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Membrane-spanning proteins are notoriously difficult to characterize by x-ray crystallography. Hollut of VISAil 510 plong and bloow tow2DE ILOV a. Explain how the information in the diagrams below can be used in the detection of membrane-a spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. Amino terminus T 5.4 A (3.6 residues) b. Identify and briefly describe how the features of a transmembrane protein composed of B-sheets differ from that above.

Membrane-spanning proteins are notoriously difficult to characterize by x-ray crystallography. Hollut of VISAil 510 plong and bloow tow2DE ILOV a. Explain how the information in the diagrams below can be used in the detection of membrane-a spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. Amino terminus T 5.4 A (3.6 residues) b. Identify and briefly describe how the features of a transmembrane protein composed of B-sheets differ from that above.

Biochemistry
Biochemistry
9th Edition
ISBN:9781319114671
Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Chapter1: Biochemistry: An Evolving Science
Section: Chapter Questions
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### Characterization of Membrane-Spanning Proteins *Membrane-spanning proteins* are notoriously difficult to characterize by x-ray crystallography. #### a. Detection of Membrane-Spanning Proteins **Question:** Explain how the information in the diagrams below can be used in the detection of membrane-spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. **Diagram Explanation:** - The diagram depicts an alpha helix structure with an amino terminus. - It shows the repeating structure of an alpha helix with spacing marked as 5.4 Å, which corresponds to 3.6 residues per turn. **Analysis:** This information assists in identifying proteins that can span the lipid bilayer. Given the typical thickness of 30 Å for the lipid bilayer, the periodic nature of the alpha helix structure can be used to calculate how many turns or residues of an alpha helix are necessary to span the membrane. #### b. Features of Transmembrane Proteins with β-Sheets **Question:** Identify and briefly describe how the features of a transmembrane protein composed of β-sheets differ from that above. **Analysis:** - β-sheets differ in structure from alpha helices as they involve extended strands that can form broader sheets through hydrogen bonding. - In the context of transmembrane proteins, β-sheets will form a barrel-like structure (β-barrel) to traverse the lipid bilayer, differing from the cylindrical helices of alpha helices. - These sheets provide a different mode of spanning the membrane due to their distinct arrangement and bonding, affecting how they fit within the lipid bilayer. ### Conclusion Understanding these structural differences is crucial for characterizing the membrane-spanning regions of proteins, which has implications for their functional roles and for biotechnological applications.
Transcribed Image Text:### Characterization of Membrane-Spanning Proteins *Membrane-spanning proteins* are notoriously difficult to characterize by x-ray crystallography. #### a. Detection of Membrane-Spanning Proteins **Question:** Explain how the information in the diagrams below can be used in the detection of membrane-spanning proteins consisting of alpha helices, given that the lipid portion of a typical bilayer is approximately 30 Å thick. **Diagram Explanation:** - The diagram depicts an alpha helix structure with an amino terminus. - It shows the repeating structure of an alpha helix with spacing marked as 5.4 Å, which corresponds to 3.6 residues per turn. **Analysis:** This information assists in identifying proteins that can span the lipid bilayer. Given the typical thickness of 30 Å for the lipid bilayer, the periodic nature of the alpha helix structure can be used to calculate how many turns or residues of an alpha helix are necessary to span the membrane. #### b. Features of Transmembrane Proteins with β-Sheets **Question:** Identify and briefly describe how the features of a transmembrane protein composed of β-sheets differ from that above. **Analysis:** - β-sheets differ in structure from alpha helices as they involve extended strands that can form broader sheets through hydrogen bonding. - In the context of transmembrane proteins, β-sheets will form a barrel-like structure (β-barrel) to traverse the lipid bilayer, differing from the cylindrical helices of alpha helices. - These sheets provide a different mode of spanning the membrane due to their distinct arrangement and bonding, affecting how they fit within the lipid bilayer. ### Conclusion Understanding these structural differences is crucial for characterizing the membrane-spanning regions of proteins, which has implications for their functional roles and for biotechnological applications.
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