Unit 1 Flashcards by Avery W

What are the biological atoms?

Sulfur, Phosphorus, Oxygen, Nitrogen, Carbon and Hydrogen

How well did you know this?

Not at all

Perfectly

What is a macro-molecule?

a large complex structure

How well did you know this?

Not at all

Perfectly

What is a polymer?

chain of repeating smaller subunits linked by covalent bonds

How well did you know this?

Not at all

Perfectly

What are the 4 types of macro-molecules?

Proteins, Carbohydrates, Lipids, Nucleic Acids

How well did you know this?

Not at all

Perfectly

What is a carbohydrate?

biological macromolecule that always has carbon, hydrogen and oxygen in a 1:2:1 ratio. Also has a high number of hydroxyl groups to allow for energy storage

How well did you know this?

Not at all

Perfectly

What is starch used for?

short term energy storage in plants

How well did you know this?

Not at all

Perfectly

What is glycogen used for?

short term energy in animals and an be broken down for energy faster than starch

How well did you know this?

Not at all

Perfectly

What is cellulose used for?

provides structural support in plants

How well did you know this?

Not at all

Perfectly

What is a lipid?

biological macromolecule with high proportions of non-polar CH bonds and they are hydrophobic whch plays a key role in determining their function

How well did you know this?

Not at all

Perfectly

Why are lipids good for long term energy storage? Why not?

they have many CH bonds which can store energy longer but they are also less accessible so are used after carbohydrates.

How well did you know this?

Not at all

Perfectly

How are lipids used in humans?

insulation, protection for major organs, in cell membranes

How well did you know this?

Not at all

Perfectly

What are the main structural features of a carbohydrate?

lots of OH (hydroxyl) groups

- carbon, hydrogen and oxygen occur in 1:2:1 ratio

How well did you know this?

Not at all

Perfectly

What are the main structural features of a lipid?

have long tails with many carbons
have ester bond and a double bonded oxygen
has a head and tail ends (usually)

How well did you know this?

Not at all

Perfectly

What is a triglyceride?

lipid molecule made of glycerol molecule and 3 fatty acids linked by ester bonds

How well did you know this?

Not at all

Perfectly

What is a fatty acid?

a hydrocarbon chain ending in a carboxyl group (COOH)

- can be saturated (all single bonds) or unsaturated (1+ double bonds)

How well did you know this?

Not at all

Perfectly

What is monounsaturated?

one double bond

How well did you know this?

Not at all

Perfectly

What is polyunstaurated?

2 or more double bonds. Humans cannot sythesize this so it is necessary in our diets.

How well did you know this?

Not at all

Perfectly

What is a phospholipid?

composed of a glycerol molecule bonded to 2 fatty acids and a phosphate group with an R group.

How well did you know this?

Not at all

Perfectly

What are phospholipids commonly found in?

they make up the cell membrane

How well did you know this?

Not at all

Perfectly

What is so important about the head and the tail of a phospholipid?

the head is polar and hydrophillic and the tail is non-polar and hydrophobic. This is important in forming the phospholipid bilayer.

How well did you know this?

Not at all

Perfectly

What is the phospholipid bilayer?

structure with heads of phospholipid toward aqueous envirronment in cells cytoplasm and extracellular fluid and tails toward centre interacting with each other

What are some other lipids?

Cholesterol, Steroids, Waxes

What is a protein?

has an amino group and carboxyl functional group and an R group that determines the amino acid

What are the main structural features of a protein?

amino group (look for the nitrogen)
has an R group
has a carboxyl group (carbon with both a double bonded oxygen and hydroxyl group)

What are the 6 functions of proteins?

1. catalyze chemical reactions 2. structural support 3. Transportation 4. Movement (muscle tissue) 5. Regulation (hormones) 6. Disease Defence (anitbodies made by immune system)

What is the general structure of a protein?

- long chains of amino acids | - unique sequence of amino aacids

What are the 4 levels of protein organization?

1. Primary 2. Secondary 3. Tertiary 4. Quaternary

What is denaturation?

conformational change to a protein that can cause permenant or temporary changes and may cause the protein to lose its functional ability under certain circumstances

What are the conditions for denaturation?

Temperature, pH and ionic concentrations

What is a nucleic acid?

organic compound that carries hereditary information in cells and is composed of nucleotide monomers

What are the main structural features of a nucleic acid?

- has phosphodiester bonds - has backbone made of alternating sugar-phosphate-sugar-phosphate chains - middle is made of nitrogenous bases held by hydrogen bonds

What are the 4 types of biochemical reactions?

neutralization, redox, condensation/dehydration synthesis, hydrolysis

What Dehydration Synthesis?

joins monomers together to create polymers, H+OH= water. WATER IS A PRODUCT

What is Hydrolysis?

breaks down polymers into monomers with addition of water. Hydrogen goes to one monomer and hydroxyl group goes to the other WATER IS A REACTANT

What is an enzyme?

biological catalyst that speeds up reactions by decreasing activation energy. Usually end in "ase"

What is activation energy?

the energy required to break bonds

What is a substrate?

the molecule which is catalyzed by an enzyme. It attaches to the enzyme at the active site

What is the active site?

where substrate binds and shape is a perfect match

What is the enzyme-substrate complex?

when the substrate and the enzyme come together

What is the induced fit model?

as a substrate approaches an active site, interactions between functional groups causes the protein to alter its shape to fit the substrate

What is a coenzyme?

organic, assists enzymes, ex. vitamins

What is a cofactor?

mineral or metal ions ex. iron, zinc, sodium

What are the factors that affect enzyme activity?

Temperature and pH level

How does temperature affect enzyme activity?

there is an optimum range that is relative to the organisms environment where certain enzymes can work and when they cannot

How does pH affect enzyme activity?

there is an optimum range where enzymes work best at specific pH levels. Ex. pepsin in the stomach only wors at a pH of 2

What 2 ways can you regulate enzyme activity?

Activators- increase activity | Inhibitors- decrease activity

Why do you regulate enzyme activity?

to control biochemical pathways

What are the 2 types of inhibition?

Competitive and Non-Competitive

What is competitive inhibition?

inhibitor bonds at active site therefore restricting access for normal substrate

What is non-competitive inhibition?

inhibitor binds to allosteric site and causes the shape of the active site ti change therefore the substrate cannot bind to the active site.

What is the allosteric site?

a different location than the active site on an enzyme where other molecules or non-competitive inhibitors can bind

What is feedback inhibition?

where the end product of a biochemical pathway increases and causes end product t "feedback" to allosterically inhibit a substrate at the beginning of the pathway