Biochemistry I Exam II Flashcards

12111398237	Proteins	What is the most abundant biomolecule in the body?	0
12111416769	Glycine	What is the only amino acid that lacks a chiral center?	1
12111422268	C-terminal	What part of the amino acid contains a carboxylic acid?	2
12111427364	N-terminal	What part of the amino acid contains an amine group?	3
12111435971	L-chiral	What type of chirality has a CRN clockwise arrangement?	4
12111451559	D-chiral	What type of chirality has a CRN counterclockwise arrangement?	5
12111458271	Racemic	If the chiral center is a 50-50 mixture of L and D it is referred to as what?	6
12111468811	L-chiral	Alanine has what chirality?	7
12111479144	Alanine	Which amino acid functions to make new glucose? (Gluconeogenesis)	8
12111530151	Aliphatic	What is the term for an R group that contains a hydrocarbon?	9
12111564989	Leucine	Which amino acid is metabolized into the cholesterol precursor HMG CoA?	10
12111583033	Valine	Which amino acid is responsible for the improper folding of red blood cells?	11
12111588839	Hemoglobin	Valine replaces glutamate and causes improper folding in what structure of a red blood cell?	12
12111601438	Maple Syrup Urine Disease	What disorder occurs when infants are unable to metabolize branched chain amino acids?	13
12111620655	Sickle cell anemia	What genetic mutation occurred in order to prevent malaria, but causes improper folding of RBC's?	14
12111640071	Methionine	Which amino acid contains a sulfur and is a precursor for a very import myelinating molecule?	15
12111652511	Proline	Which amino acid disrupts a-helix and B-pleated sheet formations in secondary structure folding of proteins?	16
12111676928	Phenylalanine	Which amino acid is a precursor for tyrosine?	17
12111683899	Phenylketonuria (PKU)	What disorder is a result of decreased metabolism for the amino acid phenylalanine?	18
12111698380	Tryptophan	Which amino acid is a precursor for serotonin, melatonin, and niacin?	19
12111705402	Tyrosine	Which amino acid is a precursor for thyroxine and is very important to the beginning pathways of cell signaling? I.e- RTK pathways	20
12111725109	Very low protein	What should someone with PKU ingest in their diet?	21
12111731353	Cystic Fibrosis	What is the most common genetic disorder?	22
12111749106	Serine and threonine	Which amino acids main function is to H bond to other molecules in protein regulation pathways?	23
12111766687	Cysteine	Which amino acid contains a thiol (SH group) that acts as an antioxidant?	24
12111780794	Glutamine	Which amino acid is the main nitrogen carrier and is primarily synthesized in the brain?	25
12111795037	Histimine	What molecule is important for its buffering capacity in hemoglobin?	26
12111835933	Hydroxylysine	Which amino acid derivative is found in collagen?	27
12111841904	Isoelectric point	When are amino acids least soluble?	28
12111852917	pK1	Which pK is a measure of the dissociation of the carboxylic acid group (C-terminal) on an AA?	29
12111865757	pK2	Which pK is referring to the amine group of an AA?	30
12111871070	pKR	Which pK is referring to the dissociation of protons from the R group on an amino acid?	31
12111886957	Zwitterion	What is the term that describes the net neutrality of an amino acid?	32
12111903668	Isoelectric point (pI)	What is the point where an AA or protein is a zwitterion (neutral)?	33
12111911098	net positive	What is the charge when pH	34
12111919626	Net negative	What is the charge when pH>pI?	35
12112091397	Dehydration reactions	What type of reaction is involved in the synthesis of ALL macronutrients?	36
12112119951	Glutathione	What is the smallest peptide?	37
12112124426	pKR	Which pK group is the most important group for buffers?	38
12112134821	Conjugated proteins	What is a protein that has chemical constituents? i.e- glycoproteins and metalloproteins	39
12112155246	Conformation	What is the spatial arrangement of atoms within a protein?	40
12112159237	Native conformation	What is it called when a protein is in its most stable, functional conformation?	41
12112198692	Hydrophobic	What type of amino acids are buried in the middle of a structure, away from water?	42
12112208272	Primary	What level of protein structure is just the order in which amino acids are aligned?	43
12112222295	Secondary	What level of structure contains a-helix, B-sheets, and B-turns?	44
12112244829	Beta turns	What reverses the direction of polypeptides from parallel to anti-parallel?	45
12112280593	Quaternary	What level of structure consists of two or more polypeptide strands that fold over and bond by non-covalent interactions? i.e- hemoglobin	46
12112295575	Primary and tertiary	Which levels of structure use covalent (true) bonds?	47
12112303110	Four	How many different polypeptide strands make up hemoglobin?	48
12112310608	Fibrous	What type of protein contains a single secondary structure, and functions to provide support?	49
12112319463	Globular	What type of proteins have several secondary structures and make up enzymes?	50
12112336039	Glycine	What AA does collagen have the most of?	51
12112344264	Triple helix	What type of structure is collagen?	52
12112348972	Scurvy	What disorder occurs from a lack of vitamin C?	53
12112355337	Vitamin C	What is required for hydroxylation of proline and lysine in collagen synthesis?	54
12112374068	Posttranslational modification	What is the term that describes the addition of a functional group after the protein is synthesized?	55
12112388002	Proline hydroxylase and lysyl hydroxylase	What requires vitamin C to add a hydroxyl group to proline and lysine?	56
12112420064	Lysyl oxidase	What compound deaminates lysine and forms a reactive aldehyde?	57
12112427164	Copper (Cu)	What is lysyl oxidase dependent upon?	58
12112436447	Matrix metalloproteins (MMP's)	What degrades collagen?	59
12112452166	Motif	What pattern of folding is not inherently stable?	60
12112455830	Domain	What is the part of a polypeptide chain that is independently stable?	61
12112501064	Entropy (S)	As a protein is folded what decreases?	62
12112529158	Chaperones	What are the molecules that assist in the folding of proteins?	63
12112563003	Degraded or accumulated	What happens to a protein if it misfolds?	64
12112579913	Proteostasis	What process controls protein synthesis, folding, refolding, and degradation of proteins?	65
12112647689	Globular proteins	What type of proteins are easily denatured?	66
12112657438	intrinsically unstructured proteins (IUPs)	What is a protein that has no specific structure on at least part of it?	67
12112666903	Signaling pathways	What are IUP's important for?	68
12112678124	Metamorphic proteins	What are proteins that are able to form multiple structures that all have different functions?	69
12112729253	Ligand	What are molecules that are reversibly bound by a protein?	70
12112740343	Induced fit	What is the structural adaptation of a protein in which a conformational change occurs for the the binding of a ligand?	71
12112759677	One	How many oxygens can myoglobin carry?	72
12112763504	Four	How many oxygens can hemoglobin carry?	73
12112771735	One	If a protein has one polypeptide strand (heme), how many oxygens can it carry?	74
12112789336	Relaxed	If a hemoglobin is acting as oxyhemoglobin and has a high affinity for binding oxygen, it is in which state?	75
12112835450	Tense	If a hemoglobin is acting as deoxyhemoglobin and has a low affinity for binding oxygen, it is in what state?	76
12112849693	Cooperative binding	What term describes the ability of oxygen to bind as more oxygen binds in a hemoglobin?	77
12112864565	High and easy	What is the affinity for oxygen to bind to a hemoglobin if the hemoglobin already has three O2 bound? How difficult will it be for the last oxygen to bind?	78
12112953203	Allosteric	If interactions of compounds affect the ability of heme groups to bind oxygen, it is said to be what?	79
12112983534	Deoxyhemoglobin (tense)	A decrease in pH shifts the hemoglobin towards what state?	80
12112988049	Oxyhemoglobin (relaxed)	An increase in pH shifts the hemoglobin towards what state?	81
12113032371	Low affinity	Is affinity for oxygen high or low in peripheral tissues?	82
12113050641	Carbon monoxide (CO)	What has a 250 times higher affinity to bind to iron in hemes than oxygen?	83
12113073308	Doesn't allow for release of O2 in tissues	What effect does CO have on the oxygen in hemoglobin?	84
12113084056	Hemolytic and obstructive	What are the types of jaundice?	85
12113105859	Hemolytic	Wha type of jaundice has high levels of unconjugated bilirubin?	86
12113115769	Obstructive	What type of jaundice is able to excreted in the kidneys and has high levels of conjugated bilirubin?	87
12113148859	IgG	What class of immunoglobulins is most common?	88
12113152095	IgA	What class of immunoglobulins is found in secretions (tears, saliva, breastmilk)?	89
12113157096	IgE	What immunoglobulin is the main antibody produced in response to food allergies?	90
12113167194	IgM	What immunoglobulin is the first antibody produced during an immune response?	91
12113697907	Speed up reactions	What is the primary function of an enzyme?	92
12113702873	No	Are enzymes consumed in a reaction?	93
12113706239	Cofactor	What is the inorganic component of an enzyme?	94
12113709064	Coenzyme	What is the organic component of an enzyme?	95
12113723612	Vitamins	What are often used as coenzymes ?	96
12113739639	Apoenzyme	What is the protein part of an enzyme?	97
12113758803	Holoenzyme	What is the complete, active enzyme called? (The "whole" enzyme)	98
12113773766	Zymogen	What is the inactive enzyme precursor called?	99
12113782312	End in "-ogen" or begin with "pro"	How do you distinguish an inactive enzyme from an active one?	100
12113800619	Oxidoreductase	What class of enzymes involves the addition or removal of H+? REQUIRES NAD+ or FAD	101
12113816026	Transferase	What class of enzymes involves the transfer of a functional group? Will often involve ATP, ending with a phosphate being bound to the product	102
12113829485	Two	How many reactants and products will be involved in transferase?	103
12113840816	Isomerase	What class of enzymes rearrange functional groups on one molecule? Only involves one reactant and one product	104
12113853237	Hydrolase	What class of enzymes causes hydrolysis to break bonds? Water is a reactant.	105
12113859983	Lyase	What class of enzymes cleaves C-C, C-S, or C-N bonds ?	106
12113868736	Ligase	What class of enzymes is the only class that involves the formation of bonds, and typically uses ATP, but results in a free phosphate group?	107
12113988606	Active site	What is the part of an enzyme that contains a binding site and a catalytic site?	108
12114023448	induced fit	Which active site model is the most common and allows for the enzyme to "mold" into a form where the substrate can bind?	109
12114045305	Binding energy	What is the energy released through the formation of weak bonds in the active site?	110
12114078828	KM	What is equal to one half of V Max?	111
12156291279	Vo is dependent on [S]	What happens if [S]<	112
12156302631	Vo is dependent on both [E] and [S]	What happens if [S]>Km?	113
12156316490	Vo is dependent on [E], enzyme is saturated with S	What happens if [S]>>Km	114
12156346340	1/Vmax	What is the y-intercept of a line weaver burke plot?	115
12156355463	-1/Km	What does the x-intercept of a Lineweaver-Burk plot represent?	116
12156363077	Km/Vmax	What is the slope of a lineweaver burke plot?	117
12156387957	The number will be bigger	What will happen if the line is closer to the origin of a lineweaver burke plot?	118
12156404528	[E]	What does velocity of enzyme and substrate reactions depend on?	119
12156415599	Decrease enzyme activity	What happens if there is a deficiency in vitamins or minerals?	120
12156426734	Increase in rate	What happens to the enzyme if there is an increase in temperature?	121
12156445214	pH 1.5	What is the optimum pH of pepsin?	122
12156449814	pH 6.2	What is the optimum pH of sucrase?	123
12156452882	pH 6	Wha tis the optimum pH of polyphenol oxidase?	124
12156463340	Denaturation of the enzyme	What will extreme temperatures and pH do to the enzyme?	125
12156475563	Covalent bonds	What type of bond is in irreversible inhibitor reactions?	126
12156480612	Noncovalent bonds	What kind of bond is in reversible inhibitor reactions?	127
12156494344	Active site	Where will a competitive inhibitor bind to?	128
12156505301	Increased Km and no change in Vmax	What effect does a competitive inhibitor have on Km and Vmax?	129
12156530563	Only binds the complex	What will an uncompetitive inhibitor bind to?	130
12156541814	Decreases Km and decreases Vmax	What effect does the uncompetitive inhibitor have on the Km and Vmax?	131
12156569456	Active site or complex	What will the noncompetitive inhibitor bind to?	132
12156580157	Decreases Vmax and doesn't change Km	What is the effect of the noncompetitive inhibitor on Km and Vmax?	133