STUDY GUIDE! BCMB 230
Popular in Human Physiology
Popular in Biochemistry
This 13 page Study Guide was uploaded by Jordan Gause on Friday February 5, 2016. The Study Guide belongs to BCMB 230 at University of Tennessee - Knoxville taught by John Alston in Spring 2016. Since its upload, it has received 195 views. For similar materials see Human Physiology in Biochemistry at University of Tennessee - Knoxville.
Reviews for STUDY GUIDE!
Report this Material
What is Karma?
Karma is the currency of StudySoup.
You can buy or earn more Karma at anytime and redeem it for class notes, study guides, flashcards, and more!
Date Created: 02/05/16
STUDY GUIDE FOR EXAM 1 (Chapter 1-5) Chapter 1: Homeostasis VOCAB - physiology: study of function; how things work - epithelial tissues: help with movement in and out of organisms, line intestines/skin - functional unit: subsets inside organs, which are created by joining of tissues (EX: nephron, which does the work of the organ) - organ system: group of related organs that work together - homeostasis: tendency for our body to maintain relative constant internal environment (EX: blood sugar, blood pressure) - set point: idealized value for object interested in; different for each person - negative feedback: change in variable being tested/regulated causes a response that brings this same variable back towards it’s set point, change in INTERNAL ENVIRONMENT (EX: when you get hot and sweat) - positive feedback: accelerates a process (EX: giving birth and contractions) - feed forward: don’t see an internal change, but there’s still a response; ANTICIPATION, but condition hasn’t changed yet (EX: mouth watering when smell food) - reflex opponent: pre-programmed response to stimuli - effectors: what does the actual reflex such as muscles, glands, and enzymes - extrinsic: nervous system reflexes and endocrine system reflexes; controlled from outside the organ - intrinsic: local reflexes; controlled from inside an organ - afferent: approaching something - efferent: exiting something - integrating center: processing center; PRIMARILY spinal cord or brain stem - hormone: chemical messenger; targets cells in one or more distant places in body - neurotransmitter: chemical messenger (neuron messenger) in close proximity - paracrine substance: chemical messenger which has an affect on another cell - autocrine substance: talks to itself Questions (answers are in back of book) 1. What are the 4 types of specialized cell types/tissues? 2. What are the three types of reflexes? 3. What would be the effect on the human body if negative feedback didn’t occur when you got cold? 4. In a reflex arc initiated by touching a hand to a hot stove, the effector belongs to which class of tissue? a. nervous b. connective c. muscle d. epithelial 5. Physiological changes that occur in anticipation of a future change to a homeostatic variable are called _________ processes. 6. A _____________ is a chemical factor released by cells that acts on neighboring cells without having to first enter the blood. Chapter 2: Chemical Composition of the Body and Its Relation to Physiology VOCAB - chemical bonds: hold atoms together; influence shape of a molecule; occurs when electrons transfer or are shared - covalent bonds: strongest and most common; sharing of electrons (need chemical reaction) - polar bonds: atoms at the end of bond are (+) and (-), electrons not equally shared, water soluble (EX: H20) - nonpolar bonds: electrons are shared equally, not water soluble (lipid soluble) - ionic bonds: weaker than covalent bonds, bond between ions, attraction between oppositely charged ions, DON’T NEED CHEMICAL REACTION (cations + and anions -) - hydrogen bonds: only occur with polar covalent bond molecules, weaker than ionic bonds, O N and S are atoms most likely used in this bond besides H - Van der Waals bonds: between the nuclei of very close-spaced atoms, can play a role in molecular shape - amphipathic molecule: sphere shaped in water, caused because nonpolar AND polar - hydrogen ions: measure the amount with the pH - pH: scale of how many hydrogen ions there are in a solution - acidic: release hydrogen ions in the water, pH<7 - basic: take up/use hydrogen ions in the water, pH>7, also called alkalines - carbohydrates: energy balance mostly, have about twice as much H as C and O (EX: C6H1206) - monosaccharide: simple sugar - polysaccharide: way we store sugar because multiple chains of molecules - lipids: fats; energy form, mainly C and H, use building blocks called fatty acids, have polar groups at the end, number of C is an even number - saturated fats: all hydrogen ions are used, no double bonds - unsaturated fats: not all the hydrogen ions are used because of the double bonds - triglycerides: nonpolar, constitutes most of fat in body, form when glycerol and 3 fatty acids form, major storage for lipids - phospholipids: amphipathic molecule, glycerol + 2 fatty acids+ phosphate container, in the structure of plasma membrane in the cell wall - cholesterol: C and H, chemical messengers (normally hormone) - proteins: very large; amino acids are the building blocks, amino group + COOH + R-group - R-group: makes amino acids different from each other; side chain (there are 20 types of amino acids) - peptide bonds: bond formed between the amino and carboxyl group - polypeptide: sequence of amino acids linked by peptide bonds, all proteins are polypeptides but not all polypeptides are proteins (proteins larger) - primary structure: influences how strings of amino acids fold on themselves, straight line of amino acids - secondary structure: actual folding of the amino acids - alpha helix: spiral folding - pleated sheet: folded fan - tertiary structure: secondary structure folded on self (interaction with R-groups) - quaternary structure: not all proteins have this; interaction between multiple polypeptides (tertiary structure) - denature: MAY be reversible, but not always; very hard to control with environmental conditions so want to prevent it, just change shape, not primary structure, this changes a great # of proteins, not just one - degrade: NEVER reversible, good CONTROL aspect because we use enzymes to speed up chemical reactions, chop off amino acid so change primary structure Questions 1. What are the three main macromolecules? 2. What is the difference between the terms polypeptide and protein? 3. Of the bonding forces between atoms and molecules, which are strongest? a. hydrogen bonds b. bonds between oppositely charged ionized groups c. bonds between nearby nonpolar groups d. covalent bonds e. bonds between polar groups 4. Molecules containing both polar and nonpolar regions are known as ________. ‘ Chapter 3: Cellular Structure, Proteins, and Metabolic Pathways VOCAB - ligand: any molecule (or other protein or ion) that is bound to a protein, no covalent bonds used so not permanent - binding site: region of a protein where a ligand binds, have a specific shape and charge distribution (R-group) - affinity: how likely/long I’m going to have an interaction between the ligand and the binding site (stronger connection if have right shape AND charge) - specificity: protein binding site only accepts limited types of ligands (EX: hemoglobin has binding site for 02 but also will accept CO - saturation: increasing ligand concentration increases saturation, and increasing saturation increases the function of the protein; 100% saturation=all binding sites for that protein are occupied - competition: multiple ligands can bind on same site, if one has more concentration or is a better fit they will “win” and kick out the other ligand - allosteric modulation: when a protein contains 2 different binding sites, the binding of a ligand to one site alters the shape of the other site - regulatory site: controls the shape of the protein by binding to a modulator molecule ligand - functional site: turns on and off the activity of a protein - covalent modulation: covalent bonding of charged chemical groups to some of the protein’s side chains, only single binding site, but can add a phosphate group, chemical reaction is involved - phosphorylation: changes the shape of the binding site - kinase: enzyme involved in covalent modulation, used if want to activate protein - phosphatase: another enzyme involved in covalent modulation, used it want to deactivate protein - transcription: make copy of what I need from DNA to RNA - exons: info I need - introns: info I don’t need - splicing: still have some introns, so take out this info, creates mRNA, acts on primary RNA transcript - translation: outside nucleus, take code in mRNA and use it to creat right primary structure, folding is part of this - prion: causes proteins to fold the wrong way - post translation modification: allosteric modulation and covalent modulation are examples of this - splitting: take protein and change primary structure and cause it to change the function, different from degradation because splitting is used to activate a protein while degradation is used to destroy a protein - plasma membrane: a lot of cellular activity is here, outside part of cell - phospholipid bilayer: main part of plasma membrane, polar and nonpolar ends where polar ends face outside and act as a barrier for water and water soluble substances - integral protein: embedded into nonpolar areas - transmembrane protein: on both sides of the membrane (span entire membrane), type of integral protein, help getting water soluble things across cell - peripheral proteins: bound to polar regions of the integral protein (EX: enzymes) - glycocalyx: on outside of membrane, help with cell recognition (EX: blood type is presence of protein with this) - cholesterol: key ingredient in the body, helps things move around; helps cell membrane from breaking - cytoplasm: inside part of cell, divided into cytosol and organelles - cytosol: fluid portion and anything dissolved in the fluid - nonmembranous organelles: organelles in cell that don’t have a membrane around them; cytoskeleton, filaments, ribosomes - cytoskeleton: skeleton of cell; gives cell some shape and may allow for movement - filaments: long chains of proteins involved - micro filaments: smallest, help with muscle contraction and support - intermediate filaments: larger than micro filaments, help with structure - micro tubules: larger than intermediate and micro filaments, move around chromosomes during division of cells; produce centrioles, mitotic spindle, and cilia - ribosomes: made up of RNA and proteins (translation), released into the cytosol, where they do function, also attach to ER which transfers them to the Golgi Apparatus - membranous organelles: organelles in cell that have membrane around them; ER, Golgi Apparatus, Lysosomes, Mitochondria - rough endoplasmic reticulum (ER): folded sheets of membrane and have ribosomes attached - smooth endoplasmic reticulum (ER): lipid metabolism and calcium storage - golgi apparatus: shipping/packaging center, final manipulations/modifications - vesicles: package we get from Golgi Apparatus, sphere of membrane and inside is something made in the cell - lysosome: strong enzymes that degrade proteins (acidic), recycling center of cell - apoptosis: activate lysosome and destroy cell completely, must be tightly controlled - peroxisomes: antioxidants, cause chain reactions and destroy cell membranes - mitochondria: has a double membrane, synthesis of ATP (more mitochondria= more ATP/energy) - irreversible reactant: huge difference in potential energy of products and reactants - reversible reactant: equilibrium between products and reactants - law of mass action: relative concentration of reactants and products, rate of forward=rate of reverse; so if A+B=C+D and A becomes 2A, than the reaction must move forward to maintain equilibrium Questions 1. What is it that these proteins do? 2. Allosteric Modulation is good with negative feedback because……? 3. What aspect is making a protein work or not during an Allosteric Modulation? 4. 3 ways we can control proteins 5. Difference between splitting and splicing? 6. Where is transcription and splicing occurring? 7. What determines the direction of the chemical reaction in a reversible reactant? 8. The fluid inside cells but not within organelles is called……? Chapter 4: Movement of Molecules Across Cell Membrane VOCAB - diffusion: movement of molecules from one location to another, very random movements (area of high concentration to low concentration) - gradient: difference in concentrations - viscosity: thickness of liquid - permeability: how easy something can move through the membrane - ion channels: water filled passageway that spans the bilayer, helps ions diffuse across the membrane - aquaporins: specific for water diffusion - monoatomic: mostly what these channels are going to accept; only one atom such as Na+ - polyatomic: multiple atoms, like HCO3, not normally transferred through ion channel - gating: manipulate shape of channel (if it’s opened or closed) - ligand gate channel: has binding site to channel proteins inside channel, producing either allosteric or covalent modulation - mechanical gate channel: disturbance to the membrane (stretching), affecting the channel protein - voltage gated channel: changes in membrane potential (voltage) can cause movement of certain charged regions on a channel protein, which alters its shape - mediated transport: has a membrane protein that has a binding site for the transported solute, which gets bonded to the protein, changing the shape of the protein, causing the binding site to be exposed to the other part of the membrane - facilitated diffusion: one type of transport, same as diffusion expect has a binding site and transporter protein - active transport: other type of transport that uses ATP since it moves from low to high concentration, or against the gradient - primary active transport: direct use of ATP, phosphorylates itself - phosphorylates: type of covalent modulation that changes the shape of the transporter and the strength of the transporter’s binding site (only move K, Na, Ca, and H) - secondary active transport: has two binding sites, one is for ion (normally Na+) and the other is for a second molecule - cotransport: both ions move in same direction - countertransport: move in opposite direction (Na+ goes from high to low concentration) - osmosis: diffusion of water (high concentration to low concentration) - osmolality: # of particles, tells us about water concentration, talks about penetrating and nonpenetrating solutes - isotonic solution: no net movement, cell unchanged because particles moving equally - hypotonic solution: water moves into the cell causing cell to possibly burst, less solutes outside cell than inside - hypertonic solution: water moves out of the cell causing cell to shrink, more solutes outside than inside - penetrating solutes: moving through the membrane - nonpenetrating solutes: not moving through the membrane; usually polar - tenicity: hyper/hypo/isotonic solutes, talks about just nonpenetrating solutes - intracellular: fluid inside cell is cytosol - extracellular: fluid outside cell either plasma or interstitial fluid - endocytosis: another way to move solute/water particles IN the cell - exocytosis: movement OUT of cell - paracellular transport: go in between cells; limited by size of particle - tight junction: reduces paracellular transport (not absolute) - transcellular transport: go through the cell, can do this by facilitated transport or active transport etc. - maximal flux: max amount/value of molecules allowed in the cell; can fix this by adding proteins - cellular respiration: sum of chemical reactions from glucose to ATP - glycolysis: in the cytosol - Krebs Cycle: in the mitochondria - oxidative phosphorylation: other word is called electron transport, in the mitochondria - acetyl coenzyme A: important for the linking step between glycolysis and Krebs Cycle - aerobic pathway: use of oxygen - anaerobic pathway: doesn’t require use of oxygen, extra step used in glycolysis if there is no oxygen to be used - protein metabolism: degrading proteins to amino acids, have to get rid of amino group (deamination) - urea: made by the NH3 from deamination, in the liver - transamination: switches the amino acid and keto acid R-group so they can attach to the binding site (EX: when NH2 and R- group binds to form amino acid) - beta oxidation: process that breaks down fatty acid’s chains of Carbons and creates ATP Questions 1. What is the energy source for diffusion? 2. Where does the concentration move (up or down) if each of these increased? (size of particle, interaction of particles, viscosity, gradient, surface area, permeability) 3. What is permeable to the cell membrane? 4. What are the three factors that change how long/often a channel opens? 5. Why do we have to use mediated transports for things such as amino acids and glucose? 6. In a primary active transport, does Na+ and Ca+ move to the outside or inside of the cell? What about K+? 7. What types of transports can move glucose? 8. 2 ways to change primary structure? 9. 2 ways to get multiple proteins from a single protein? 10. What is the normal osmolality of fluid outside and inside a cell? 11. What class of molecule is always penetrating? 12. What are the two types of ways to get through an epithelial layer? 13. How can I manipulate paracellular transport? 14. How do we store energy? 15. What is the general process of getting ATP from glucose? 16. If you don’t have enough oxygen, how many ATPs will you make? NEED TO KNOW THE GLYCOLYSIS, KREBS CYCLE, OXIDATION PHOSPHORYLATION, LINKING STEP BETWEEN GLYCOLYSIS AND KREBS CYCLE, BETA OXIDATION, AND PROTEIN METABOLISM DIAGRAMS/FLOW CHARTS GLYCOLYSIS KREBS CYCLE CELLULAR RESPIRATION DIAGRAM DEAMINATION TRANSAMINATION METABOLISM OVERVIEW
Are you sure you want to buy this material for
You're already Subscribed!
Looks like you've already subscribed to StudySoup, you won't need to purchase another subscription to get this material. To access this material simply click 'View Full Document'