BIS 2A SINGER

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98 Terms

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Design Challenge

A written plan that identifies a problem to be solved together with its requirements and constraints

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Hypothesis

A testable prediction, often implied by a theory

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Prokaryote

A unicellular organism that lacks a nucleus and membrane bound organelles

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Eukaryote

A cell that contains a nucleus and membrane bound organelles

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Organelle

specialized structure that performs important cellular functions within a eukaryotic cell

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Nucleoid

A dense region of DNA in a prokaryotic cell.

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Nucleolus

Found inside the nucleus and produces ribosomes

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Nucleus

Control center of the cell

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Cytoplasm

A jellylike fluid inside the cell in which the organelles are suspended

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Cytosol

Fluid portion of cytoplasm

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Plasma Membrane

A selectively-permeable phospholipid bilayer forming the boundary of the cells.

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Internal Membranes

membranes surrounding organelles

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Inner Membrane

Where is ATP synthase located in the mitochondrion?

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outer membrane

Outermost membrane in the mitochondria that protects and holds the form of the organelle.

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Cell Wall

A rigid layer of nonliving material that surrounds the cells of plants and some other organisms.

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Cytoskeleton

A network of fibers that holds the cell together, helps the cell to keep its shape, and aids in movement

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Flagella

whiplike tails found in one-celled organisms to aid in movement

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Pilli

Hollow tubes used to move cells or exchange DNA between bacteria by conjunction.

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Ribosomes

Makes proteins

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Endomembrane System

A network of membranes inside and around a eukaryotic cell, related either through direct physical contact or by the transfer of membranous vesicles.

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Rough ER

That portion of the endoplasmic reticulum studded with ribosomes.

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Smooth ER

That portion of the endoplasmic reticulum that is free of ribosomes.

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Golgi Apparatus

A system of membranes that modifies and packages proteins for export by the cell

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Primary Lysosomes

contain inactive enzymes

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Secondary Lysosomes

Membrane-enclosed organelle formed by the fusion of a primary lysosome with a phagosome, in which macromolecules taken up by phagocytosis are hydrolyzed into their monomers.

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Mitochondria

Powerhouse of the cell

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Matrix

Innermost compartment of the mitochondrion

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Cristae

Infoldings of the inner membrane of a mitochondrion that houses the electon transport chain and the enzyme catalyzing the synthesis of ATP.

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Chloroplast

An organelle found in plant and algae cells where photosynthesis occurs

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Thylakoid

A flattened membrane sac inside the chloroplast, used to convert light energy into chemical energy.

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Stroma

fluid portion of the chloroplast; outside of the thylakoids

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Granum

stack of thylakoids

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Peroxisomes

Contain oxidase enzymes that detoxify alcohol, hydrogen peroxide, and other harmful chemicals

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Glyoxysomes

found in fat tissue, converts fat into sugar

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Vacuole

Cell organelle that stores materials such as water, salts, proteins, and carbohydrates

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Atom

Smallest unit of matter that retains element properties

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The most common atoms in Biology

Carbon, Hydrogen, Nitrogen, Oxygen, Phosphorus, and Sulfur

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Electronegativity

the tendency of an atom to attract electrons

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Dipoles

positive and negative charged ends of a polar covalent molecule

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Ionic bonds

Metals interacting with a nonmetal, opposite charges. Takes electrons and aren't usually stable.

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Covalent bonds

Nonmetals interacting with nonmetals, shared electrons, and are usually stable.

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Non polar bonds

When the sharing of electrons is basically equal. Nonpolar covalent

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Polar bonds

When the sharing of electrons is not equal. Polar covalent

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Hydrogen bonds

Type of covalent bond, between a partial positive charge of H and partial negative of other atoms. Usually with O, N, or F.

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Van Der Walls bond

Interaction of electrons of nonpolar substances

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Water

H20 Polar Covalent

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Hydrophilic

Molecules are polar and will interact with water

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Hydrophobic

Molecules are nonpolar and won't interact with water

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Dissociation

Disrupting the bonds and breaking them apart.

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pH < 7

Acid (High H+ proton concentration)

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pH = 7

Neutral (water)

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pH > 7

Base (Soap)

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Are there more or less H+ ions at a higher pH?

less

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pH = pKa

[protonated] = [deprotonated]

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pH > pKa

Deprotonated predominates

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pH < pKA

Protonated predominates

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Methyl functional group

Unable to form hydrogen bonds(only one that never can) Nonpolar

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Hydroxyl functional group

Can form hydrogen bonds, Polar

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Carboxyl functional group

Can form hydrogen bonds, Polar

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Amino functional group

Can sometimes form hydrogen bonds

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Phosphate functional group

Can form hydrogen bonds

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Lipids

Energy-rich organic compounds such as fats and oils. Are Hydrophobic and nonpolar

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Steroids

Fats that have 4 carbon rings. Ex. Cholesterol

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Phospholipids

Make up the duel layer of cell membranes, fatty acid chains and polar head group

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Carbohydrates

The starches and sugars present in foods, have a CH2O forumula.

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Nucleotides

Made of pentose sugar. nitrogenous base, and phosphate group. Monomers of nucleic acids

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Purines

Adenine and Guanine

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Pyrimidines

Cytosine, Thymine, Uracil

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Amino acids

Building blocks(Monomers) of proteins. Structure consists of central carbon bounded to amino group, R group, and a carboxyl group.

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Primary structure of proteins

Linear sequence of amino acids in a peptide bond.

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Secondary structure of proteins

Local folding of the polypeptide chain, held together by hydrogen bonds, usually forms a-helix and b-pleated sheets.

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Tertiary structure of proteins

Unique 3D structure of a polypeptide, has to do with how the R groups interact, and forms disulfide linkages between areas in the chain.

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Quaternary structure of proteins

How multiple polypeptide subunits of a protein interact.

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Denaturation

Protein structure changes, but primary sequences don't. Can be reversed, but function of protein is lost.

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Catalyst

Helps increase the speed at which the reaction takes place by lowering the activation energy to start the reaction. Doesn't change the reaction or free energy.

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Enzymes

Protein catalysts

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Substrates

The reactants that bind to the enzyme

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Active sites

the site on an enzyme that attaches to a substrate

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Competitive inhibition

Competes with the substrate for the active site

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Noncompetitive inhibition (Allosteric inhibition)

Alters enzyme elsewhere.

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Allosteric activation

Changes the binding site to fit the substance.

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1st Law of Thermodynamics

Energy is constant, it can be moved but not created or destroyed

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2nd Law of Thermodynamics

Every energy transfer or transformation increases the entropy of the universe.

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Gibbs Free Energy (Enthalpy)

Amount of energy available and useful to do work ΔG

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Endergonic

The free energy in a system increases (unfavorable) Absorbed ΔG>0

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Exergonic

The free energy in a system decreases (Favorable) Released ΔG<0

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OIL RIG

oxidation is loss, reduction is gain

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Oxidation half reaction

Loses an electron, becomes positively charged (Reducing agent)

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Reduction half reaction

Gains an electron, becomes negatively charged (Oxidizing agent)

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Electron Tower

Tool that ranks different half reactions

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A+B -> A+ + B-

Oxidation half: A ->A+

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Reduction half B ->B-

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The Reduction potential

the tendency of a substance to gain electrons

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Redox Tower

Tool that ranks the ability to accept or donate in relation to other half reactions. The more positive it is, the more likely it is to accept electrons

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ΔG = -nFΔE

ΔG = Gibbs Free energy

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-n= Number of moles of electrons transferred

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F= Constant 96.485 kJ/V

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ATP

(adenosine triphosphate) main energy source that cells use for most of their work