Answer:
<em> e) Ala</em>
Explanation:
Alpha helix is a secondary structure of proteins, it is made of 3.6 aminoacids residues per turn, this structure is possible thanks to local hydrogen bonding between C=O and N-h groups. The result is a cylindrical structure with a hydrogen-bonded backbone and the outside studded with side chains.
Glycin has an -H in its side chain, this makes it a too flexible molecule, therefore it's unusual to find them in alpha-helical structures because their presence could cause the helix to deform. Large R-groups can also affect this stability, phenylalanine has a bulky aromatic side group, this discards it as a stabilizer. Serine has a hydrogen bond donor or acceptor as a side chain, due to the proximity to the main chain it competes with the main chain to form NH and CO bonds. Alanine is the most common amino acid in alpha-helix structures because it has a short and no charged R group (unlike arginine that even when it's short it has a charged R-group), this makes it flexible enough to keep the structure stabilized.
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The muscle that inserts on the acromion and scapular spine is the Trapezius.
The trapezius muscle inserts into the scapular spine acromion and posterior superior lateral clavicle. Contraction of its various parts thus allows the scapula to be lifted, suspended, stabilized, and rotated. inserted. The deltoid muscle inserts into the acromion process, the main muscle that raises and extends the arm.
In humans, the acromion process can be flat curved hooked, or convex depending on the shape. The intrinsic muscles of the scapula include the rotator cuff teres major subscapularis teres minor and infraspinatus. These muscles attach to the surface of the scapula and assist in the abduction and external and internal rotation of the glenohumeral joint.
Learn more about The acromion here:-brainly.com/question/28192526
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E. Starting at the most basic level is the atom
Answer:
13,15
Explanation:
the sequence is adding by (+2)
