Participation Problem: Chapter 10, Problem 4: The lipid portion of a typical bilayer is about 30 Å thick. (a) Calculate the minimum number of residues in an a-helix required to span this distance. (b) Calculate the minimum number of residues in a ß-strand required to span this distance. Skip part (c) (d) The epidermal growth factor receptor (EGFR) has a single transmembrane helix. Find it in this partial sequence. ...RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH... Table for reference (for parts a-b):

Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
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Chapter1: Biochemistry: An Evolving Science
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Participation Problem: Chapter 10, Problem 4: The lipid portion of a typical bilayer is about 30
Å thick.
(a) Calculate the minimum number of residues in an a-helix required to span this distance.
(b) Calculate the minimum number of residues in a ß-strand required to span this distance.
Skip part (c)
(d) The epidermal growth factor receptor (EGFR) has a single transmembrane helix. Find it in
this partial sequence.
...RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH...
Table for reference (for parts a-b):
TABLE 6.1 Parameters of some polypeptide
secondary structures
Structure Type
B Strand (antiparallel)
B Strand (parallel)
a helix
310 helix
Polypeptide II helix
Residues
per Turn
2.0
2.0
3.6
3.0
3.0
Rise (h) per
Residue
3.4 Å
3.2 Å
1.5 Å
2.0 Å
4.7 Å
Pitch (p)
6.8 Å
6.4 Å
5.4 Å
6.0 Å
9.4 Å
Transcribed Image Text:Participation Problem: Chapter 10, Problem 4: The lipid portion of a typical bilayer is about 30 Å thick. (a) Calculate the minimum number of residues in an a-helix required to span this distance. (b) Calculate the minimum number of residues in a ß-strand required to span this distance. Skip part (c) (d) The epidermal growth factor receptor (EGFR) has a single transmembrane helix. Find it in this partial sequence. ...RGPKIPSIATGMVGALLLLVVALGIGILFMRRRH... Table for reference (for parts a-b): TABLE 6.1 Parameters of some polypeptide secondary structures Structure Type B Strand (antiparallel) B Strand (parallel) a helix 310 helix Polypeptide II helix Residues per Turn 2.0 2.0 3.6 3.0 3.0 Rise (h) per Residue 3.4 Å 3.2 Å 1.5 Å 2.0 Å 4.7 Å Pitch (p) 6.8 Å 6.4 Å 5.4 Å 6.0 Å 9.4 Å
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