Busy. Please wait.
or

show password
Forgot Password?

Don't have an account?  Sign up 
or

Username is available taken
show password

why


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
We do not share your email address with others. It is only used to allow you to reset your password. For details read our Privacy Policy and Terms of Service.


Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
Don't know
Know
remaining cards
Save
0:01
To flip the current card, click it or press the Spacebar key.  To move the current card to one of the three colored boxes, click on the box.  You may also press the UP ARROW key to move the card to the "Know" box, the DOWN ARROW key to move the card to the "Don't know" box, or the RIGHT ARROW key to move the card to the Remaining box.  You may also click on the card displayed in any of the three boxes to bring that card back to the center.

Pass complete!

"Know" box contains:
Time elapsed:
Retries:
restart all cards
share
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

Bio-Chem 1 Test

QuestionAnswer
What are the four bio molecules? Amino acids/proteins Carbohydrates Nucleotides/Nucleaic acids Lipids
The solvent in bio chemistry is what? Water
Switter ion has a positive and negative charge
True or false: Most amino acids are chiral compounds? True!
Alpha amino acids consist of a ____ and a ____ amine and a COO- group
aromatic amino acids absorb_____ by using a spectrograph or what ever its called.. UV light
Aromatic R groups? Tryptophan, Tyrosine, Phenyalanine
Positively Charged R groups Arginine, Lysine, Histidine
Negatively Charged R groups Aspartate, Glutamate,
Nonpolar alaphatic R groups Leucine, Iso-Leucine, alnine, glycine, Proline, Valine, Methionine (Dont like water, R groups form a hydrophobic interatction)
Polar, Uncharged R groups Serine, Threonine, Cysteine, Asparagine, Glutamine (Hydrogen Bonding)
Essential Amino Acids Valine, Leucine, Isoleucine, Methionine, Threonine, Phenylalanine, Tryptophan, Lysine
DNA------------>Proteins expression
DNA------>mRNA-------> Transcription, Translation
Uncommon amino acid selenocysteine
Metabolites Citrulline, Carnetine, Taurine, Creatine
L-Citrulline and Ornithine Intermediats of urea cycle
Carnitine Transfers FA across membranes into mitochondria so it can be used for energy production
Taurine: Bile acid (acts like soap and creaks up FA) Helps aid in digestion
Creatine: Intermediat storage of energy in muscles (skeletal)
PI PI= pka+pka2 Basic: pkR+pk2 -------- ------- 2 2 Acidic: pkR+pk1 --------- 2
Non covalent(weak interactions) in aqueous solutions: Hydrogen Bonding Ionic Bonding Hydrophobic Interaction (nonpolar function groups associate with each other, want to get away from H20) Vanderwalls forces
Proline: Only one where R group forms ring with alpha amino group
Gylcine Is chiral true or false? False
Methionine: Contains sulfure Theo ether
Cystenine: Second amino acid which contains sulfur. 2 cysteine--> disulfide bond
A280 is used to estimate the concentration of what? Protein concentration
Positively Charged R groups Nitrogen containing R groups, are basic in nature and can get positively charged when pronated Basic amino acids
Histidine: Very often found at the active site of enzymes. Enzymes are proteins that function as catalysts because pkR is close to 7
Negatively charged R group: Acidic Amino acid pkR is less then 7 ending with ate=acid
Olgopeptide: small polymer (with a few amino acids) Ex. oxytocin (hormone), 9 amino acids. Triggers contractions Bradykinin: 9 amino acids (inflamation)
polypeptide/Proteins Polypeptide: are less then or equal to 10,000g/mol Proteins: > 10,000 g/mol
Alanylglutamylglycyllysine 1 2 3 4 Produces 4 water molecules
HDL/LDL High density lipoprotein/ Low density lipoprotein
Proline: Restricts folding of backbone because a-N is part of backbone
Glycine: very small, vertually not steric hindered. allows for very narrow turns
Tryptophan: Very large, alot of steric hindrance, leads to some restrictions as to how the backbone can fold
Fibrous proteins: -Linear, long strands of polypeptides or proteins, forming "fibers" - Typically only one type of secondary structure - Functions: support shape and structure
Globular proteins: more or less spherical shape Much more complexity and variability with respect to secondary structure Functions: biocatalyst and regulation
Fibrous Proteins: -Keratin Structure- all alpha helix
Fibrous proteins: - silk fibroin all beta sheet
Fibrous proteins: -Collogen Struture: all alpha helix - triple helixes of poly peptides -Disulfide bond, H bonding
Ligand(Key) : Molecule (or ion) that can bind reversably to a protein creating quilibrium between protein & Ligand P+L ---->PL
Binding Site (Lock): -Where Ligands bind -Structure complimentry to structure of ligand -binding non covalent -a protein can have multiple binding sites and multiple ligands
Enzymes: E+S---->ES---->EP------> E+P = product (E= enzyme, S= Substrate)
Oxygen binding proteins: Oxygen bings at prosthetic group (Heme) (Porphyrine)ex. chlorophyll
Examples of globular proteins: Myoglobin/Hemoglobin
Myoglobin: -binds oxygen -contains a heme group(prosthetic)which is responsible for carrying oxygen molecules to muscles
Protein function: Oxygen wants the last electron in the outer shell of FE2 (attracted to the unpaired electron in FE2+) Free electron pars stabalize Fe2+
Ligand binding site: Theta= occupied binding sites/available binding sites
Allosteric effect: - Binding of a ligand leads to a... Confermation change of prtein structure and changes properties of other ligand binding sites within the protein
Allosteric effect: - In heoglobin Deoxyhemoglobin-->low affinity for oxygen; upon binding of one oxygen confirmation of hemoglobin changes-->increase in affinity for oxygen
Allosteric effect: Sigmoid bonding curves result from alosteric efects
BPG Bisphosphoglycerat -- -- ---
BPG (Bisphosphoglycerat): Allosteric activator of hemoglobin increase the sigmoid effect-->decrease the affinity for oxygen
Less Oxygen creates more? BPG
BPG effect on Hemoglobin: -Low O2 supplies for hours -[BPG] go up-->lower affinity for O2 -Change in [BPG] takes 24-48 hours (time it takesk to recover from altitude sickness)
High altitude for a long time: -More red blood cells -increase in Hemoglobin -increased # of binding sites
lifespan of a red blood cell: 120 days
Effect of pH on O2 binding of Hb: pH affects protenation of charged R groups--> changes in non covelant interactions pH decreases-->affinity for O2 decreases pH increases-->affinity for O2 increases
pH in blood: -Cellular respiration C6H12O6+6O2--->6CO2+6H2O (glucose) CO2+H2O-->H2CO3--> H+ + HCO3- <-- <-- (pH)
Stabalization of pH: -Buffers (phosphate, amino acid R groups) - about 30% of CO2 binds to Hb(and does not react with water) -about 10% will form carbonic acid
(In lungs) (In tissue) CO2 + H2O ---> H+ + HCO3- pH increases pH decreases pH effect= "BOHR effect"
Carbon Monoxide: -Oderless gas -Binds to Oxygen binding site, 240x more tightly bound then oxygen -prevents O2 from binding -Prevents switch to lower affinity state(hyperbola) -anemia ---> sigmoid binding curve
Hemoglobin: -Hb is transferred via the placenta from mother to child - About 30mmHg(4kpa) of hemoglobin in tissues and 80mmHg(13kpa) in lungs
Anemia: -iron defficiency -most common form -If iron is not present we cannot make hemoglobin, oxygen cant be transferred -Hb function is not altered-->alosteric affect of O2-->high and low affinity
Sickel Cell Anemia: -Under supply of oxygen -CO prevents switch to lower affinity state(hyperbola) -Sigmoid binding curve
Better to have anemia or CO poisoning? Anemia!
Fetal Hb: -Not bonding site for BPG -As soon as a baby is breathing-->gamma polypeptide NOT expressed and expression of beta polypeptide starts -alpha2gamma2: gamma polypeptide has slightly different AA sequence which leads to higher O2 affinity
Genetics sickle cell anemia: -Mutation in gene of Beta subunit (point mutation=1 base in DNA is changed) -Homozygous individuals(carry mutation on both chromosomes)at high risk
Genetics of sickle cell anemia: - Heterozygous/homozygous -Homozygous individuals(carry mutation on both chromosomes)at high risk -Heterozygous individuals(carry the sickle cell trait)
Heterozygous (carriers of sickle cell anemia) -Minimal Risk -Have protection from malaria
Malaria: Caused by a parasite called plasmodium which feeds on red blood cells
The configuration at the alpha-carbon of the vast majority of naturally occurring amino acids is_____? L-configuration
Threonine is an_______ amino acid Polar, uncharged R group
____ Has a pkR that is close to 7 and hence is commonly found at the active site of enzymes. Histidine
Hydrophobic interactions occur between ______ R-groups Nonpolar, aliphatic R groups
The only uncommon amino acid found in proteins that is modified pre-translation is_____? Selenocysteine
Carnitine (an uncommon amino acid) Transports fatty acids into the mitchondria
The pl of aspartate is______? (pK1=1.88, pK2=9.60, pKR= 3.65) Aspartate is a negatively charged R group. Negative=acidic PI calculations: -basic---> pkR+pk2/2 -acidic----> pkR=pk1/2 -neutral--> pk1+pk2/2
True or flase: Every peptide bond is an amide bond? TRUE!
What creats proteins? Ribosomes
Oligopeptide: -Small polymer (w/few amino acids) Ex. oxytocin(hormone)--> 9 AA's -Triggers contractions -Antiboitics->inhibit the growth of bacteria
Polypeptide: Less then or equal to 10,000 g/mol
Proteins: > then 10,000g/mol
Alanylglutamylglycyllysine ----- ------- ----- ----- Produces 4 water molecules
"Sub-Units" individual poly peptides encoded by seperate genes -become functional via further modification
Di-Sulfide bond: Covalent stabalizing factor to stabalize functional proteins (needs enzymatic action) --between polypeptides or within
Insulin was published in: 1953
The three dimensional structure of proteins: -Primary structure Amino acid sequence
The three dimensional structure of proteins: -Secondary structure Motives in confirmation found in many tertiery structures alpha-helix beta sheet
The three dimensional structure of proteins: - tertiary structure 3-D structure (confirmation) of a polypeptide and its prosthetic group
The three dimensional structure of proteins: -Quarterary structure 3-D arrangement of subunits, in a functional protein
Stabilizing forces: -Non covalent forces (form randomly) -Hydrogen bonding -Ionic Bonding -Hydrophobic Interactions -Vanderwalls forces
Protein backbone: Main stabilizing force is H-bonding Beta-confirmation= backbone
Tertiary and Quaternary structures: -Distant AA's can interact and cantribute to stabilization of 3D structure. - Noncovalent and covalent stabilizing forces
Proline: restricts folding of backbone because a-N is part of backbone
Glycine: Very small, virtually not sterically hindered; leads to some restrictions as to how the backbone can fold.
Tryptophan: Very large, very sterically hindered,leads to some restrictions as to how the backbone an fold
Collagen Biosynthesis: -A Ribosomes in the rough ER
Collagen Biosynthesis: -B 1st enzymatic modification -Hydroxylation -Vitaman C required
Collagen Biosynthesis: -C 2nd enzymatic modification -glycosylation (polydroxy compound)
Collagen Biosynthesis: -D 3rd enzymatic modification - Di-sulfide bonds between 3 modified polypeptides arargned in a triple helix
Collagen Biosynthesis: -E Pro-Collagen -In golgi vessicles
Collagen Biosynthesis: -F 4th enzymatic modification - in extra cellular matrix - removal of C and N terminous
Ligand Binding: The higher kd= the lower the affinity of the protein for the ligand. Lower kd= higher affinity of protein for ligand
kd: kd=[ligand] where 50% of binding site is occupied
Difficient in Vit C = ? Scurvy!! -Insuficient collagen
Symptoms of sickel cell anemia: Weakness, Muscle pain, Dizziness, Shortness of breath, Heart murmur, Death (often before age 15)
Death occuring from sickle cell anemia: -physical exertion -infection - Do to under supply of oxygen---> not enough ATP available in the cells - increased energy needs to heal the body
Created by: Jtanko23