Save
Upgrade to remove ads
Busy. Please wait.
Log in with Clever
or

show password
Forgot Password?

Don't have an account?  Sign up 
Sign up using Clever
or

Username is available taken
show password


Make sure to remember your password. If you forget it there is no way for StudyStack to send you a reset link. You would need to create a new account.
Your email address is only used to allow you to reset your password. See our Privacy Policy and Terms of Service.


Already a StudyStack user? Log In

Reset Password
Enter the associated with your account, and we'll email you a link to reset your password.
focusNode
Didn't know it?
click below
 
Knew it?
click below
Don't Know
Remaining cards (0)
Know
0:00
Embed Code - If you would like this activity on your web page, copy the script below and paste it into your web page.

  Normal Size     Small Size show me how

4U Biology

Chemistry of Life

QuestionAnswer
Carbohydrates macromolecule made up of glucose subunits joined by glycoside linkages
Protein macromolecule made up of amino acid subunits linked by peptide bonds
Lipids macromolecule made up of glycerol + fatty acid subunits, joined by dehydration synthesis rxns
Nucleic acids macromolecule made up of nucleotide (phosphate + ribose sugar + nitrogenous base) subunits joined by phosphodiester bonds
Ionic bond attraction between a positively charged metal ion and a negatively charged non-metal ion.
Covalent bond formed when electrons are shared between two non-metal atoms.
London Dispersion Force A type of IMF where electrons around one molecule momentarily repel the electrons of a nearby molecule.  This creates brief temporary dipole. Weakest type of IMF.
Dipole-Dipole Force of Attraction A type of IMF where dipoles (of opposite charges) on separate molecules are attracted to each other. The 2nd weakest type of IMF
Hydrogen bond A type of IMF where a partially positive hydrogen dipole on one molecule is attracted to a partially negative dipole on a separate molecule.
Ion-Dipole Force of Attraction A type of IMF where a fully charged ion is attracted to an oppositely charge dipole on a separate molecule. Strongest type of IMF
Hydrophobic water-hating. Nonpolar molecules will be attracted to each other but repelled by polar molecules.
Intermolecular Forces of Attraction (IMFs) cause separate molecules to be attracted to each other
Polar molecule if it has polar bonds (where eletronegativity difference is btwn 0.41--1.7) AND if these polar bonds don't cancel each other out due to asymmetrical shape
"Like dissolves like" means that polar and ionic compounds dissolve in polar solvents whereas non-­‐polar compounds dissolve in non-­‐polar solvents.
monosaccharides glucose, galactose and fructose. The latter two are also C6H12O6 but have a different shape from glucose
polymer many subunits linked together to make a long chain
disaccharides maltose (gluc + gluc); lactose (gluc + gal); sucrose (gluc + fruc)
condensation rxn type of biochemical reaction in which two molecules are joined together to form a larger molecule. It is also known as a dehydration synthesis since a molecule of water is removed.
hydrolysis rxn type of biochemical reaction in which H2O is added at the bond point to break apart the molecule into its smaller components
Polysaccharides Energy storage (eg. starch in plants, glycogen in animals) and Structure (eg. cellulose in plants, chitin in animals)
denaturation the process where a protein loses its specific three-dimensional folded structure due to external stress, such as heat, chemicals, or changes in pH,
primary structure the sequence of amino acids in a polypeptide chain
entropy the degree of randomness or disorder in a system. Systems will move toward increased disorder spontaneously.
activation energy energy needed to initiate a chemical rxn.
catalyst reduces activation energy in a rxn therefore the rxn goes faster. Can be re-used.
Substrate the molecule an enzyme binds to because it recognises its particular shape
Active site spot on an enzyme where the substrate fits, allowing the enzyme to react chemically with the substrate
induced fit The change in shape of the active site to accommodate the substrate. This occurs because of intermolecular forces
competitive inhibitor Competes with substrate for enzyme active site. Similar to the substrate, so it can enter the active site. They block the real substrate.
non-competitive inhibitor Attaches to another site on the enzyme, changing its shape so that the substrate cannot enter active site. This inhibitor is not affected by substrate concentration.
allosteric regulation This regulation controls enzyme activity by having activators or inhibitors binding to sites on the enzyme that are not active sites.
Created by: jcepella
 

 



Voices

Use these flashcards to help memorize information. Look at the large card and try to recall what is on the other side. Then click the card to flip it. If you knew the answer, click the green Know box. Otherwise, click the red Don't know box.

When you've placed seven or more cards in the Don't know box, click "retry" to try those cards again.

If you've accidentally put the card in the wrong box, just click on the card to take it out of the box.

You can also use your keyboard to move the cards as follows:

If you are logged in to your account, this website will remember which cards you know and don't know so that they are in the same box the next time you log in.

When you need a break, try one of the other activities listed below the flashcards like Matching, Snowman, or Hungry Bug. Although it may feel like you're playing a game, your brain is still making more connections with the information to help you out.

To see how well you know the information, try the Quiz or Test activity.

Pass complete!
"Know" box contains:
Time elapsed:
Retries:
restart all cards