Basics of Protein Structure

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The second level of structure is called secondary structure, and is the shapes (conformations) formed by short sequences of amino acids. This level of structure is stabilized by <scene name='57/575866/H_bond_a_helix/3'>hydrogen bonds</scene> along the <scene name='57/575866/Backbone/2'>backbone</scene>. (More about [[hydrogen bonds]].) The two most common shapes are [[Helices in Proteins|alpha helices]] and [[Sheets in Proteins|beta strands]]. These are favored simply because [[Tutorial:Ramachandran principle and phi psi angles|two atoms cannot occupy the same space]] (steric collisions).
The second level of structure is called secondary structure, and is the shapes (conformations) formed by short sequences of amino acids. This level of structure is stabilized by <scene name='57/575866/H_bond_a_helix/3'>hydrogen bonds</scene> along the <scene name='57/575866/Backbone/2'>backbone</scene>. (More about [[hydrogen bonds]].) The two most common shapes are [[Helices in Proteins|alpha helices]] and [[Sheets in Proteins|beta strands]]. These are favored simply because [[Tutorial:Ramachandran principle and phi psi angles|two atoms cannot occupy the same space]] (steric collisions).
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==Protein Structure Data==
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The [[Protein Data Bank|World Wide Protein Data Bank]] (WWPDB) is where all experimentally-determined published protein structures are made freely available. Each model has a unique accession code, called a [[PDB code]]. One model of human insulin, shown at right has the PDB code <tt>3i40</tt>.
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==Further Reading==
For a more in depth discussion of protein structure, see [[Introduction to protein structure]]
For a more in depth discussion of protein structure, see [[Introduction to protein structure]]

Revision as of 18:46, 1 February 2020

Structure of insulin (PDB entry 3I40)

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

Ann Taylor, Eric Martz, Joel L. Sussman

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