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33 Cards in this Set
- Front
- Back
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Know the biological functions for proteins
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keratin and collagen-give strenght and support to tissues
membrane proteins-transport samll organic molecules and ions across cell membranes insulin-regulates blood glucose levels hemoglobin-transports oxygen from the lungs to the tissues enzymes- catalyze and regulate all aspects of cellular function |
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Melvin Muddleup weighs 110 pounds.
How many grams of protein should Melvin consume in a day? Melvin is an adult |
0.8 grams of protein per kilogram of body weight
88 grams |
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How many common amino acids occur in the human body?
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20
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How many amino acids are essential for adults?
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10
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What can a vegetarian eat to assure that all essential amino acids are being consumed?
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grans-wheat, rice, and corn
legumes-beans, peas, and peanuts combo of these |
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What is a zwitterion?
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a salt that contains both a positive and a negative charge and it is neutral
proton transfer from the acid to the base in amino acid causes this salt to form |
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What is an isoelectric point of an amino acid?
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(pI) the pH at which the molecule is neutral
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Where is the N-terminal and C-terminal ends on a polypeptide?
Box in amide or peptide bond |
Left side-N-terminal end
Right side-C-terminal end C double bonded to O and connected to NH group!! |
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Why do enkephalins only have a short term affect in the brain of relieving pain?
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Because their peptide bonds are readlily hydrolyzed by enzymes in the brain
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What biological effect do oxytocin and vasopressin have?
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Oxytocin- stimulates the contraction of uterine muscles and initiates the flow of milk in nursing mothers
Vasopressin-ADH targets the kidneys and helps to keep the electrolytes in body fluids in the normal range-is secreted when the body is dehydrated and causes the kidneys to retain fluid thus decreasing the volume of the urine |
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What is the primary structure of a protein?
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it is the sequence of amino acids from the N-terminal end to the C-terminal end
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What are three types of secondary protein structure?
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alpha helix (fibrous protein)
beta pleated sheet random coil |
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How are fibrous proteins and globular proteins different?
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fibrous proteins are long linear polypeptide chains that are bundled together to form rods or sheets (insoluable in water and serves structural roles giving strength and protection to tissues and cells)
Globular proteins- coiled into compact shapes with hydrophilic outer surfaces that make them water soluable (Enzymes and transport proteins are globular to make them soluble in blood and other aqueous envir) |
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What are four types of attractive forces that maintain proteins tertiary structure?
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disulfide bond
hydrogen bonding salt bridges (+ and -) hydrophobic attraction (attraction of non-polar amino acids) |
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What would be the quaternary structure for a protein?
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the spacial orientation of multiple chains
ex: hemoglobin-2 alpha and 2 beta together as four chains |
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alpha keratins
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the proteins found in hair, hooves, nails, skin, and wool
long sections of alpha helix units having large numbers of alanine and leucine residues very soluable in water |
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collagen
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the most abundant protein in vertebrates
found in connective tissue such as bone, carliage, tendons, teeth, and blood vessels |
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hemoglobin
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conjugated proteins
globular present in red blood cells-transports oxygen to wherever is needed in the body 2 alpha chains 2 beta chains all four together make quartinary structure |
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myoglobin
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conjugated protien
globular protein stores oxygen in tissues |
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What happens to a protein when it undergoes hydrolysis?
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the amide bonds undergo hydrolysis forms the individual amino acids that comprise the primary structure
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List three ways to denature a protein
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high temp (raise temp)
add acid (lower pH) add base (raise pH) agitation use an organic solvent heavy metals such as Hg, Pb |
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apoenzyme
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the protein part of the enzyme
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cofactor
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the non protein part of the enzyme
can be a metal ion such as iron or copper can be an organic molecule(coenzyme) |
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substrate
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is the reaction in an enzyme catalized reaction
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active site
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the location on the enzyme where the substrate binds
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holoenzyme
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the protein plus non-protein part
biolgically active |
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enzymes always end in...
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-ase
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Use the lock and key model of enzyme action to explain why many enzymes will only react with one substrate
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the enzyme is selective for only one substrate, because only one substrate has the RIGHT SHAPE TO FIT at the acitve site
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What are some differences between the lock and key model and the induced fit model?
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The active site CHANGES SHAPE
the acitve site changes shape to match the shape of the substrate |
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Explain how an irreversible inhibitor can permanently destroy and enzymes activity.
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the inhibitor molecule forms a COVALENT bond with the enzymethat blocks access to the acitve site
permantly destroys actvity |
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What are two types of reversible inhibition?
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competitive
non-competitive |
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How are zymogens activated?
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additional amino acids in peptide chain are cleaved
(a zymogen is an inactive form of an enzyme) |
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Why do enkephalins only have a short term affect in the brain of relieving pain?
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Because their peptide bonds are readlily hydrolyzed by enzymes in the brain
blocks receptor site |
