As seen in Fig 5-10 and 5-11 in barrel-form and in Fig 5-15 and 7-15 in ribbon f
ID: 68996 • Letter: A
Question
As seen in Fig 5-10 and 5-11 in barrel-form and in Fig 5-15 and 7-15 in ribbon form, what secondary structure is most commonly used to form transmembrane domains?
NH COOH Extracellular side Cytoplasmic side 413 20 M1 M2 M3 M4 -20 2 100 200 300 400 average of hydrophobicity is plotted for the entire amino acid sequence of the -subunit of the nicotinic ACh receptor. Each the plot represents an average hydrophobic index of a Figure 5-10 The secondary structure of membrane- spanning proteins. A. A proposed secondary structure for a subunit of the nicotini nt in acetylcholine (ACh receptor channel present in skeletal muscle sequence of 19 amino acids and corresponds to the midpoint Each cylinder (M1-M4) represents a putative membrane- spanning -helix comprised of approximately 20 hydrophobic amino acid residues. The membrane seaments are connected tor subunit gene. Four of the hydrophobic regions (M1-M4) by cytoplasmic or extracellular seaments (loopsl of hydroic correspond to the membrane-spanning segments. The hydro- residues. The amino terminus (NH) and carbaxy terminus (COOH) of the protein lie on the extracellular side of the membrane of the sequence. The amino acid sequence of the subunit is inferred from the nucleotide sequence of the cloned recep- phobic region at the far left in the plot is the signal sequence the extracellular surface of the cell during protein synthesis. The signal sequence is cleaved from the mature protein. (Reproduced, with permission, from Schofield et al. 1987 B. The membrane-spanning regions of an ion channel protein can be identified using a hydrophobicity plot. Here a runningExplanation / Answer
The structure that is more likely acceptable is the beta helix structure.
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