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53 Cards in this Set
- Front
- Back
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What does the word protein mean?
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of the first rank (Greek)
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What % of your body is protein?
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50% dry mass
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What are the main elements found in protein?
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carbon, hydrogen, oxygen, nitrogen, and sulfur
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Where do you find proteins in your body? function?
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skin=elasticity
muscles=cables to move bones teeth=whitens hormones=membrane receptors hemoglobin=haulers blood vessels=elasticity |
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What are some non peptide components that can be added to proteins?
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metal ions or organic molecules
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How many AA are there?
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infinite
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How mant AA are in the standard set?
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20
8-9 of them needed to live 9=histonine bacteria grows in stomach |
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if you connect a large number of AA together you form a ?
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polypeptide
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Why do you not have free rotation around the peptide bond?
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the groups are too big
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What are the four ligands off an AA?
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Hydrogen, NH2, Carboxlyic, residue group
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What is unique about Glycine?
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side group of H
achiral no d and l form |
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What is unique about Cysteine and Methionine?
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contains sulfur
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What is unique about Proline?
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forms a ring
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What does Zwitter mean in German?
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hybrid
hermathodite |
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Isoelectric molecule
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the molecule is neutral
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Isoelectric point
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the point where no net migration of an AA can occur in an electric field
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Dynamic equilibrum
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a situation in which two opposing events occur at identical rates so that no net change happens
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Why is important for organism to control thwir pH levels?
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if the pH isnt controled, the electric charge on the protein changes. that affects the molecular level of life
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What are the fpur main types of AA
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nonpolar
polar acidic basic |
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What are the four levels of AA structure?
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primary
secondary tertitary quaternary |
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What are london forces
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the attraction between temporary dipoles
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What stereoisomer is metabolically active for human>
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L-AA
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What stereoisomers are metabolically active for bacteria?
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D and L-AA
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what are hydrogen bonds
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a force of attraction between hydrogens
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What is an Amide bond?
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bonds that hold amino acid together
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What are the two most important kinds of secondary structures?
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alpha helix and beta sheets
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What is a motif
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a specific area that looks similar
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Where do you find beta helixs?
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in verebrates
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Whta is the function of beta proteins?
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give strength to bones
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How are hydroprolines formed?
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formed after the intial polypeptide is made
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What do proline and hydroporline do?
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addvitamin C
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deficiency of Asorbic acid
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wounds not to heal and blood vessels to become fraagile
scurvy |
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what is ascorbic acid
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vitamin C
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how many AA in a loop?
in ten coils |
3.6 per loop
36 per ten coils |
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London forces
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a instint amount of time when it is blonking at the same time to form a polar bond when it is a nonpolar to polar attraction
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Dieases
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scrapie=sheep
mad cow=cow Creutzfeldt-Jakob D=humans spongiform encephalopathy kuru =humans |
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What is the pH of blood
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7.4
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Hemoglobin
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C2952 H4664 N812 O832 S8 Fe4
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Sickle cell
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one AA change in beta subunit of hemoglobon causes major change cell shape
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homozygous
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1 copy of bad gens from each parent
dead by 10 blood clots lethargy |
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hetergous
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1 copy from one parent
incomplete recesss exacerbated by strenuous exercise common in africa decent misquitos dont like |
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Collagen
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collegen has a left hand helix (beta_
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ionic bond
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salt bridge
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disulfide bond
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covalent
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london forces
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hydrophobic
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h-bond
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hydrophilic
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sickle cells dealing with valine and glu?
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valine is nonpolar
glu is polar |
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define fibrous
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like a rope
keratin/collagen fibers used for structural purposes |
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exapmles of fibrous
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hair
nails claws skin cartilage bone muscle fibers silk |
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decribe globular
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all enzymes (ball shaped)
all tansport proteins are globular exapmle=hemoglobin protein hormones are globular globulars a re metabolically active, not a structure part globular shape is held together by h bonds |
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how do you denture proteins
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change pH
heat it up |
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what changes when you change the pH of a protein
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h bonds change
secondary, tertiary and quaternary structures change usually temporary |
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describe what happens when you heat up a protein?
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peptide (covalent) bonds break
permanent change |
