Term
What links positive and Negative charged side chains on protein molecules? |
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Definition
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Term
What type of bond is a transient electrostatic interaction between oermanent and/or induced dipoles? |
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Definition
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Term
What is the importance of hydrophobic bonds in the body? |
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Definition
The provide structure and stability in membranes and proteins |
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Term
What is an amphipathic molecule? |
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Definition
One which contains both polar and nonpolar groups or regions. |
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Term
What does water DISSOCIATE into? |
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Definition
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Term
What does water ionize into? |
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Definition
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Term
What helps us prevent a dramatic change in pH throughout the body> |
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Definition
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Term
Regarding pH and pKa, how is a buffer most effective? |
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Definition
When the pH is +/- 1 unit within the pKa |
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Term
What are the 3 important buffers within our body? |
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Definition
Bicarbonate, Phosphate, and Protein |
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Term
What is the importance of the bicarbonate buffer? |
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Definition
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Term
With the bicarbonate buffer, what adjusts the [ ] of CO2? |
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Definition
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Term
What regulates the [ ] of HCO3- in the bicarbonate buffer? |
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Definition
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Term
True or False: There is a low [ ] of phosphates in intracellular fluids? (Phosphate Buffer) |
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Definition
False, there is a high [ ] |
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Term
What functional group is R-SH |
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Definition
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Term
What type of reaction is an intra-molecular shift of atoms or groups |
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Definition
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Term
During an oxidation, how is the molecule affected with respect to # of oxygens? Hydrogens? |
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Definition
Gains oxygens or loses hydrogens |
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Term
Which metabolic pathway would be considered biosynthetic/synthetic? |
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Definition
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Term
In a water molecule, which bonds are covalent? |
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Definition
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Term
In the absence of H2O, ionic forces are very strong. True or False? |
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Definition
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Term
What is a good example of a dipole-dipole interaction? |
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Definition
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Term
What is the technical name for london dispersion forces? |
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Definition
Induced dipole - Induced dipole interaction |
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Term
What is the difference between amphipathic (amphiphilic) and amphoteric? |
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Definition
Amphipathic - contains hydrophilic and hydrophobic groups
Amphoteric - can act as an acid or a base |
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Term
Describe the structure of an integral protein. |
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Definition
Hydrophobic A.A.'s form an alpha-helix and span the membrane |
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Term
What are the 3 components of the Bicarbonate buffer? |
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Definition
CO2 + H2O ----> H2CO3
H2CO3 -----> H+ +HCO3-
CO2 + H2O ----> H+ +HCO3- |
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Term
Are most amino acids in proteins levo or dextro? |
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Definition
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Term
What is a standard amino acid? non-standard? |
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Definition
Standard- found in protein sources
non-standard - not found but modified after protein translation |
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Term
At physiological pH are negatively charged amino acids considered acidic or basic? Positively charged? |
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Definition
Negatively - considered acidic
Positively - considered basic |
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Term
What type of bonds link amino acids? |
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Definition
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Term
What bonds together when amino acids combine with one another? |
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Definition
Carboxyl group of one a.a. and amino group of another a.a. Water is eluted |
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Term
What are 3 benefits of peptide bonds on protein polymers? |
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Definition
Add stability, creates planar structures, creates rigidity |
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Term
What is the primary structure of proteins? |
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Definition
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Term
With protein folding, what causes chain folding? |
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Definition
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Term
With an alpha helix, how is the helix formed? |
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Definition
H-bond between N-H of one amino acid and carbonyl oxygen of an amino acid 4 residues away |
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Term
How are beta-pleated sheets formed? |
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Definition
N-H group of one amino acid bonds with carbonyl group of adjacent chain |
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Term
What protein structure is known as the 3-D conformation? |
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Definition
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Term
On tertiary structures, where could one find H-bonds? |
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Definition
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Term
What is the difference between simple and conjugated proteins? |
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Definition
Simple- only amino acids
Conjugated- protein and nonprotein groups |
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Term
What is the prosthetic group in a glycoprotein? |
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Definition
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Term
What is the general structure of collagen? |
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Definition
3 helicies twisted together |
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Term
With collagen molecules, where can you find covalent bonding? |
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Definition
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Term
Which type of proteins contain a cavity/cleft and why? |
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Definition
Globular proteins. Cavity/cleft results from region of water depletion or the binding of a ligand |
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Term
What does amino acid catabolism result in? |
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Definition
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Term
What is the isoelectric point? |
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Definition
pH where the net charge is zero |
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Term
How is a strong acid/base a denaturing agent? |
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Definition
Alters H-bonds/salt bridges |
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Term
How are organic solvents and detergents denaturing agents? |
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Definition
Disrupts hydrophobic interactions |
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Term
How are reducing agents denaturing agents? |
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Definition
Converts disulfide bridges and disrupts H-bonds |
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Term
How can an increase in salt [ ] be denaturing? |
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Definition
Because salt binds to charged protein groups and causes a loss of solubility. Causes a precipitation |
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Term
How are heavy metals denaturing agents? |
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Definition
Disrupt salt bridges and bind to R-SH groups |
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Term
How can an increase in temperature be a denaturing agent? |
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Definition
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Term
How can mechanical stress be a denaturing agent? |
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Definition
Disrupts Protein structure |
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Term
What 4 ways can nitrogen be lost? |
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Definition
loss of epithelial cells, excretion of NH3 or urea, loss of undigested proteins, loss through sweat |
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Term
Where is the site of amino acid catabolism? (Generally and Specifically) |
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Definition
Liver in mitochondria and cytoplasm |
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Term
What is NH3 eliminated as in our body? |
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Definition
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Term
When NH2 is removed from amino acids, what is left? |
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Definition
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Term
What can alpha keto acids form? |
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Definition
Pyruvate and/or intermediates of TCA cycle |
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Term
NH2 + ? -----> glutamic acid |
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Definition
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Term
Glutamic acid undergoes deamination. Afterwards, what is formed? |
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Definition
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Term
What is NH4+ converted into? |
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Definition
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Term
How is carbanoyl phosphate formed? |
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Definition
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Term
Carbonyl phosphate + ornithine ----> ? |
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Definition
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Term
What significant event happens after citrulline forms? |
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Definition
It escapes the matrix into cytoplasm |
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Term
How is argininosuccinate formed? |
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Definition
Citrulline + aspartate + atp |
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Term
What does argininosuccinate break down into? |
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Definition
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Term
What are the products of the hydrolysis of arginine? and how does this occur |
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Definition
urea and ornithine by enzymatic reactions |
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Term
How does the [ ] of NH3 affect the rate of the urea cycle? |
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Definition
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Term
What does high protein and starvation do to the urea cycle? |
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Definition
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Term
Where do the 2 amino groups in urea come from? |
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Definition
1 from the interconversion of aspartic acid to pyruvate and the other from free ammonia created in gluconeogenesis |
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Term
What to urea cycle intermediates are shared with the TCA cycle and how? |
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Definition
Produces fumarate used in tca cycle and uses aspartate created by tca cycle |
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Term
How many atp's are used in the urea cycle |
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Definition
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Term
where does the excretion of nh3 take place? |
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Definition
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Term
What disease is caused by decreased protein intake? |
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Definition
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Term
What disease is caused by starvation? |
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Definition
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Term
How does liver failure affect NH3 balance? |
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Definition
NH3 is not converted to urea |
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Term
What does kidney failure do in respect to ammonia balance? |
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Definition
failure to excrete ammonia |
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Term
What do glucogenic amino acids break down into? |
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Definition
citric acid cycle intermediates |
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Term
How is succinyl CoA formed? |
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Definition
Unidirectional Transamination of essential amino acids |
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Term
Succinyl CoA is important for the formation of ________ which is then converted into _______ and ________ |
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Definition
Porphyrins for hemoglobin and myoglobin |
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Term
What is the reduced form of folic acid called? |
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Definition
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Term
What do Ketogenic amino acids produce in regards to energy sources? |
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Definition
Acetyl CoA and acetoacetate |
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Term
What does glycine and glutamate serve as? |
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Definition
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Term
What is tyrosine important in the formation of? |
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Definition
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Term
Dopamine is the substrate molecule for the development of what (2)? |
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Definition
epinephrine (adrenaline) and nor-epinephrine (noradrenaline) |
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