BIOS41_Lecture5_01232008

BIOS41_Lecture5_01232008 - 04_19_functiondomains Many...

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BIOS 41 Biology Core I: Cellular and Molecular Spring 2008 Professor J. A. Sands Lecture 5, January 23 Proteins (Chapter 4, pages 119-143)
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04_01_peptide bonds.jpg Amino acids are linked together by peptide bonds.
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04_02_polypeptide back.jpg Proteins are made of a polypeptide backbone with attached side chains.
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04_03_20 amino acids.jpg Twenty different amino acids are found in proteins.
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04_04_noncovalent.jpg Three types of noncovalent bonds help proteins fold.
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04_05_Hydrophobic.jpg Hydrophobic forces help proteins fold into compact conformations.
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04_09_Proteins.jpg Shapes and sizes of some proteins .
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04_10_1_alpha h. beta s.jpg One common folding pattern, the alpha helix.
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04_10_2_alpha h. beta s.jpg Other folding pattern: beta sheet
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Unformatted text preview: 04_19_functiondomains.jpg Many proteins are composed of separate functional domains. 04_21_Serine proteases.jpg Proteins can be classified into families. Each family member has an amino acid sequence and 3-D structure that closely resembles that of the other family members . Shown here is an example of a protein family: the serine proteases, a group of enzymes involved in digestion and blood clotting. 04_23_asymmetrical as.jpg Some proteins are formed as a symmetrical assembly of subunits. Hemoglobin, shown here, is an example. 04_27_Viral capsids.jpg Viral capsids are made of protein assemblies. 04_29_Disulfide bonds.jpg Disulfide bonds help stabilize a favored protein conformation....
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BIOS41_Lecture5_01232008 - 04_19_functiondomains Many...

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