Save
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

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.

Question

Proteins Contain ...
click to flip
focusNode
Didn't know it?
click below
 
Knew it?
click below
Don't know

Question

Proteins
Remaining cards (37)
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

Unit 1

2.12

QuestionAnswer
Proteins Contain ... Carbon, Hydrogen, Oxygen, and Nitrogen and, Formed from Amino Acids
Proteins all proteins contain carbon, hydrogen, oxygen, and nitrogen and are the most abundant organic molecules in the body
Amino acids are the... monomer for proteins
Proteins carry out several functions including Support Movement Transport Buffering Metabolic regulation Coordination and control Defense
Protein structure: organic polymers that consist of long chains if similar organic molecules called amino acids
There are 20 ... amino acids in the body
Peptide bond covalent bond between carboxyl group of one amino acid and the amino group of another.
Peptides molecules consisting of amino acids held together by peptide bonds
Dipeptide molecule created containing 2 amino acids
Polypeptide molecule created containing 3 or more amino acids
Polypeptides with more than 100 amino acids are usually called... proteins; familiar proteins include hemoglobin, collagen, and keratin.
Primary structure sequence of amino acids along the length of single polypeptide.
Secondary structure: shape that results from the presence of hydrogen bonds between atoms at different parts of a polypeptide chain
Tertiary structure: complex coiling and folding that gives a protein its final 3-D shape.
Quaternary structure: nteraction between individual polypeptide chains to form a protein complex.
Globular proteins compact, generally rounded and soluble in water.
Globular proteins.. can function only if they remain in solution Unique shape of protein comes from tertiary structure Hemoglobin and Myoglobin are both globular proteins
Fibrous proteins form extended sheets or strands and insoluble in water
Fibrous proteins... Tough, durable. Usually play structural role in body. Shape usually due to secondary structure
Shape of a protein determines its ... functional characteristics and the sequence of amino acids ultimately determine its shape. Ex. Certain cancers and Sickle Cell anemia result from changing a single amino acid in the sequence of complex proteins
ertiary and Quaternary shapes of complex proteins depend not only on their amino acid sequence, BUT also... local environmental conditions
Substrates Reactants in enzymatic reactions
Active site Special region of enzyme that substrates must bind to
A Simplified View of Enzyme Structure and Function Substrate binds to active site of enzyme. Once bound to the active sites, the substrates are held together, making their interaction easier. Substrates binding alters the shape of the enzyme, and this change promotes product formation.
A Simplified View of Enzyme Structure and Function.. Product detaches from enzyme; entire process can now be repeated
Specificity Each enzyme catalyzes only one type of reaction.
Saturated Enzyme that has reached its saturated limit is said to be saturated
Saturation Limit Substrate concentration required to reach the maximum rate of reaction
Cofactor An ion or a molecule that must bind to an enzyme before substrates can also bind.
Without a cofactor, the enzyme is intact but nonfunctional
With a cofactor, the enzyme can catalyze a specific reaction
Coenzyme non-protein organic molecules that function as cofactors. Ex. Our bodies convert vitamins into co-enzymes. The human body cannot synthesize most of the vitamins it needs, it must obtain these from your die
Temperature and PH... affect enzyme function.
Denaturation Change in tertiary and quaternary structure (unfolding of protein) that makes it nonfunctional caused by high heat or low pH (acid)
Denaturation example When you fry an egg, the temperature rises causing the protein in the egg white to denature. Eventually causing the proteins to become completely and irreversibly denatured forming an insoluble white mass
Glycoproteins and Proteoglycans are... combination of protein and carbohydrate molecules
Glycoproteins Large proteins with small carbohydrate groups attached
Proteoglycans Large polysaccharide molecules linked by polypeptide chains
Created by: casas125903
 

 



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