Biochem Digging Up Bones Flashcards
DNA TO DNA
Replication
DNA TO RNA
TRANSCRIPTION
RNA TO PROTEINS
Translation
H+ acceptor
Base
H+ donor
Acid
Donates few of its H+
Weak acid
Donates almost almost all of its H+ and forms a weak conjugate
Strong acid
A solution that resists changes in its pH when acid or base are added
Buffer
The migration of water from the side of a membrane that is hypoosmotic to the side that is hyperosmotic
Osmosis
Facilitated transport of a molecule down the concentration gradient by a carrier, does not use energy
Passive transport
Facilitated transport of a molecule down the concentration gradient by a carrier, uses energy
Active transport
Types of co-transport
Symport
Antiport
Process by which matter from the outside an organism is transformed into energy or material for the organism
Metabolism
Reactions that break the bonds of complex molecules
Catabolism
Reactions which synthesize complex molecules from simpler molecules
Anabolism
Energymedium for reqctions inside the cell
ATP
Loss of electron
Oxidation
Gain of electrons
Reduction
Carbohydrate yields # kcal
4kcal/gam
Protein yields # kcal
4 kcal/gram
Alcohol yields # kcal
7kcal/gram
Fats yields # kcal
9kcal/gram
Excretory form of protein
Urea
Bacteria cqn metabolize urea to ?
Ammonia
Where is ethanol is metabolized?
Liver
Alcohol inhibits ?
Gluconeogenesis
Starch is made in these 2 sites
Liver
Muscle
It is the major energy store in the body
Fat(triacylglycerol)
2 Sources of monounsaturated fats
Olive oil
Canola oil
All plants have unsaturated fats except 2?
Coconut oil
Palm oil
Energy source utilized by muscle at rest? Active?
At rest: Fat
Active: Carbohydrates
Energy source utilized by brain?
Carbohydrates
Number of amino acids in animal metabolism
20
ESSENSTIAL AMINO ACIDS
phenylalanine, valine, tryptophan, threonine, isoleucine, methionine, Histidine, Argninine, Lysine
[PVT TIM HAL] always trys never tyrs
An amino acid with a sidechain that forms a ring with the amino group of the back bone
Proline
These amino acids are hydrophobic and bond together through hydrophobic interactions
Valine, Leucine, isoleucine
amino acids with aromatic side chains
phenylalanine, tyrosine, tryptophan
amino acids that contain sulfur
cysteine, methionine
an imino acid and forms a ring with its own backbone
proline
determine the function of the protein
side chains
nonpolar side chains, hydrophobic or hydrophilic?
hydrophobic
Polar acidic amino acids
aspartate glutamate
polar basic amino acids
histidine arginine lysine
amino acid that has an imidazole ring, offers buffering at physiologic pH to protein. decarboxylated to histamine
histidine
2 amino acids that contain hydroxyl groups which can ofrm hydrogen bonds
serine and threonine
formed by a disulfide bond joining 2 cysteine residues
cystine
keratin has many cystine
amino acid used in the first step of heme synthesis
Glycine
blood glycoproteins in diabetics contains glucose linked to this amino acid
lysine
amino acid with the largest side chain, it is hydrophobic with an aromatic ring
tyrosine
deficiency of this amino acid can cause hartnup disease and pellagra
tryptophan ( coverted to niacin)
amino acids that carries nitrogen from the periperal tissues to the liver
Alanine glutamine
amino acid disrupts the a-helix in a polypeptide
proline
this amino acid is the phosphorylation site of enzyme modification
serine
amino acid deaminated to form ammonia
glutamine
dipolar ions
zwitterion
essential amino acids
(PVT TIM HALL always trys never tyrs)
phenylalanine valine tryptophan threonine isoleucine methionine leucine lysine
relatively essential amino acids
histidine arginine
none essential amino acids
(PACT)
proline, arginine(adult) , cysteine, tyrosine
disease resulting from adequate inadequate intake of protein, but adequate intake of calories
kwashiorkor
disease resulting from inadequate intake of both calories and protein
marasmus
disease presents with unpigmented hair which appears reddish, fatty liver, edema, protruding abdomen
kwashiorkor
disease presents with retarded growth, emaciation, cachexia, but now low albumin or edema
marasmus
sequence of amino acids in a polypeptide chain
primary structure
hydrogen bonding which produces regularly repeated structures( alpha helix and b pleated sheets)
secondary structure
overall 3 dimensional shape of the protein
tertiary structure
a number of subunits with spatial arrangement
quarternary structure
Peptide bonds are formed by joining amino acids by this reaction
dehydration
Dehydration reaction that forms the peptide bond can be reversed by this reaction
hydrolysis
all peptide bonds of a polypeptide chain will be broken and the individual amino acids released in this condition
strong acid solution at 43°C(110°F) for 24 hours
amount of energy which must be added to a reaction to allow it to go forward
Gibb’s free energy of activation
rate that a reaction occurs
reaction velocity
increases the speed of a reaction by lowering the reactions energy of activation
catalysts
protein catalyst which may require a vitamin or mineral cofactor
enzyme
catalyzes reactions adding or removing nucleoside triphosphate(usally ATP)
kinase
removes H+
dehydrogenase
the substance which is recognized by the enzyme and is transformed into the product of the reaction
substrate
substance formed by the interaction of the substrate and enzyme
product
part of the enzyme which is catalytic
active site
attraction between enzyme and substrate
affinity
theory which states substrate and enzyme always fit each other
Lock and key theory
theory which states substrates and enzyme fit only at binding
induced fit theory
enzymes which have different amino acid sequences, but catalyze the same reactions
isoenzyme
An enzyme which requires a cofactor to be active
holoenzyme
protein part of a holoenzyme
apoenzyme
a cofactor which is permanently complexed with its enzyme
prosthetic group
enzyme which contains another site, different from the active site, at which an effector binds
allosteric enyme
An enzyme whose substrate is also its effector
homotrophic enzyme
an enzyme which has a different molecule as an effector
heterotrophic enzyme
enzyme which may increase or inhibit substrate binding, binding to one site can alter other sites. sigmoidal plot, as opposed to michaelis menten kinetics(hyperbolic)
allosteric enzyme
activating or inactivating regulatory enzymes
phosphorylation
activator- phosphorylase
deactivator- phosphatase
Factors that affect the rate of a reaction
substrate concentration
temperature
pH
Kinetic order: reactions where the rate is independent from substrate concentration
zero order
Kinetic order: rate is independent from substrate concentration; proportional
first order
enzymes that have a hyperbolic curve
michaelis-menten equation
this equation rearranges the michaelis-menten equation so that the line plotted is straight
lineweaver-burke plot
inhibitor is shaped similar to the substrate and temporarily competes with it for binding sites
competitive inhibition
binds temporarily to enzyme somewhere other than active site but halts catalysis
non-competitive inhibition
bind covalently to enzymes and permanently inactivates them
irreversible inhibitors
catalyze irreversible reactions and are usally the committe step in the pathway
allosteric enzyme
change in heat of reactants and products
enthalpy
change in randomness or disorder of the reactants and products
entropy
reaction occurs spontaneously when change is negative, and not spontaneous when positive
free energy
