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Vocabulary flashcards covering key concepts from the notes on life properties, cell types, and scientific inquiry.
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Order
Living organisms are highly organized.
Sensitivity (Response to environment)
Organisms respond to various stimuli.
Reproduction
The ability of organisms to create new life.
Growth & Development
Organisms can grow and develop throughout their life cycle.
Regulation
Mechanisms that help cope with environmental stresses (e.g., cellular interdependence).
Homeostasis
Maintaining internal balance, e.g., sweating to cool off, shivering to heat up.
Energy Processing
Organisms use energy for metabolic activities, e.g., photosynthesis & cellular respiration.
Organization of matter in biology
Atoms → Molecules → Macromolecules → Organelles → Cells → Tissues → Organs & Organ Systems → Organisms/Populations & Communities → Ecosystems → Biosphere.
Features common to all cells
Plasma membrane, Cytoplasm/Cytosol, DNA, Ribosomes.
Prokaryotic cell characteristics
Nucleoid; no membrane-bound organelles; cell wall; some have flagella or pili.
Eukaryotic cell characteristics
Larger than prokaryotes; true nucleus with DNA surrounded by a membrane; membrane-bound organelles.
Hypothesis
A testable and falsifiable statement.
Experimental design
Includes sample size and methods to avoid bias.
Independent variable
Manipulated variable.
Dependent variable
Measured variable.
Results interpretation
Interpreting results by measuring dependent variables and checking for statistical significance.
HEER
Stands for Hypothesis, Experimental design, Experimental variables, Results (interpretation).
Matter
A substance that occupies space and has mass
Elements
Unique forms of matter with specific chemical/physical properties that cannot be broken down by ordinary chemical reactions.
Atom
The smallest unit of matter that retains chemical properties. Made up of protons (+, nucleus), neutrons (neutral, nucleus), and electrons (-, orbitals)
Atomic #
The number of protons in the nucleus.
Isotopes
Different forms of the same atom that vary only in the number of neutrons
Atomic mass
The calculated mean of the mass numbers for the naturally occurring isotopes of an element.
Periodic table organized in which way
By atomic number, into rows and columns based on shared chemical & physical properties.
Bohr model of the atom
A central nucleus (protons + neutrons) with electrons in circular orbitals at specific distances (energy levels).
Octet rule
Atoms are more stable when their outermost (valence) shell is filled with 8 electrons (except the innermost shell, which holds 2).
Electron orbitals
Regions where electrons are most likely to be found, with complex shapes due to wave-like behavior.
Why do atoms form chemical bonds?
Because not all elements have enough electrons to fill their outer shells, they bond to achieve stable electron configurations.
Molecule
Two or more atoms chemically bonded together.
Ions
Atoms that gain or lose electrons to become more stable. Cations = positive (lost electrons), Anions = negative (gained electrons).
# of electrons each electron shell can hold
1st shell (1s): 2, 2nd shell (2s, 2p): 8, 3rd shell (3s, 3p, 3d): 18
Electron transfer
Movement of electrons from one element to another
Ionic bonds
Bonds formed between oppositely charged ions (e.g., NaCl)
Covalent bonds
Bonds where atoms share electrons (single, double, triple bonds). Can be polar (unequal sharing) or non-polar (equal sharing).
Hydrogen bonds
Weak bonds where a hydrogen in a polar covalent bond is attracted to another electronegative atom (important in water & DNA).
What are functional groups?
a group of atoms responsible for the characteristic reactions of a particular compound
OR
Atoms that confer specific properties to hydrocarbons and define chemical behavior
Main functional groups
Hydroxyl: Polar, hydrophilic
Carboxyl: Acidic, releases H+
Amine: Basic, accepts H+
Phosphate: Acidic, releases H+
Methyl: Nonpolar
Carbonyl: Polar, increases polarity
Sulfhydryl: Polar, contains sulfur
Proteins
Abundant organic molecules with diverse functions. Polymers of amino acids in a linear sequence
Protein’s monomer
Amino Acids
Structure of an amino acid
Central carbon (α) bonded to an amino group (NH2), carboxyl group (COOH), hydrogen atom, and an R group.
Bond that links amino acids
Peptide bond formed during dehydration reaction.
What determines a protein’s shape and function?
Sequence and number of amino acids
Primary structure of proteins
Unique sequence of amino acids in a polypeptide chain.
Secondary structure of proteins
Folding of polypeptide in some regions (e.g., α-helices, β-sheets)
Tertiary structure of proteins
Overall 3D shape due to hydrophobic, ionic, hydrogen bonding, and disulfide linkages
Quaternary structure of proteins
Formed from interactions of multiple polypeptides (subunits).
Denaturation
Loss of protein’s function due to changes in temperature, pH, or chemicals, without changing primary sequence
Chaperones/Chaperonins
Proteins that assist in proper protein folding and prevent aggregation
Protein Aggregation
Misfolded/unfolded proteins clump into stable aggregates
Protein functions examples
Enzymes (amylase, lipase)
Transport (hemoglobin)
Structural (actin, keratin)
Hormones (insulin)
Defense (immunoglobulins)
Contractile (actin, myosin)
Storage (albumin).
Lipids
Nonpolar, hydrophobic macromolecules. Function in energy storage, insulation, protection, membranes, hormones.
Fats made of
Fatty acids + glycerol (or sphingosine); also called triglycerides or triacylglycerols
Saturated vs unsaturated fats
Saturated: no double bonds, solid at room temp.
Unsaturated: double bonds, bent structure, liquid at room temp.
Omega fatty acids
Essential fatty acids with cis double bonds, e.g., Omega-3.
Waxes
Lipids made of long fatty acid chains esterified to alcohols. Provide waterproofing in nature.
Phospholipids
Lipids with glycerol backbone, 2 fatty acids, and phosphate group. Form bilayers in cell membranes.
Steroids
Lipids with 4 fused carbon rings. Examples: cholesterol, testosterone
Carbohydrate
Energy source and structural macromolecules, made of C:H:O in 1:2:1 ratio.
Carbohydrate monomer
Monosaccharides (simple sugars like glucose, fructose, galactose).
Disaccharides
Two monosaccharides linked by glycosidic bonds (lactose, maltose, sucrose).
Polysaccharides
Long chains of monosaccharides (starch, glycogen, cellulose). Storage and structural roles.
Cellulose
Structural polysaccharide in plants (also used by herbivores like cows).
Nucleic acids
Macromolecules that carry genetic information (DNA, RNA).
Nucleic acid’s monomer
Nucleotides (nitrogenous base + pentose sugar + phosphate group).
DNA
Double-stranded molecule carrying genetic material. Bases pair A-T, G-C. Antiparallel strands.
RNA
Single-stranded molecule involved in protein synthesis. Bases are A, U, G, C
Types of RNA
mRNA (messenger), rRNA (ribosomal), tRNA (transfer), miRNA (micro)
Central dogma of life
DNA → RNA → Protein. DNA transcribed into RNA; RNA translated into protein
Dehydration synthesis
Reaction where monomers bond to form polymers, releasing water
Hydrolysis
Reaction where water breaks polymers into monomers
4 macromolecules & their monomers
Proteins → amino acids
Lipids → fatty acids + glycerol
Carbohydrates → monosaccharides
Nucleic acids → nucleotides