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MCAT - Biology 1 - 1

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Section 1

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Carbohydrate formula

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Date created

Mar 1, 2020

Cards (100)

Section 1

(50 cards)

Carbohydrate formula

Front

Cn(H2O)n Composed of: Carbon, Hydrogen, Oxygen; Most C are linked to H and OH;

Back

saturated fatty acid

Front

A fatty acid in which all carbons in the hydrocarbon tail are connected by single bonds, thus maximizing the number of hydrogen atoms that can attach to the carbon skeleton.

Back

Steroids

Front

lipids characterized by a carbon skeleton consisting of four fused rings

Back

VLDL (very low density lipoprotein)

Front

the type of lipoprotein made primarily by liver cells to transport lipids to various tissues in the body; composed primarily of triglycerides.

Back

Carbohydrates

Front

the starches and sugars present in foods

Back

Hexoses

Front

6 carbon sugars

Back

tertiary protein structure

Front

occurs when certain attractions are present between alpha helices and pleated sheets

Back

Prostaglandins

Front

A group of bioactive, hormone-like chemicals derived from fatty acids that have a wide variety of biological effects including roles in inflammation, platelet aggregation, vascular smooth muscle dilation and constriction, cell growth, protection of from acid in the stomach, and many more.

Back

amylose and amylopectin

Front

both are starches alpha 1,4 and alpha 1,6 linkages

Back

phosphodiester bond

Front

the type of bond that links the nucleotides in DNA or RNA. joins the phosphate group of one nucleotide to the hydroxyl group on the sugar of another nucleotide

Back

Sphingolipids

Front

Lipids with a sphingosine backbone: ceramide, sphingomyelins, glycosphingolipids, gangliosides

Back

For glucose polymers, only bacteria break ______ linkages

Front

beta

Back

Phospholipids

Front

A molecule that is a constituent of the inner bilayer of biological membranes, having a polar, hydrophilic head and a nonpolar, hydrophobic tail.

Back

Nucleic acids

Front

polymers of nucleotides

Back

unsaturated fatty acid

Front

A fatty acid possessing one or more double bonds between the carbons in the hydrocarbon tail. Such bonding reduces the number of hydrogen atoms attached to the carbon skeleton.

Back

Nucleotides are written

Front

5' to 3'

Back

Glucose

Front

the form of sugar that circulates in the blood and provides the major source of energy for body tissues. When its level is low, we feel hunger.

Back

primary protein structure

Front

sequence of a chain of amino acids

Back

alpha linked polysaccharides

Front

starch and glycogen, common energy storage molecules the opposite side (1 carbon -OH)

Back

Hydrolysis

Front

Breaking down complex molecules by the chemical addition of water

Back

complementary strands

Front

relation between two nucleotide strands of DNA in which each purine on one strand pairs with a specific pyrimidine on the opposite strand - A and T; C and G

Back

major functions of lipids

Front

-phospholipids as a structural component of membranes -triacylglycerols store metabolic energy and provide thermal insulation and padding -steroids regulate metabolic activities -some fatty acids (eicosanoids) as local hormones

Back

Monosaccharides

Front

Single sugar molecules

Back

Starch

Front

A storage polysaccharide in plants consisting entirely of glucose.

Back

Lipoproteins

Front

clusters of lipids associated with proteins that serve as transport vehicles for lipids in the lymph and blood

Back

secondary protein structure

Front

hydrogen bonding of the peptide backbone causes the amino acids to fold into a repeating pattern

Back

waxes

Front

A type of lipid molecule consisting of one fatty acid linked to an alcohol; functions as a waterproof coating on many biological surfaces such as apples and other fruits.

Back

amide bond

Front

Between carboxylic acids and amines. Important peptide bonds that build proteins from amino acids.

Back

Adipocytes

Front

fat cells that store triglycerides

Back

Hydrophilic

Front

Having an affinity for water.

Back

HDL cholesterol

Front

good. high density lipoprotein. high protein, low fat

Back

Pyrimidines

Front

cytosine and thymine (uracil in RNA)

Back

Purines

Front

Adenine and Guanine Bases with a double-ring structure.

Back

Cellulose

Front

A substance (made of sugars) that is common in the cell walls of many organisms; uses beta linkages (unable to be digested by humans)

Back

Four nitrogenous bases in DNA

Front

Adenine, Thymine, Cytosine, Guanine

Back

Five forces contribute to the tertiary structure are

Front

- Covalent disulfide bonds between two cysteine amino acids - electrostatic ion interactions - hydrogen bonds - Van der Waals forces - hydrophobic side chains (hydrophobic bonding)

Back

Triacylglycerols (triglycerides)

Front

Preferred method of storing energy for long term use. Contain: 1) One glycerol attached to three fatty acids via ester bonds. The FA usually vary within the three tails 2) Can have saturated or unsaturated FA tails.

Back

How many hydrogen bonds are between C and G?

Front

3 hydrogen bonds

Back

Glycolipids

Front

a lipid with one or more covalently attached carbohydrates

Back

Polysaccharides

Front

Carbohydrates that are made up of more than two monosaccharides

Back

How many hydrogen bonds are between A and T?

Front

two

Back

nucleoside

Front

nitrogenous base + sugar

Back

Differences between DNA and RNA

Front

RNA contains uracil DNA contains thymine DNA has double helix RNA has a single helix

Back

phosphatids

Front

type of phosphoglyceride that have glycerol backbone with phosphate group attached

Back

Nucleotides

Front

Basic units of DNA molecule, composed of a 5 carbon sugar, a phosphate, and one of 4 DNA bases

Back

For glucose polymers, animals eat ______ linkages

Front

alpha

Back

fatty acids

Front

unbranched carbon chains that make up most lipids

Back

beta linked polysaccharides

Front

cellulose same side (1 carbon -OH)

Back

Hydrophobic

Front

Having an aversion to water; tending to coalesce and form droplets in water.

Back

LDL cholesterol

Front

bad. low density lipoprotein. low protein, high fat

Back

Section 2

(50 cards)

if enzyme substrate affinity decreases, Km....

Front

increases

Back

Ligases

Front

catalyze the formation of bonds with the input of ATP and the removal of water

Back

What amino acid disrupts alpha-helix and beta-pleated sheet formation?

Front

proline --> creates kink

Back

saturation kinetics (enzymes)

Front

as [substrate] increases, rxn rate also increases until max

Back

Km

Front

Substrate concentration at 1/2 Vmax

Back

cofactors and coenzymes

Front

-non protein, small molecules that can bind to the active site of an enzyme and participate in catalyzing the reaction (use ionization, protonation, deprotonation) -cofactors: usually inorganic molecules or metal ions -coenzymes: small organic groups such as vitamins or NAD, FAD, CoA

Back

What affects enzyme activity?

Front

pH and temperature

Back

competitive inhibitors

Front

Reduce the productivity of enzymes by blocking substrates from entering active sites. raise the apparent Km but do not change Vmax in the presence of a competitive inhibitor the rate of the reaction can be increased to the original uninhibited Vmax by increasing the concentration of the substrate

Back

Transferases

Front

transfer functional groups from one substrate to another

Back

non-competitive inhibition

Front

a type of enzyme inhibition where the inhibitor reduces the activity of the enzyme and binds equally well to the enzyme whether or not it has already bound the substrate. unlike competitive inhibitors they cannot be overcome by excess substrates so they lower Vmax. Km remains the same as they do not lower the enzymes affinity for the substrate

Back

if enzyme substrate affinity increases, Km...

Front

decreases

Back

zymogen

Front

An inactive precursor of an enzyme, activated by various methods (acid hydrolysis, cleavage by another enzyme, etc.)

Back

Oxidoreductases

Front

catalyze oxidation-reduction reactions that involve the transfer of electrons

Back

allosteric regulation

Front

The binding of a regulatory molecule to a protein at one site that affects the function of the protein at a different site.

Back

positive feedback

Front

Feedback that tends to magnify a process or increase its output.

Back

Hydrolases

Front

cleave bonds on molecules with the addition of water

Back

irreversible inhibitors

Front

chemically and covalently bind to active site; rendering it permanently inactive

Back

enzyme suffix

Front

-ase

Back

enzyme-substrate complex

Front

A temporary complex formed when an enzyme binds to its substrate molecule(s). inversely proportional to Km

Back

Kinase

Front

an enzyme that catalyzes the transfer of a phosphate group from ATP to a specified molecule.

Back

allosteric inhibition

Front

the mechanism for inhibiting enzyme action in which a regulatory molecule binds to a second site (not the active site) and initiates a conformation change in the active site, preventing binding with the substrate

Back

enzyme specificity

Front

the concept that each enzyme catalyzes only one kind of reaction.

Back

Vmax

Front

maximum initial velocity or rate of an enzyme-catalysed reaction.

Back

Enzymes

Front

Proteins that speed up chemical reactions

Back

Lipolysis

Front

breakdown of fat

Back

mixed inhibitors

Front

binded the site on the enzyme other than the active site and thus do not prevent the substrate from binding. they can bind to either the enzyme alone or the enzyme substrate complex. they act like competitive inhibitors by binding primarily to the enzyme before the substrate is associated increasing Km. I'll mix inhibitors lower vmax to some extent

Back

structural proteins function as

Front

maintain and add strength to cellular matrix and structure (collagen is the main one - most abundant protein in the body - add strength to ligaments, skin, tendons, and bone)

Back

solvation layer

Front

surrounding molecules that force hydrophobic R groups on proteins towards inner area

Back

disulfide bonds

Front

Strong chemical side bonds formed when the sulfur atoms in two adjacent protein chains are joined together.

Back

Holoenzyme

Front

enzyme with its cofactor

Back

carbohydrate suffix

Front

-ose

Back

negative cooperativity

Front

a cooperative effect whereby binding of the first ligand to an enzyme or protein causes the affinity for the next ligand to be lower

Back

allosteric activator

Front

Allosteric activators bind to an enzyme and induce its active form.

Back

Phosphatase enzymes

Front

remove phosphate groups

Back

Isomerases

Front

catalyzes the rearrangement of bonds within a single molecule

Back

Enzymes are regulated by...

Front

1. proteolytic cleavage 2. reversible covalent modification 3. control proteins 4. allosteric iteractions

Back

positive cooperativity

Front

the first substrate changes the shape of the enzyme allowing other substrates to bind more easily

Back

negative feedback

Front

A primary mechanism of homeostasis, whereby a change in a physiological variable that is being monitored triggers a response that counteracts the initial fluctuation.

Back

uncompetitive inhibitors

Front

Bind only to E-S complex - basically lock S in the enzyme, preventing release Must bind allosteric site vmax and Km decrease

Back

Coenzymes

Front

An organic molecule that is a necessary participant in some enzymatic reactions; helps catalysis by donating or accepting electrons or functional groups; e.g., a vitamin, ATP, NAD+.

Back

six categories of enzymes

Front

1. Oxidoreductases: catalyze oxidation reactions, such as the conversion of alcohol 2. Transferases: enzymes that catalyze the transfer of a group of atoms, referred to as a radical, from one molecule to another, such as the transfer of amino groups 3. Hydrolases: catalyze the reaction of a chemical with water 4. Lyases: catalyze reactions producing or resulting in double bonds, for example, conversion of sugars 5. Isomerases: catalyze the transfer of groups on the same molecule, resulting in a new structure for the molecule 6. Ligases: enzymes catalyze the joining of molecules to form larger molecules

Back

Substrate

Front

A specific reactant acted upon by an enzyme

Back

Lyases

Front

addition of groups to double bonds, or formation of double bonds by removal of groups

Back

induced fit model

Front

substrate binding to an active site improves the fit between the two

Back

Globular proteins function as

Front

enzymes, hormones, membrane pumps and channels, membrane receptors, intercellular and intracellular transport and storage, osmotic regulators, antibodies, and more (globular proteins are functional)

Back

Apoenzyme

Front

enzyme without its cofactor

Back

Michaelis constant

Front

A constant, Km, that is a measure of the kinetics of an enzyme reaction and that is equivalent to the concentration of substrate at which the reaction takes place at one half its maximum rate, 1/2 Vmax

Back

Two types of proteins

Front

globular and structural

Back

types of enzyme inhibition

Front

Competitive, non-competitive, I'm competitive, irreversible, mixed

Back

Minerals

Front

Elements found in food that are used by the body

Back