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A set of vocabulary flashcards derived from the Biology SNCB112 Quiz #1 Study Guide, covering core concepts from Weeks 1 to 3.
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Eight characteristics of life
Different levels of organization, sensitivity or response to the environment, reproduction, adaptation, growth and development, cellular composition, homeostasis, and energy processing.
Elements with highest percentage in living organisms
Carbon (C), Hydrogen (H), Oxygen (O), and Nitrogen (N).
Ionic bonding
A chemical bond characterized by the transfer of electrons between atoms.
Covalent bonding
A chemical bond characterized by the sharing of electrons between atoms.
Van der Waals interactions
Weak attractions or interactions between molecules.
Four key properties of water for sustaining life
Water is "sticky", an excellent solvent, moderates temperatures, and its solid form floats on liquid water.
Acidic aqueous solution
An aqueous solution that increases H3O+ concentration, resulting in a lower pH.
Basic aqueous solution
An aqueous solution that decreases H3O+ concentration, resulting in a higher pH.
Atomic structure of carbon
Contains 4 valence electrons and can form up to four covalent bonds with other atoms.
Lipids
Largely non-polar molecules that store energy for long-term use, provide insulation from the environment, serve as precursors of steroid hormones, and act as constituents of cellular membranes.
Nucleotide
The monomer of nucleic acids, consisting of three components: a pentose sugar, a nitrogenous base, and a phosphate group.
Purines
Nitrogenous bases containing two rings, which include adenine (A) and guanine (G).
Pyrimidines
Nitrogenous bases containing one ring, which include cytosine (C), thymine (T), and uracil (U).
Phosphodiester linkages
Linkages connecting sequential nucleotides in a nucleic acid strand.
Complementary DNA base pairing
Hydrogen bonding between nucleotides of different strands in a double helix, specifically adenine pairing with thymine (A–T) and cytosine pairing with guanine (C–G).
Amino acid structure
A monomer consisting of 1 central C, 1 H, 1 carboxyl group, 1 amino group, and 1 R-group.
Primary protein structure
The specific sequence of amino acids in a polypeptide chain.
Secondary protein structure
Protein folding patterns such as the α helix and β sheet formed due to hydrogen bonds between backbone groups.
Tertiary protein structure
The overall three-dimensional protein structure resulting from interactions between R-groups.
Quaternary protein structure
The structural level resulting from interactions between different polypeptide chains.
Denaturation
The loss of a protein's secondary, tertiary, or quaternary structure, which usually leaves the primary structure unaffected.
Four common functions of cells
Maintain internal homeostasis (plasma membrane), store and pass on information (DNA), build proteins (ribosomes), and conduct chemical processes of life (cytoplasm).
Prokaryotic cells
Smaller and simpler cells that lack a nucleus and membrane-bound organelles, but may possess a cell wall, plasmids, and extracellular structures like flagella.
Cytoskeleton composition
A cellular framework composed of microtubules, microfilaments, and intermediate filaments.
Integral membrane protein functions
Transporting substances, transducing extracellular signals, catalyzing chemical reactions, attaching the membrane to the cytoskeleton and ECM, and enabling cell-cell adhesion and recognition.
Passive transport
Membrane transport (including simple and facilitated diffusion) that moves molecules down a concentration or electrochemical gradient without cellular energy input.
Active transport
Membrane transport requiring energy input to move molecules against a concentration gradient to establish or maintain gradients.
Primary active transport
Active transport mechanisms that utilize energy directly to transport molecules.
Secondary active transport
Active transport mechanisms that utilize an existing ion gradient to move substances across a membrane.