Protein Structure & Function and Globular & Fibrous Proteins

0.0(0)
studied byStudied by 1 person
GameKnowt Play
learnLearn
examPractice Test
spaced repetitionSpaced Repetition
heart puzzleMatch
flashcardsFlashcards
Card Sorting

1/12

encourage image

There's no tags or description

Looks like no tags are added yet.

Study Analytics
Name
Mastery
Learn
Test
Matching
Spaced

No study sessions yet.

13 Terms

1
New cards

How do you identify a 4 alpha helical bundle?

  • 4 helices

  • they have polar and non polar amino acids

  • usually have up to 6 non polar residues next to each other to create hydrophobic area inside the bundle

2
New cards

How can you identify a alpha/beta protein?

have a combination of alpha and beta secondary structures

3
New cards

How can you identify a beta-alpha-beta protein?

  • each beta strand twists to distort H bond

    • can be saddle shape or barrel shape

  • amphipathic helices outside

  • hydrophobic strands in middle

4
New cards

How can you identify a domain?

  • several proteins associated together

    • frequently linked or inserted within one another

5
New cards

Name and briefly describe 2 fibrous proteins

  • alpha keratin

    • 2 polypeptide dimer that have a left handed twist

    • chains cross linked by disulfide

  • beta keratin

    • stacked anti-parallel beta sheets

    • alternating Gly & Ala/Ser residues

    • stacking makes it strong

    • dispersed among alpha helices to give some flex

6
New cards

What internal conformational change occurs when oxygen binds the heme Fe in hemoglobin?

  • A shift of the F-helix

    • histidine is in this helix

    • changes interactions

  • rotation of one alpha-beta dimer

<ul><li><p>A shift of the F-helix</p><ul><li><p>histidine is in this helix</p></li><li><p>changes interactions</p></li></ul></li><li><p>rotation of one alpha-beta dimer</p></li></ul><p></p>
7
New cards

How is the quaternary structure changed when oxygen binds the heme Fe in hemoglobin?

The space between the alpha helices tightens with oxygen is bound (0.39 nm)

<p>The space between the alpha helices tightens with oxygen is bound (0.39 nm)</p>
8
New cards

What is the Bohr effect and how does it facilitate CO2 transport?

  • The Bohr effect enhances oxygen delivery to tissues where CO₂ production is high

  • Does this by making Hb bound with O2 more acidic (lowering the pH)

  • helps CO₂ transport by promoting hemoglobin's release of oxygen and uptake of CO₂.

9
New cards

How does BPG affect the transport of oxygen by hemoglobin?

  • BPG binds to deoxy Hb (squeezed conformation)

  • lowers amount of O2 bound

    • lowering affinity of Hb for O2

10
New cards

What are globular protiens?

  • soluble in water

  • circular shape

  • alpha-helix and beta sheet stabilize structure

  • L-amino acids

11
New cards

What are 3 types of alpha helices?

  1. amphipathic - one side hydrophobic & one side hydrophilic

  2. hydrophobic - inside membrane/structure

  3. polar - solvent exposed

12
New cards

Why can’t myoglobin be used to transport oxygen from the lungs to the tissues?

  • binds too tightly with oxygen

  • meant to drop off oxygen to mitochondria

  • used for tissues

13
New cards

Does BPG inhibit or enhance O2 binding?

inhibits binding to encourage the oxygenation of tissue