Term
Water constitutes what % of a cell's weight? |
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Definition
70%-80% (The human body is usually around 60% water) |
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Term
Biomolecules that contain both hydrophilic and hydrophobic regions are called? Give an example |
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Definition
amphipathic e.g. amino acids |
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Term
| How do noncovalent bonds play a role in proteins? |
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Definition
| Intramolecular noncovalent interactions are largely responsible for the secondary and tertiary structure of proteins and therefore the protein's function in the mechanisms of life. Intermolecular noncovalent interactions are responsible for protein complexes (quaternary structure) where two or more proteins function in a coherent mechanism. |
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Term
Name types of noncovalent interactions. |
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Definition
van der Waals dipole–dipole forces hydrogen bonding London (instantaneous dipole–induced dipole) forces induced-dipole induced-dipole (dispersion forces) |
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Term
| What gives non-covalent bonds strength? |
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Definition
Noncovalent bonds, which are weak compared to covalent bonds, find their strength in numbers. Similar to Velcro, the more interactions you have, the stronger the binding of proteins. |
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Term
| Amino acids polymerize together to form? |
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Definition
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Term
| Nucleic Acids polymerize together to form? |
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Definition
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Term
| Monosaccharides polymerize to form? |
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Definition
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Term
| What are the most abundant elements in biological molecules? |
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Definition
SCHON-P Sulfur, Carbon, Hydrogen, Oxygen, Nitrogen, and Phosphorous All building blocks center around Carbon! |
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Term
| Which conformation of sugar is utilized in living cells? |
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Definition
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Term
What causes ionic interactions? Why do most ionic compounds dissolve in water? |
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Definition
Attraction of cations and anions NRG of hydration is greater than lattice NRG of crystal structure |
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Term
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Definition
Interaction of partially positive charged hydrogen in a molecular dipole with unpaired electrons from another atom. can be intra- or inter-molecular |
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Term
| Name 5 types of Hydrogen Bonds involving water |
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Definition
Water-water Alcohol-water Amine-water Peptide group-water Ester group-water |
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Term
| What has a larger bond radius: Covlent or van der Waals? |
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Definition
van der Waals! (covalent 0.062nm vs van der Waals 0.14nm) |
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Term
What causes hydrophobic molecules to adhere together? ex. Oil when in water |
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Definition
Hydrophobic effects (aggregation) e.g. Oil forms globules form because disruption of water lattice causes higher entropy (favored form) e.g. Formation of phospholipid bilayer (hydrophobic fatty acyl tails move to inside of layer) |
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Term
Which is a stronger binder (highest affinity)? Kd=10-10 or Kd=10-6 |
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Definition
Kd=10-10 Windsor Rationale: Less molecules to get the same type of binding |
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Term
| When monomers are polymerized, what is released (lost)? |
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Definition
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Term
What type of bond is formed when amino acids polymerize? What is lost? |
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Definition
Peptide bond water is lost |
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Term
What type of bond is formed when nucleotides polymerize? What is lost? |
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Definition
phosphodiester bond water is lost |
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Term
What type of bond is formed when monosaccharides polymerize? What is lost? |
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Definition
glycosidic bond water is lost |
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Term
| What is bone composed of? |
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Definition
| crystalline mineral salts and calcium, but collagen (Type 1) was stressed more by Windsor (big surprise) |
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Term
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Definition
| DNA[image]transcribed[image]RNA[image]Translated[image]Protein |
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Term
How many daltons is a 586 amino acid protein? |
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Definition
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Term
Protein's account for what percentage of a cell's weight? |
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Definition
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Term
| How is it that there are more human proteins (33,000) than genes (20,000-25,000)? |
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Definition
-Alternative RNA splicing -Protein Modifications |
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Term
| Name all the Hydrophobic Amino Acids. |
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Definition
Alanine, Valine, Isoleucine, leucine, methionine, Phenylalanine, Tyrosine, Tryptophan. LIMPVATT (Not Symbols) |
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Term
| Name all the hydrophillic Amino Acids |
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Definition
Lysine, Arginine, Histidine, Aspartate, Glutamate, Serine, Threonine, Asparagine, Glutamine SHAG-TAG-LA (Not Symbols) |
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Term
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Definition
| Lysine, Arginine, Histidine |
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Term
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Definition
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Term
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Definition
Serine, Threonine, Asparagine, and Glutamine. STAG (not symbols) |
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Term
| Where did asparagine get its name? |
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Definition
| Asparagine was first isolated in 1806 from asparagus juice, in which it is abundant -- hence its name -- becoming the first amino acid to be isolated. The characteristic smell observed in the urine of individuals after their consumption of asparagus is attributed to various metabolic byproducts of asparagine. |
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Term
What is considered the most rigid amino acid? What gives it this rigidity? |
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Definition
Proline It's distinctive cyclic structure. Found a lot in Collagen and alpha-helix |
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Term
What amino acid is the most flexible? Why? |
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Definition
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Term
| What is the only amino acid that is NOT Chiral? |
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Definition
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Term
Name amino acids that can be phosphorylated. What do they contain that allows this? |
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Definition
Serine, threonine, and tyrosine All contain -OH groups |
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Term
Name amino acids that can be glycosylated. What do they contain taht allows this? |
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Definition
Asparagine, serine, and threonine. Contain Nitrogen (N-Linked) |
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Term
| Name amino acids that can be hydroxylated |
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Definition
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Term
| Which amino acid has an imidazole, capable of binding metals? |
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Definition
Histidine has two nitrogen (imidazole) e.g. zince finger-DNA binding motif |
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Term
| What is the difference between ribose and deoxyribose? |
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Definition
The elimination of the 2' Oxygen. (Just making sure you're awake) |
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Term
How man rings do Purines have? Name the purines |
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Definition
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Term
How many rings do pyrimidines have? Name all the pyrimidines |
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Definition
One Uracil (RNA Only), Thymine (DNA Only), Cytosine ("Pie"rimidines..."C.U.T. PIE") |
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Term
What is the complementary DNA strand of the following? ACGATTCGA And the complementary RNA Strand? |
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Definition
DNA: TGCTAAGCT RNA: UGCUAAGCU |
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Term
| What is the simplest polysaccharide? |
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Definition
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Term
| What is the most common storage carbohydrate in animal cells? |
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Definition
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Term
| What are the most common storage carbohydrates in plant cells? |
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Definition
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Term
| Why is it bad to have high levels of triacylglycerol? |
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Definition
| Linked to cholesterol (LDL) |
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Term
| What is the pH inside of a cell? |
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Definition
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Term
| Where in a cell is the pH regularly around 4.5? |
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Definition
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Term
| A carbonic acid buffer has a pKa around? |
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Definition
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Term
| Acetic acid buffer has a pKa around? |
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Definition
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Term
| What is the primary type of potential enery in a living cell? |
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Definition
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Term
| If delta G is negative the reaction is (endergonic/exergonic)? |
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Definition
Exergonic Energy is released during reaction. |
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Term
| If delta G is positive, the reaction is (Endergonic/Exergonic)? |
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Definition
| Endergonic and needs energy added to the system in order for the reaction to occur! |
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Term
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Definition
| measure of a system's randomness or disorder |
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Term
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Definition
| energy needed to excite the reactants to achieve the transition state |
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Term
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Definition
| Chemical substance that accelerates the reaction by lowering the energy of the transition state, thus lowering the activation energy but doesn't change in the reaction. |
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Term
| Give an example of how unfavorable reactions are coupled with favorable ones in cellular processes. |
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Definition
Hydrolysis of ATP drives many cellular processes. e.g. NRG from Electron Transport Chain and Glycolysis produces ATP |
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Term
| What directs a protein's folding into the secondary, tertiary, and quaternary structure. |
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Definition
It's amino acid sequence in the primary stucture. |
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Term
| What are newly formed or forming polypetides called? |
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Definition
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Term
| Name perturbations that can lead to protein denaturation. |
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Definition
| heat, pH, chemicals (Urea & guanidine hydrochloride) |
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Term
What promotes protein folding in vivo? Give an example |
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Definition
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Term
| Name two characteristics of a protein that characterize how it binds to a ligand. |
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Definition
1. Specificity-ability of a protein to bind one molecule in preference to others. 2. Affinity-strength of binding (Kd =10-9 stonger binder than 10-6) |
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