Helices are common secondary structures found in proteins. Choose two different protein helices and compare and contrast their key structural features. How do helices adapt to their structural environment in the protein? In Tansey Biochemistry, there are several examples / case studies of proteins that help us understand protein structure and function. Choose two different proteins from these examples and compare and contrast their key structural features. Briefly explain how their structures are adapted to their function

Human Anatomy & Physiology (11th Edition)
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Author:Elaine N. Marieb, Katja N. Hoehn
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Chapter1: The Human Body: An Orientation
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Question No. 2
Helices are common secondary structures found in proteins.
Choose two different protein helices and compare and contrast their key structural features.
How do helices adapt to their structural environment in the protein?
In Tansey Biochemistry, there are several examples / case studies of proteins that help us understand
protein structure and function. Choose two different proteins from these examples and compare and
contrast their key structural features. Briefly explain how their structures are adapted to their function.
Transcribed Image Text:Question No. 2 Helices are common secondary structures found in proteins. Choose two different protein helices and compare and contrast their key structural features. How do helices adapt to their structural environment in the protein? In Tansey Biochemistry, there are several examples / case studies of proteins that help us understand protein structure and function. Choose two different proteins from these examples and compare and contrast their key structural features. Briefly explain how their structures are adapted to their function.
Expert Solution
Step 1
Alpha Helices Beta Helices
Right-handed coiled rod-like structure. Sheet-like structure.
Hydrogen bonds form within the polypeptide chain.

Beta sheets are reformed by linking two or more beta strands by H bonds.

Alpha helices can be a single chain. Beta helices or Beta sheets can not exist as a single beta-strand.
Alpha helices have only one type. Beta sheets can be parallel, anti-parallel, or mixed.
-R groups of the amino acids are oriented outside of the helix. -R groups are directed to both inside and outside of the sheet.

 

In alpha-helices -CO group of a single amino acid is attached to the amino acid by an H-bond where polypeptide chains twisted into a spiral that is four down the chain and in a ß pleated sheet or beta helices, two or more polypeptide chains present next to each other, forming a sheet-like structure. This formation allows all amino acids present in the chain to forms hydrogen bonds with each other forming a wave.

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