Exam 1: Chapter 2 Molecules and Cells
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| Proximate causation is the building block of cells. How does venom affect the the building blocks of cells? | Venom affect molecules and cells by reacting with certain functions of the system to immortalize it's functions.
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| Phospholipid | a polar molecule that acts as a membrane (bi-layer) in different structures of the body (ex. cell membranes, nuclear envelope, organs, etc.)
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| Phospholipid Bi-layer | composes cell membrane; a layer of the phospholipids that are embedded with different structures to help the body function
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| Why do membranes exhibit a fluid motion? | this membrane has a fluid mobility due to its fatty acids tails
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| What are the differences between the head and the tails of the phopholipid? | The head of the phosopholipd is hydrophilic and polar in charge.
The tail of the phospholipd is hydrophobic and nonpolar in charge.
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| What makes the phosphlipid amphipathic? | The phosphlipid is amphipathic because it has a both hydrophilic and hydrophobic parts.
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| Saturated Fats | Single bonded carbon chain loaded with H bonds (ex. lard, butter)
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| Unsaturated Fats | *Has at least one double bond in its carbon chain (ex. oil)
*Works similarly to membrane fluidity
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| Poly-saturated Fats | Has multiple double carbon bonds in its carbon chain
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| What is the correlation to natural selection and fluidity of the tails in fish? | As some fish are found in higher temperature the percentage of unsaturated fats in their tail are seen less.
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| Fluid Mosaic Model | consists of a mosaic of proteins and lipid molecules; exemplifies the structure and and function of a cell membrane
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| Proteins | amino acids in a polypeptide chain are linked by peptide bonds
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| Amino Acids | organic compounds that combine to form proteins; composed of amino group, carboxylic group and a side chain.
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| Protein Structure: Primary | specific sequence or colvalent bonds of an amino acid chain
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| Protein Structure: Secondary | due to charges and different amino acids
*alpha helices
* beta pleated sheets
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| Protein Structure: Tertiary | folding on itself; gives the structure function; only one subunit
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| Protein Structure: Quartiary | multiple subunits (ex. hemoglobin)
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| Epithelia | Membranous tissue composed of one or more layers of cells separated by very little intercellular substance and forming the covering of most internal and external surfaces of the body, its organs, and lines cavities
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| Simple Epithelia | single layer of cells that cover body; used to exchange material through the membrane; found in intestines, kidney tubles, blood vessels and sweat glands
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| Simple Squamous | flat, simple epithelia (ex. blood vessels)
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| Cell Membrane | encloses animal cells
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| Intracellular Membrane | encloses cell organelles
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| Phospholipid Head | polar: -P group and + Chlorine group; hydrophylic; associates with water
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| Phospholipid Tail | nonpolar: chain of CH, derived from fatty acids; hydrophobic
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| Leaflets | two phospholipid layers
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| What does fluidity depend on? | Fluidity depends on chemical saturation. The more saturated a molecule is, the more fluid it will become.
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| Integral Membrane Protein (Transmembrane Protein) | part of the membrane; cannot be removes without disassembling the membrane; amphipathic
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| Peripheral Membrane Protein | within a membrane; cannot be removed without destroying the membrane; noncovalently (weak) bonded to membrane; on one side or the other of membrane
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| Channels | permits diffusion of sloutes in an aqueous solution
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| Transporter (Carrier) | binds noncovalently and reversibly with specific molecules or ions to move across the membrane
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| Enzyme | catyllizes a chemical reaction
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| Receptor | binds with molecules and initiates change in membrane permeability or cell metabolism; mediates responses of cell messages
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| Structural Protein | attaches to molecules; creates junctions; establishes structural relations
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| Domain | repeating structure patterns of proteins
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| Carbohydrates | covalently bonded; part of intracellular membrane; hydrophilic-resides on membrane surface; attachment points for extracellular proteins and as cell recognition sites
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| Apical Surface | facing into a cavity or open space
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| Basal Surface | facing underlying tissue
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| Basement Membrane | thin, permeable, noncellular, nonliving material; point of attachment composed of glycoproteins
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| Columnar | tall, wide; line mid-gut; apical surface faces lumen
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| Microvilli | finger-like projections used for absorbtion and secretion
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| Brush Boarder | Microvilli collection
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| REVIEW PROTEIN MODEL |
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| Ampipathic | has polar and non-polar components
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| Ligand | general term for a molecule that binds to a protein
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| Enzyme Ligand | Substrates and other molecules that bind to other enzymes
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| Positive Cooperativity | allows binding of ligands (or molecules) in a substrate
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| Negative Cooperativity | inhibits binding of ligands (or molecules) in a substrate
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| Non-Cooperativity | Has no effect on ligands (or molecules)
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