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LSU - BIOL 1201 - Study Guide for Exam 2 - Study Guide

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LSU - BIOL 1201 - Study Guide for Exam 2 - Study Guide

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background image Some Things to know for Exam 2 Protein structure Shape relates to function All proteins have : Primary structure:  ­Description of the covalent bonds ( peptide bonds; polar covalent  bonds ) and the sequence of amino acids in a protein; very strong  * Figure 5.18 Secondary structure * Figure 5.19 ­result of repeated spatial pattern ­alpha helix ­beta pleated sheet  ­typically just a portion of the chain folds up into these  patterns ­flexible;  structure held in place by a bunch of weak interactions  (hydrogen bonds) Tertiary  ­looks like a blob ­3­D folding pattern ­result of weak bonds ­largely stabilized by weak bonds (hydrogen, hydrophobic  interactions) ­one exception to weak bonds: disulphide bridge (covalent bond) * Figure 5.18 Some proteins have :
background image Quaternary: multiple polypeptide chains (ex. hemoglobin) ­3­D pattern of joining several different polypeptide chains ­ how the two chains interact with each other is the quaternary  structure ­largely stabilized by weak bonds (hydrogen, hydrophobic  interactions) ­chains do not join together, just held together by weak bonds Spontaneous : ­Release free energy (exergonic) ­Delta G= negative ­Can occur without any outside help/energy ­Does not mean instantaneous ­Ex. rust ­almost all occur very very slowly Non­spontaneous ­Require free energy (endergonic) ­Delta G= positive ­Can occur only with help ­most reactions are non­spontaneous Equation for Free Energy : ∆G= ∆H­T∆S G ­ free energy
H ­ enthalpy (heat energy)
background image T ­ Temperature
S ­ Entropy (disorder)
Free energy and chemical reactions: ­Spontaneous ­Release free energy (exergonic) (reactants will end up with less energy) ­Non­spontaneous reactions: ­Require free energy (endergonic) (products will end up with more energy) Always be spontaneous: Enthalpy decreases, entropy increases Always be non­spontaneous: ­Enthaply increases, entropy decreases Induced Fit Model ­ the substrate binds to the active site ­this alters the shape of the enzyme *catabolic reaction: breaking of a bond ­creates a fit that promotes the reaction/ lowers the activation energy *figure 8.15, 8.18 in textbook Allosteric Inhibition occurs when the binding of one ligand or molecule decreases the  likeness or link for substrate at other active sites ­modifies the active site of the enzyme so that substrate binding is reduced 
or prevented
­the product may be vey different from starting material; wont be good fit a 
cooperative inhibitor

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School: Louisiana State University
Department: OTHER
Course: Introduction to Biology for Science Majors
Professor: Joseph Siebenaller
Term: Spring 2017
Tags: Biology and Biology 1201
Name: Study Guide for Exam 2
Description: basic things to know for exam 2
Uploaded: 09/28/2017
8 Pages 79 Views 63 Unlocks
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