Answer:
The amino acids in such a helix would be hydrophobic in nature.
An α helix is particularly suited to cross a membrane because all of the carbonyl oxygen atoms and the hydrogen atoms of amide of the peptide backbone take part in intrachain hydrogen bonds, thus stabilizing these polar atoms in a hydrophobic environment.
Explanation :
Many transmembrane protiens use several alpha-helices wrapped up together.
It is usually seen as the helical structure can internally satisfy all the hydrogen-bonds , it doesn't leave any polar groups that are exposed to membrane if the sidechains are hydrophobic.
Sometimes, 2 to 3 alpha helices will wrap around each other , forming coiled coil. In an aphipathic alpha helix , the hydrophobic R groups on one side of each helix interact with each other while the hydrophilic R groups on the other side of each helix will interact with water.
Answer:
→alpha-helices
→Non-polar Amino acids
→because they and non -polar and hydrophobic.
Explanation:
Membrane proteins can be intrinsic (integral ) that is embedded in the membrane bilayer or extrinsic(peripheral) attached to the outer membrane layer.
These integral protein transcend the entire phospholipid bilayer, with the alpha- helices. The latter have hydrophobic side chains of non-polar amino acids. They are held to the cell membrane with these side chains which forms hydrophobic interactions with fatty acyl group of the phosphoslipid bilayer, and sometimes ionic bond with the polar head of phospholipid.
These alpha helix are non-polar(uncharged) and hydrophobic.A characteristic feature that make them to interact and fixed into the integral phospholipid hydrophobic medium.
