List the 4 major types of protein conformations (levels) and describe each.
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List the 4 major types of protein conformations (levels) and describe each.

[From: ] [author: ] [Date: 12-07-04] [Hit: ]
Primary is the most simple. It is just a chain of amino acids held together by either a covalent or peptide bond.Secondary is a step above that is when the polypeptides form hydrogen bonds between each other to form either an alpha helix structure or a beta structure.The alpha helix looks somewhat like DNA and the beta sturcutre can be thought of as beta sheets, just stacks of proteins as if theyre paper. The Tertiary Structure is when the protein will get a 3D form by adding more bonds between the polypeptides which will help to determine the purpose of the protein.......
I can't find it in my textbook

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By conformations I assume you mean the 4 levels of protein structure??

If so..

There are four levels Primary, Secondary, Tertiary, and Quaternary. Each is characterized by a distinct layout of amino acids which will form the protein.

Primary is the most simple. It is just a chain of amino acids held together by either a covalent or peptide bond.

Secondary is a step above that is when the polypeptides form hydrogen bonds between each other to form either an alpha helix structure or a beta structure.

The alpha helix looks somewhat like DNA and the beta sturcutre can be thought of as beta sheets, just stacks of proteins as if they're paper.

The Tertiary Structure is when the protein will get a 3D form by adding more bonds between the polypeptides which will help to determine the purpose of the protein. These bonds can be hydrogen bonds, salt bridges, or even disulfide bonds.

Finally Quaternary structures are when a protein can develop multiple subunits. For example it's when the protein goes from being a tertiary structure, to having multiple tertiary structures attached.

I hope this helps :)

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Primary linear structure is the linear order of amino acids.
Higher order properties depend on amino acid’s primary order.

Secondary- regional structure is the formation of stable local patterns within the folded molecule.
Regional structures:
Alpha helix is held together by hydrogen bonds between the C=O and N-H groups.
Beta pleated sheet structure
Zeta irregular structure


The tertiary shape a protein takes in 3-D is made up of all the local modules like beta pleated sheets and alpha helices (the protein's secondary structure). The protein is folded into a stable conformation depending on the chemistry of its surroundings and on the chemical interactions of its amino acid side chains (the primary structure).
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