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CSU - LIFE 102 - Life 102 Exam 2 Study Guide - Study Guide

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CSU - LIFE 102 - Life 102 Exam 2 Study Guide - Study Guide

School: Colorado State University
Department: Life Science
Course: Attributes of Living Systems
Professor: Louis Bjostad
Term: Spring 2016
Tags: Biology
Name: Life 102 Exam 2 Study Guide
Description: Typed study guide that covers chapters 8-11 from lecture notes. Outline form. Key terms, ideas, specific molecules and proteins we need to know are highlighted in different colors.
Uploaded: 03/09/2016
0 5 3 47 Reviews
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background image Exam 2 Study Guide  Life 102  Prof. Lou Bjostad By Elise Benton 
background image KEY TERMS        KEY IDEAS      KEY MOLECULES      KEY PROTEINS CHAPTER 8 CHEMICAL REACTIONS bonds breaking and forming Activation energy: initial energy needed to start reaction (energy barrier)  often supplied as heat from surroundings  METABOLISM: totality of an organism chemical reactions  metabolism is an emergent property of life: emerges from interactions between molecules within
the cell 
metabolic pathways: series of steps that begins with a specific molecule and ends with a 
product 
each enzyme and molecule different from last catabolic pathways: release energy by breaking down complex molecules into simpler one uses hydrolysis cellular respiration­ breaks down glucose with oxygen anabolic pathways: consume energy to build complex molecules from simpler ones synthesis of proteins from amino acids
PHYSICS
kinetic energy: energy of motion heat: or thermal energy, kinetic energy associated with random movement of atoms or 
molecules
potential energy: energy due to location or structure  chemical energy: potential energy available for release in a chemical reaction  thermodynamics: study of energy  transformations First Law of Thermodynamics:  energy can be transferred or transformed, but not created or 
destroyed
2nd law of thermodynamics: energy transfer/transformation increases entropy: disorder of 
universe 
some energy is unusable some is lost as heat  cells create ordered structure from less ordered materials universes total entropy is increased  free energy change: ΔG, living systems free energy can do work  negative free energy change processes are spontaneous  no energy input, occur on their own can be used to do work  start: more free energy, less stable, greater work capacity  change: spontaneous change, free energy decreases, system becomes more stable, free 
energy is released and used for work 
end: less free energy, more stable, less work capacity exergonic reaction: releases free energy into its surroundings spontaneous, often gravitational 
background image endergonic reactions: absorbs free energy from its surroundings  non spontaneous
ATP
ATP does work by energy coupling  overall exergonic reaction energy is released when terminal phosphate bond is broken  ATP­ phosphate group= ADP release of energy powers cellular work energy is consumed to add phosphate to ADP to make ATP= phosphorylation molecules that gain phosphate are phosphorylated energy to phosphorylate comes from catabolic reactions ATP used to change shape of carrier proteins, propel motor proteins through cytoskeleton
ENZYMES: catalytic, speed up metabolic reaction without being consumed by it
speed up reaction by lowering activation energy  don’t affect total free energy change, only speed up reaction that was going to happen anyways specificity each enzyme only works with specific molecules substrate: reactant that enzyme works with  active site: region on enzyme where substrate binds lowers activation energy orients substrate correctly strains substrate bonds provides favorable microenvironment covalent bonds to substrate induced fit: active site slightly changes shape to better fit substrate, enhances ability to catalyze 
reaction
enzymes have specific temp and pressure in which they operate Regulating enzyme activity all cells regulate metabolic pathways  switching: on/off genes that encode enzymes regulation allosteric regulation: inhibits or stimulates enzyme activity regulatory molecules bind to protein at ONE site and affects protein function at ANOTHER site polypeptide subunits enzymes have active and inactive forms activator: stabilizes active form inhibitor: stabilizes inactive form cooperativity: amplifies enzyme activity binding of substrate stabilizes changes in shape to all other subunits, makes each loading faster enzyme inhibitors competitive: bind to active site of enzyme, competing with substrate noncompetitive: bind to another part of enzyme, causes enzyme to change shape  active site less effective feedback inhibition: end product of metabolic pathway shuts down the pathway prevents waste of cell resources, no more product synthesized than necessary  localization of enzymes in cells

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School: Colorado State University
Department: Life Science
Course: Attributes of Living Systems
Professor: Louis Bjostad
Term: Spring 2016
Tags: Biology
Name: Life 102 Exam 2 Study Guide
Description: Typed study guide that covers chapters 8-11 from lecture notes. Outline form. Key terms, ideas, specific molecules and proteins we need to know are highlighted in different colors.
Uploaded: 03/09/2016
12 Pages 76 Views 60 Unlocks
  • Better Grades Guarantee
  • 24/7 Homework help
  • Notes, Study Guides, Flashcards + More!
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