Biochemistry: Amino Acids and Proteins

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Can you name the Biochemistry: Amino Acids and Proteins?

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DefinitionTerms
Removing HCO3- ion (bicarbonate) from the blood by kidneys helps to ____________ pH.
The concept that deoxygenated Hb has a higher affinity for CO2
Acidosis can be an indicator for.....
Drug that induces erythropoesis of gamma-globin
Adult Hb shifts the O2 binding curve to the...
High temperature shifts the O2 binding curve...
-log[H+]=
Phenylalanine (Essential or Non-Essential)
When oxygen is bound to the heme iron it is in which form? (T or R)
Cysteine (Essential or Non-Essential)
pKa=
Asparagine (Essential or Non-Essential)
Blood pH above ________ can result in coma and death.
________________ regions tend to be structural and functional regions between homologous proteins.
Low 2,3-BPG levels shift the O2 binding curve
A2 Hemoglobin structure
At low pH the amino acid is ______________ at both the amino and carboxyl groups.
Threonine (Essential or Non-Essential)
Which organ plays the fastest role in maintaining blood pH?
Arginine (Essential or Non-Essential)
Heat shock protein family that is only involved in protein folding
Methionine (Essential or Non-Essential)
These help to stabilize the folding and unfolding intermediates
Hb with ferric form of iron ion can't beind oxygen. This form of Hb is called....
Which hemoglobin state has a lower binding affinity for oxygen?
Removing CO2 from the blood by the lungs helps to ____________ pH
When blood pH is above _________ it is considered alkalosis
Tryptophan (Essential or Non-Essential)
Heat shock protein family that is involved in protein folding, prevents aggregation and assists transport of proteins to organelles
At high pH the amino acid is ______________ at both the amino and carboxyl groups.
Hypoventhilation makes the blood
DefinitionTerms
Glutamine (Essential or Non-Essential)
A1C Hemoglobin structure
Chemical that minimized the change in pH of a solution by binding excess H+ while also being able to release H+ if pH is low
When oxygen is not bound to the heme iron it is in which form? (T or R)
Functional regions of the tertiary structure are referred to as
Sickle cell doesn't affect which Hb subunit chain?
High 2,3-BPG levels shift the O2 binding curve....
Protein folding is primarily driven by
Serine (Essential or Non-Essential)
Persistent, prolonged vomiting can result in...
Proline (Essential or Non-Essential)
Which secondary structure is more stable?
Co-chaperson for Hsp60
Normal range of female Hb at sea level
Lysine (Essential or Non-Essential)
Normal range of male Hb at sea level
High serum carbon monoxide concentration shifts O2 binding curve
The higher the altitud you to the _________ Hb your body will produce? (more/less)
Fetal Hb shifts the O2 binding curve to the....
Isoleucine (Essential or Non-Essential)
The lid structure of the E. coli chaperonin system is
Low temperature shifts the O2 binding curve....
Alanine (Essential or Non-Essential)
Leucine (Essential or Non-Essential)
The E. coli chaperonin system requires ________ ATP
Similar proteins found in different organisms
Glycine (Essential or Non-Essential)
Low pH causes the O2 binding curve to shift...
Histidine (Essential or Non-Essential)
P50 of fetal Hb (mmHg)
Co-chaperone for Hsp70
DefinitionTerms
Failure of the lungs to eliminate CO2 as fast as it is produced is called
When there are equal amounts of protonated and deprotonated acid molecules...
P50 of adult Hb (mmHg)
Deoxygenated Hb has a higher affinity for H+ ions
Pressure at which 50% of hemoglobin is saturated
 
Valine (Essential or Non-Essential)
Drug that inhibits Hsp90 by binding to the ATP binding pocket
Blood pH below _______ can result in coma and death.
Hsp90 works with which other protein?
When the blood pH drops below ________ it is considered acidosis
High pH causes the O2 binding curve to shift...
Hsp protein mutaions are known to be responsible for
Alpha helicies are generally ______ resides long with _______ amino acids per turn
Hsp70 mainly serves to
Enzyme that assists in the formation, rearrangement and breaking of disulfide bonds
The most important buffer in maintaining pH balance in the blood
Blood pH must be maintained around....
A Hemaglobin structure
Low serum carbon monoxide concentration shifts the O2 binding curve
Amino acid that forms covalent bonds between sulfers
The concept that upon each binding of an O2 to a heme subunit causes a higher affinity for the next O2 binding is called...
This type of breathing can cause alkalosis.
F Hemaglobin structure
Chemical that 'locks' Hb in T-state forcing the release of oxygen
Secondary structure is a result of __________________ between amino acids within a protein.
Aspartic Acid (Aspartate) (Essential or Non-Essential)
Glutamic Acid/Glutamate (Essential or Non-Essential)
Less toxic Hsp90 inhibitor that blocks ATP binding pocket

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