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KINE 301 - Week 2 - 2016 - Dr. Gibson

by: Jay Ko

KINE 301 - Week 2 - 2016 - Dr. Gibson KINE 301

Marketplace > Rice University > Kinesiology > KINE 301 > KINE 301 Week 2 2016 Dr Gibson
Jay Ko
Rice University
GPA 3.8

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Notes from week 2 in the 2016 fall semester with Dr. Gibson
Human Physiology
Dr. Brian Gibson
Class Notes
Kinesiology, Physiology
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This 5 page Class Notes was uploaded by Jay Ko on Friday September 9, 2016. The Class Notes belongs to KINE 301 at Rice University taught by Dr. Brian Gibson in Fall 2016. Since its upload, it has received 3 views. For similar materials see Human Physiology in Kinesiology at Rice University.


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Date Created: 09/09/16
8/29/16 – Ch. 4 Properties of Living Organisms o Emerging properties are ones that cannot be predicted o Table properties  See table 4.1  Energy transfer in the environment o We take in 2000 calories in the day  Burn off the rest but some stores as fat and most goes in as protein  The relationships between kinetic and potential energy o Kinetic energy – the energy of movement  Motor protein  Moving something back and forth between a membrane  Muscle movement o Potential energy – stored energy  Concentration gradients  Cell membrane and on one side, lots of sodium and the  other side doesn’t o Utilizing this concentration gradient to do  something o How much energy do you have to put in to keep  sodium there?   ATPases move these things o Chemical bonds  Every split bond is energy released  Chemical reactions o Combination reaction = A+B  C o Decomposition = C  A+B o Single displacement o Double displacement  Activation energy and exergonic/endergonic reactions o Activation energy  Push needed to start a reaction o Exergonic reactions release energy because the products have less energy  than the reactants  Large net free energy change o Endergonic reactions trap some activation energy in the products, which  then have more free energy than the reactants  Energy transfer and storage in biological reactions o When energy is released, released as high energy electrons captured by  NADPH, NADH, FADH2 o A lot of energy released is lost as heat energy  Some reactions have large activation energies o To lower the activation energy  Use enzymes  Need control  Diagnostically Important Enzymes o Specific increased levels of enzymes can lead to diseases  Effect of pH on enzyme activity o Most enzymes in humans have optimal activity near the body’s internal  pH of 7.4  Enzymes lower the activation energy of reactions  Classification of Enzymatic Reactions  Metabolic pathways resembles a road map o Metabolism – any reaction in the human body o Anabolism – Building things up o Catabolism – Breaking things down  Feedback Inhibition o When we finally accomplish a goal and have enough of whatever we’re  producing, it will be shut off.   The Reversibility of Metabolic Reactions is controlled by enzymes o Some reversible reactions use one enzyme for both directions  Carbonic acid  Increasing CO2 will decrease carbonic anhydrase  Increasing H2O will increase carbonic anhydrase o Reversible reactions requiring two enzymes allow more control over the  reaction o Irreversible reactions lack the enzyme for the reverse direction   ATP Production o Aerobic Metabolism of Glucose  Glucose + O2 + ADP + Pi  CO2 + H2O + ATP  Glucose + 6O2 (30­32 ADP + Pi  30­32ATP)  6CO2 + 6H2O  Advantages  Fast   Anaerobic  Disadvantages  Low energy yield  Lactic acid  Occurs in the cell’s cytosol o Krebs  Aerobic   Occurs in the mitochondria  Dependent on the number of mitochondria o Glycolysis – FOR REAL  Key regulator enzyme  Phosphofructokinase  o PFK  6 carbon glucose become 2, 3 carbon pyruvates  9 or 10 steps  First half of this process consumes energy  Get 2 ATP at a fast rate without oxygen  Glucose goes into the cell and cannot leave the cell when a  phosphate attaches to it  Add an ATP do start the process – a primer step  All turns into 2 Glyceraldehyde 3­phosphate   This turns into 2 1,3 Bisphosphoglycerate  o NADH is produced – electron carrier  Worth about 2.5 or 4 ATP each  2 Pyruvate is produced at the end of glycolysis o Pyruvate, Acetyl CoA, and the Citric Acid Cycle  If the cell has adequate oxygen, pyruvate is transported into the  mitochondria  Pyruvate reacts with coenzyme A to produce acetyl CoA, one  NADH, and one CO2  Acetyl CoA has two parts: a carbon acyl unit, derived from  pyruvate, and coenzyme A  Coenzyme A is made from the vitamin pantothenic acid.  Coenzymes like enzymes are not changed during reactions and can be reused  2­Carbon acyl unit enters the cycle by combining with a 4­carbon  oxaloacetate molecule  The 6­carbon citrate molecule goes through a series of reactions  until it completes the cycle as another oxaloacetate molecule.   Two carbons are removed in the form of CO2.  Most of the energy released is captured as high­energy electrons on three NADH and one FADH2. Some energy goes into the high­ energy phosphate bond of one ATP. The remaining energy is given off as heat.   Electron Transport System o Electrons moved from citric acid cycle. o Pumped H+ ions in the intermembrane space. o Hydrogen ions will lead back to the ATP synthase o Produces water and gains ATP o Some hydrogen that comes into the ETS can leak back into the matrix and  lose a little bit of the 3­2 relationship.  Summary o Does not yield exactly 2 or 3 ATP as originally described in texts due to  hydrogen leaks. o Cytoplasmic NADH sometimes yields only 1.5ATP/NADH instead of  2.5ATP/NADH o Aerobic metabolism  0 NADH and 2 ATP  o Aerobic  6 H2O  30­32 ATP  6CO2  Pyruvate is the branch point between aerobic and anaerobic metabolism of  glucose o But what happens when oxygen supply cannot keep pace with ATP  demand, such as often as if happens during strenuous exercise  It will get backed up o Does this depend completely and only on the levels of available oxygen  within the cell? Why or why not?  The genetic code as it appears in the codons of mRNA o 20 amino acids can make over a million types of proteins o Proteins are key to cell function o One amino acid change like in sickle cell anemia will deform a red blood  cell  Hemoglobin protein will change  Changes shape of the cell into a sickle and not a biconcave disk  Overview of protein synthesis o Gene activation  Transcribed and rewritten  Genes continuously transcribe to mRNA o mRNA processing  Alternative splicing  Interference   mRNA can be silenced this way  Creation of isozymes is probably explained by alternative spicing   Happens in the nucleus o Translation  rRNA in ribosomes  tRNA  Amino acids  These three used to create the protein o Post transitional modification  Fold and cross links  Cleave protein into smaller parts or peptides  Addition of   Sugars  Lipids  ­CH3  Phosphate  Assembly into polymeric proteins o Overview of transcription  RNA binds to DNA  Section of DNA that contains the gene unwinds  RNA bases bind to DNA creating a single strand of mRNA  mRNA and RNA polymerase detach from the DNA and the  mRNA goes to the cytosol after processing  o mRNA processing  Introns removed and exons kept  More than one protein can be created if exons are split up o Overview of translation  Transcription  mRNA processing  Attachment of ribosomal subunits  Translation  Termination   Disease States o Sickle Cell Anemia  One substitution valine for glutamate  Negative effect on protein and cell  Functional consequences to organism  o Tay Sachs Disease  Hexosaminidase A  These enzymes are supposed to be breaking things apart  Too low of a level or there but not acting properly   Which enzyme from which storage vesicle?  Normal activity of the enzyme?   Negative effects of malfunctioning enzymes?   Function consequence to organism? 


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