Protein Folding

Explore how hydrophobic and hydrophilic interactions cause proteins to fold into specific shapes.

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Explore how hydrophobic and hydrophilic interactions cause proteins to fold into specific shapes. Proteins, made up of amino acids, are used for many different purposes in the cell. The cell is an aqueous (water-filled) environment. Some amino acids have polar (hydrophilic) side chains while others have non-polar (hydrophobic) side chains. The hydrophilic amino acids interact more strongly with water (which is polar) than do the hydrophobic amino acids. The interactions of the amino acids within the aqueous environment result in a specific protein shape.

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Copyright
© Copyright The Concord Consortium

Record Link
<a href="">The Concord Consortium. Protein Folding. Concord: The Concord Consortium, 2013, August 16.</a>

AIP
Protein Folding (The Concord Consortium, Concord, 2013, August 16), WWW Document, (https://concord.org/).

AJP
Protein Folding (The Concord Consortium, Concord, 2013, August 16), WWW Document, (https://concord.org/).

APA
Protein Folding. (2013, August 16). Retrieved 2017, June 25, from The Concord Consortium: https://concord.org/

Disclaimer: The Concord Consortium offers citation styles as a guide only. We cannot offer interpretations about citations as this is an automated procedure.

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This activity runs entirely in a Web browser. Preferred browsers are: Google Chrome (versions 30 and above), Safari (versions 7 and above), Firefox (version 30 and above), Internet Explorer (version 10 or higher), and Microsoft's Edge.

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Next-Generation Molecular WorkbenchThis resource is a part of the Concord Consortium's Next-Generation Molecular Workbench project.

Grade Level
Middle School, High School, Higher Education
Subject
Biology
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