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33 Cards in this Set
- Front
- Back
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where does chymotrypsin cleave
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aromatics, tyrosine, phe, trp
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where does trypsin cleave
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Arg, Lys
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carboxy peptidase
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hydrolyzes the carboxy terminal end of a peptide bond
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what are the only 2 AA with 2 chiral centers
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thr T, isoleucine (I)
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edman-degradation techinque is necessary to determine the amino acid sequence of a peptidey using what reagent
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phenylisothyiocyanate,
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what fraction of the coordination sites of ferrous iron in heme is occupied by O2 in and oxyhemoglobin subunit
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there 6 binding sites, 4 are coordinated to heme (via amide bonds), 1 bound to histidine, 1 bound to O2
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in myoglobin where is the heme group housed
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in the tetrapyrole ring
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how are His E7 and F8 important in bind O2 and locating the heme group
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N of His F8 bind to the 5th site on iron and HisE7 act as a gate of oxygen
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true or false myoglobin and hemoglobin are enzymes
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fales: they are globular proteins
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which globular protein is a tetrameric protein
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hemoglobin is a heterotetramer, 2alpha and 2 beta chains
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H2CO3
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carbonic anhydrase, enzyme that catalyzes the formation of bicarbonate and H+
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what effect does carbonic anhydrase have heme
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Heme in the tissues is bound by O2 carbonic anhydrase pushes oxyhemoglobin from the oxy to the deoxy form by pushing H+ onto heme allowing O2 to go to cells
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how does bicarbonate travelto lungs
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in 2 forms:
1. dissolved in plasma (3/4) 2. carbamino-hemoglobin, whose formation promotes the unloading of O2 fomr O2-Hb |
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what is the effect of DPG (aka BPG) on hemoglobin
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DPG/ BPG binds the T-form of hemoglobin, and shifts the sigmoidal curve to the Rt. (dec. O2 affinity)
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oxidoreductases
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catalyze redox reactions
ex: reducatses or peroxidases |
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transferases
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transfer a group fom on emolecule to another
ex: transaminases |
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lyases
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catalyze removal of grps to form dbl. bonds
ex: decarboxylases |
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isomerases
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catalyze intra molecular rearrangements
ex: epimerases, isomerases, mutases |
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ligases
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bond 2 molecules together many are called synthases
ex: carboxylases |
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how does cymotrypsin cleave proteins
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at the carboxyl end of armatics,= tyrosine, phe, trp
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aspartate transcarbamoylase (ATC-ase)
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catalyzes reactions between aspartate and carbamoyl phosphate this leads to synthesis of nucleobases needed for DNA and RNA synthesis
It is an example of allosteric binding=sigmoidal curve |
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what is the michaelis menton equation
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V=Vmax(S)/(S)+Km
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where does a competitive inhibitor bind
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Competes with substrate to bind the active site of the enzyme so it binds free enzyme= dec. in vmax and Km
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How do Vmax and Km change in competitve inhibition
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Vmax = same Km= inc.
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How do Vmax and Km change in non-competitive
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Vmax = dec, Km= same
binds free enzyme and E-S complex, binds at a site other than the active site |
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How do Vmax and Km change in un-competive
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Vmax = dec, Km=dec.
binds only the enzyme substrate complex |
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How do Vmax and Km change in in mixed
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Vmax = dec, Km = inc.
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catalytic effeiciency
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Kcat/Km
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turnover Number
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Kcat = Vmax/Eo
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ATC-ase is an example of an allosteric regulation what is its ATC-ase's activator & inhibitor
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ATP = activator, shifts sigmoidal curve to Rt. CTP =inhibitor shift sigmoidal curve to the lft.
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when divising a purification procedure for a desired protein which of the following is ABSOLUTELY essential part of the procedure
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ASSAY OF THE PROTEIN
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what is them most common technique used to selectivly precipitate out a desired protein or a larger portionof unwanted material
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Salting in: a poorly soluble protein is made more soluable by addition of salt
salting out: there is precipitation of a soluable protein by the addition of salt |
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Ion exchange chromatography
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you have a mixture of - and + charged proteins and beads of + charge. those with + charge will be flushed out while the neg. charged proteins stay behind. the - charged proteins are later flushed with with a - charged resin
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