BIO 1: Molecular Bio and Cell Resp (MCAT)

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MCAT

The 6 lipids

fatty acids, triacylglycerols, phospholipids, glycolipids, steroids, terpenes

triacylglycerol

They store metabolic energy and provide thermal insulation and padding.

glycerol

A simple polyol compound. It is a colorless, odorless, viscous liquid that is widely used in pharmaceutical formulations. It has three hydroxyl groups that are responsible for its solubility in water and its hygroscopic nature.

polyol

An alcohol containing multiple hydroxyl groups.

phospholipid

Structural components of membranes.

glycolipids

Are lipids with a carbohydrate attached.

steroids

They regulate metabolic activity.

terpenes

A large and diverse class of organic compounds, produced by a variety of plants, particularly conifers.

fatty acids

Some serve as local hormones, such as eicosanoids.

hydrogen bond

The attractive interaction of a hydrogen atom with an electronegative atom, such as nitrogen, oxygen or fluorine, that comes from another molecule or chemical group.

hydrolysis

The process of splitting a compound into fragments with the addition of water; a kind of reaction that is used to break down polymers into simpler units, e.g. starch into glucose.

amphipathic

Of, or relating to, a molecule having hydrophobic and hydrophilic regions.

Van der Waals forces

The attraction or repulsion of forces because of already created or quickly induced dipoles.

protein

A molecule composed of polymers of amino acids joined together by peptide bonds. It can be distinguished from fats and carbohydrates by containing nitrogen.

amino acid

The building block of protein in which each is coded for by a codon and linked together through peptide bonds. Has NH2 and COOH in it.

peptide bond

The covalent bond joining amino acids, particularly at the carboxyl group of one amino acid to the amino group of the other amino acid, with the concomitant release of a molecule of water.

polypeptide

Other name for proteins.

10

How many amino acids are essential to humans?

essential

_____ amino acids are ones that must be ingested because the body can't make them.

side chains

Amino acids differ in this structurally. They are also called R groups.

primary structure

Sequence of amino acids in a polypeptide.

secondary structure

Deal with the conformation of a protein and may be an α-helix or a β-pleated sheet.

tertiary structure

The 3D structure that may arise from large proteins when they clump together onto themselves.

quarternary structure

When two or more polypeptide chains bind together.

denatured

When the conformation of a protein is disrupted. If the agent that does this is removed, it can go back to normal.

globular, structural

Two types of proteins?

collagen

Most abundant protein in the body and is a a structural protein.

proteoglycan

Mixture of proteins and carbohydrates that is mostly carbohydrates.

cytochrome

A class of hemoprotein found in mitochondria that transport electron or protons.

conjugated

Proteins with nonproteinaceous components are called _______ proteins.

glucose

The most commonly occuring six-carbon carbohydrate.

anomer

Stereoisomers of a sugar which differ only in how they are configured about their respective carbonyl (anomeric) carbon atom.

animals

In glucose, ____ break alpha linkages.

bacteria

In glucose, ____ break beta linkages.

glucose

Plants make starch and cellulose from what?

amylose, amylopectin

Starch comes in these two forms.

isomer

Amylose is an ____ of cellulose.

isomer

One of two or more molecules that have the same chemical formula but have a different stereochemical arrangement of their atoms.

animals, bacteria

____ digest glycogen, ____ digest cellulose.

nucleotide

Made of a five-carbon sugar; a nitrogenous base; and a phosphate group.

nitrogenous bases

Adenine, guanosine, cytosine, thymine, and uracil.

phospholipid bonds

The bonds that hold nucleic acids together to make DNA and RNA.

third

Phospholipid bond is made from the phosphate group of one nucleotide and the __ carbon of the pentose on the other nucleotide.

adenine

What binds with thymine?

thymine

What binds with adenine?

cytosine

What binds with guanine?

guanine

What binds with cytosine?

top

The (top/bottom) strands runs 5'->3'.

bottom

The (top/bottom) strands runs 3'->5'.

uracil

What replaces thymine in RNA?

nucleotide

ATP is a (protein/carbohydrate/nucleotide/lipid).

cyclic AMP

Abbreviation for cyclic adenosine monophosphate, a second messenger essential in many biological processes of various organisms.

minerals

The dissolved inorganic ions inside and outside the cell. They can also assist as cofactors.

cofactor

An inorganic complement of an enzyme reaction, usually a metal ion.

enzyme

Globular proteins that act as a catalyst, lowering the energy of activation for reactions to increase the rate of reaction.

no

Are enzymes consumed in a reaction?

no

Do enzymes alter equilibrium of a reaction?

substrate

Reactant which enzyme uses.

active site

Place where substrate bonds to enzyme.

enzyme specificity

When an enzyme is made for a certain substrate that fits in a certain way.

induced fit

When the enzyme and substrate alter their shape a little to fit together.

saturation kinetics

As more substrate is added, the rate of a reaction increases, but it starts to level off at some point.

yes

Does temperature affect reaction rate?

yes

Does pH affect reaction rate?

37

What is the degrees Celcius for the best temperature for enzymatic reactions.

metal ions

Cofactors can be coenzymes or ______.

vitamins

Many coenzymes are _____ or their derivatives.

competitive, irreversible, noncompetitive

The three types of enzymatic inhibition are?

competitive inhibition

Something blocks the substrate at the active site from binding to the enzyme. This is reversible.

noncompetitive inhibition

It changes the conformation of the enzyme so that the substrate can't bind to the enzyme's active site.

irreversible inhibition

When something blocks the enzyme's ability to function by binding to it. Not reversible.

enzymes

Proteolytic cleavage, reversible covalent modification, control proteins, and allosteric interactions. What do these four regulate?

zymogen

Inactive form of an enzyme.

proenzyme

Inactive form of an enzyme.

cleavage of peptides

A zymogen/proenzyme is activated by ___ _ ___.

-ogen

Suffix for a proenzyme/zymogen?

yes

Are some enzymes activated or deactivated by phosphorylation?

control proteins

These are protein subunits that activate or inhibit enzymes, like G-proteins.

allosteric regulation

The modification of an enzyme configuration resulting from the binding of an activator or inhibitor at a specific binding site on the enzyme.

negative feedback

When the creation of end product stops the reaction from going on.

positive feedback

When the creation of end products makes it make more product.

positive cooperativity

When a substrate binds to an enzyme, making it easier to bind with more substrate.

negative cooperativity

When a substrate binds to an enzyme, making more substrate harder to bind to the enzyme.

-ase

Suffix for an enzyme?

kinase

A (kinase/phosphatase) is an enzyme that phosphorylates something.

phosphotase

A (kinase/phosphatase) is an enzyme that dephosphorylates something.

ligand

An ion or molecule that binds to a central metal atom to form a coordination complex.

metabolism

All cellular chemical reactions.

anabolism

Molecular synthesis.

catabolism

Molecular degradation.

three parts of metabolism

1) Macromolecule catabolism, 2) Oxidized to acetyl CoA, pyruvate, other metabolites, 3) If oxygen available, mixes with metabolites to citric acid cycleto make energy.

respiration

Energy-aquiring stage in the metabolism.

aerobic, anaerobic

2 types of respiration?

anaerobic resipration

Respiration where oxygen is not needed.

glycolisys

First stage of anaerobic and aerobic respiration. Breaks 6-carbon glucose molecule to 2 3-carbon molecules of pyruvate.

pyruvic acid

Pyruvate conjugate?

yes

Does glycolysis act where there is and isn't oxygen?

cytosol

Where does glycolysis occur?

no

Can phosphorylated molecules go through the membrane?

substrate level phosphorylation

The 3-carbon molecules in respiration give up one phosphate to make ADP into ATP.

mono

Fructose and glucose are ___-saccharides.

2, 4

In respiration, _ ATP are spent and _ ATP are made.

glucose

Galactose can be converted to ____ to then be used in respiration.

fermentation

A name for anaerobic respiration.

lactic

Fermentation has glycolysis and the ____ acid cycle.

NADH, pyruvate

Fermentation occurs with the lack of oxygen or when there isn't enough ____ and ____.

NAD+

Fermentation turns NADH into ____.

aerobic respiration

Respiration that requires oxygen.

matrix of a mitochondrion

If anaerobic respiration is possible, glycolysis product goes to ___.

inner

Which part of the mitochondrion is less permeable? Inner or outer?

acetyl CoA

When pyruvate is inside the matrix of the mitochondrion, it is turned into ____, and CO2 is released.

coenzyme

Is acetyl CoA an enzyme or coenzyme?

1 ATP, 1 FADH2, 3NADH

Krebs cycle makes ___, ____, and ___, and is called substrate-level phosphorylation.

electron transport chain

This couples electron transfer between an electron donor (such as NADH) and an electron acceptor (such as O2) with the transfer of H+ ions (protons) across a membrane. The resulting electrochemical proton gradient is used to generate chemical energy in the form of adenosine triphosphate (ATP).

mitochondria

Where is the electron transport chain?

oxygen

Electrons go down the ETC to be accepted by ____.

protons

As electrons are passed down the ETC, ____ are pumped into the membrane.

proton-motive force

The energy that is generated by the transfer of protons or electrons across an energy-transducing membrane and that can be used for chemical, osmotic, or mechanical work.

ATP synthase

An enzyme that catalyzes the formation of ATP from the phosphorylation of ADP with inorganic phosphate, using a form of energy, such as the energy from a proton gradient.

2

Net ATP production from fermentation?

oxidative phosphorylation

A metabolic pathway that generates ATP from ADP through phosphorylation that derives the energy from the oxidation of nutrients.

products

____ of respiration: oxygen + CO2 + H2O

reactant

____ of respiration: glucose

combustion

What kind of reaction is respiration?

36

How many ATP made in aerobic respiration?

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