Integral Proteins Flashcards
How do integral proteins interact with the core of the membrane?
Tightly bound to the membrane through interactions with fatty acid chains in hydrophobic core of bilayer
Can integral proteins be removed from the membrane?
No, not without breaking it
How do integral proteins span the membrane?
With single or multiple transmembrane (TM) segments
What are TM segments made up of?
Mainly made up of amino acids with hydrophobic side chains
Integral proteins are amphipathic, what does this mean?
Have both hydrophobic and hydrophilic regions
What is the distribution of integral proteins across the bilayer?
Asymmetrically distributed
How can integral protein be extracted?
Only by sing agents that disrupt the membrane structure e.g. organic solvents (chloroform) or detergents
Glycophorin A is an example of an integral protein. Where is it found and why is it found here?
Found in RBCs - enabling them to slip through vasculature easily
Describe the features of Glycophorin A.
- Single TM domain
- Is a glycoprotein
- Asymmetrically orientated
What is the extracellular domain of Glycophorin A like?
Extracellular domain is glycosylated (extra carbohydrates added)
