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


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
edit
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

WEEK 5:

Protein Folding + Function

QuestionAnswer
polypeptide folding into tertiary structure is driven by what interactions between secondary structure elements + entropy (burying hydrophobic residues)
hydrophobic interactions non polar parts buried inside to maximise entropy
electrostatic interactions VDW, hydrogen bonds, ionic interactions
major stabilising forces in proteins hydrophobic interactions, electrostatic interactions, covalent bonds
entropy disorder - ability to make other interactions
haemaglobin contains what 2 alpha subunits + 2 beta subunits + haem group
deoxyHb alpha beta dimers are held together by ionic bonds + hydrogen bonds
how do bonds in deoxyHb alpha beta dimers weaken when oxygen bond
T (tuat) Hb deoxygenated Hb
R (relaxed) Hb oxygen binding
Hb oxygen sigmoidal curve explanation
main protein classes fibrous, globular, membrane
fibrous secondary structure eg keratin
globular secondary structure elements interspaced with irregular loops
membrane integral membrane proteins with 1 or more hydrophobic domains spanning lipid bilayer eg ion channels
disruption to metabolic pathway
impairment/ loss of defence
protein aggregation
dysfunction of regulatory protein/ receptor
sickle-cell anaemia single mutation in beta subunit of Hb, at position 6 (glutamate) becoming valine, 2 copies of Hb aggregates
pathology of sickle cell anaemia Hbs carrying E6V mutation aggregates forming fibres in low oxygen conditions, distorting erythrocytes into sick shape so block capillary blood flow
mechanisms to prevent/ remove misfolded proteins chaperone mediating folding, proteasome (via ubiquitin) + lysosome (in autophagy) to mediate breakdown
transmissible spongiform encephalopathies genetic or acquired
prion proteins form insoluble fibrillary aggregates + small soluble oligomers
glycosylation attachment of carbohydrates, sugars either N-liked (to asparagine) or O-linked to serine/threonine, involvedi n cell-cell recognition
glycosylation importance adids folding, infuence new protein,
hydroxylation
Created by: kablooey
Popular Medical sets

 

 



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