosphate group
-A five-carbon sugar (ribose or deoxyribose)
-A nitrogenous base.
What are the two groups of nitrogenous bases in nucleotides?
Purines (Adenine and Guanine)
Pyrimidine (Thymine, Cytosine, Uracil in RNA)
Purines
Double-Ring Structure
Pyrimidines
Single-Ring Structure
Phosphodiester Bonds in DNA/RNA
Connect the monomers within a single strand
Hydrogen Bonds in DNA
Connect the nitrogenous bases between different strands of DNA.
Transcription
The process by which the information in a DNA sequence is copied into a complementary RNA sequence.
Translation
The process by which ribosomes synthesize proteins using the information carried by messenger RNA.
Codon
A sequence of three nucleotides in mRNA that corresponds to a specific amino acid or stop signal during protein synthesis.
Gene
A segment of DNA that contains the instructions for building a specific protein or set of proteins.
Chromosome
A structure composed of DNA and proteins that organizes and condenses genetic material within the cell nucleus.
RNA Polymerase
An enzyme that synthesizes RNA from a DNA template during the process of transcription.
Chromatin
A complex of DNA and proteins (histones) that forms chromosomes within the nucleus of eukaryotic cells.
Chromatin Organization
-A structure that includes nucleosomes
-DNA wraps around histone proteins, forming a bead-like structure.
-The nucleosomes further coil and fold to form higher-order structures, ultimately leading to the formation of chromosomes.
Eukaryotic Chromosomes
multiple and linear
Histones
Globular protein that assist in DNA packaging in eukaryotes. Form octamers around which DNA is wound to form a nucleosome.
What is the significance of chromatin structure?
The structure of chromatin is crucial for regulating gene expression, DNA replication, and repair, as it determines the accessibility of DNA to various cellular machinery.
Amino Acid
Organic compounds that serve as the building blocks of proteins, characterized by a central carbon atom bonded to an amino group, a carboxyl group, a hydrogen atom, and a variable side chain.
Central Carbon
The carbon atom in an amino acid that is bonded to four different groups, making it a chiral center in most amino acids.
Amino Group
A functional group consisting of a nitrogen atom bonded to two hydrogen atoms, typically represented as -NH2, which is part of every amino acid.
Carboxyl Group
A functional group consisting of a carbon atom double-bonded to an oxygen atom and single-bonded to a hydroxyl group (-COOH), found in all amino acids.
Side Chain (R Group)
The variable group attached to the central carbon of an amino acid that determines its unique properties and classification.
Peptide Bond
The covalent bond formed between the carboxyl group of one amino acid and the amino group of another, resulting in a dipeptide and releasing a molecule of water.
Hydrophobic Amino Acids
A category of amino acids with nonpolar side chains that do not interact favorably with water, often found in the interior of proteins.
Hydrophilic Amino Acids
A category of amino acids with polar or charged side chains that interact favorably with water, often found on the surface of proteins.
Essential Amino Acids
A group of amino acids that cannot be synthesized by the body and must be obtained through diet.
Non-Essential Amino Acids
A group of amino acids that can be synthesized by the body and do not need to be obtained from dietary sources.
Basic structure of amino acids
-A central carbon atom (C) bonded to an amino group (NH2)
-A carboxyl group (COOH)
-A hydrogen atom (H)
-A variable R-group (side chain).
Groups of amino acids
Amino acids are categorized into nonpolar, polar, acidic, and basic groups based on the properties of their R-groups.
Protein construction diagram
Proteins are constructed from amino acid monomers linked by peptide bonds, which are formed through a dehydration reaction between the carboxyl group of one amino acid and the amino group of another.
Primary Sequence of Protein
Amino Acids
Secondary Sequence of Protein
alpha helix and beta pleated sheet
Tertiary Sequence of Protein
Polypeptide chain is bent and folded into 3D structure
Quaternary Sequence of Protein
2 or more polypeptide chains bound together
Protein Motifs
Specific arrangements of amino acids that have a particular function
Protein Domains
Distinct functional and structural units within a protein.
Denaturation of proteins
The process by which a protein loses its native structure due to factors such as:
-Heat
-pH changes
-Chemical Exposure
Chaperonins
protein molecules that assist the proper folding of other proteins