BCH4024 - Mareci Lecture 5

BCH4024 - Mareci Lecture 5 - Lecture 5 Course Subsection...

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Lecture 5 Course Subsection Outline L-3. Amino Acids (AA’s) L-4. Peptides and Peptide Bonds ept des a d ept de o ds L-5. Three-dimensional Structure of Proteins L-6. Protein Dynamics and Protein Folding L-7. Protein Function; Hemoglobin L-8. Protein Function, Contractile and Motile Systems Copyright University of Florida. All Rights Reserved 1
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Lecture 5 General Characteristics of Protein Structure 1. No two atoms on groups of a molecule can approach each other closer than allowed by their van der Waals radii . 2. The amide group must remain in a planer orientation relative to the carboxyl group in the peptide bond. In general, the -carbons on adjacent AA’s are in a trans configuration. Copyright University of Florida. All Rights Reserved 2
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Lecture 5 Structure of the Peptide Bond Peptide bond is a resonance-hybrid of two structures so the O=C-N-H bonds are co-planar Figure 4.2, p. 119: Lehninger Principles of Biochemistry is- rans isomerization is defined by the Cis Trans isomerization is defined by the orientation of adjacent C across the peptide bond. The peptide bond is nearly always in a trans onfiguration since the steric hindrance of side Copyright University of Florida. All Rights Reserved 3 configuration since the steric hindrance of side chains is greater for a cis configuration.
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Lecture 5 Peptide “planar” angle Copyright University of Florida. All Rights Reserved 4 Edison, Nature Structural Biology 2001:8;201-202 (available on BCH 4024 web site on WebCT)
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Lecture 5 General Characteristics of Protein Structure (continued) 3. AA residues can rotate about covalent bonds to the -carbon so that the peptide-bond planes can rotate relative to each other. Also the side chains have additional degrees of rotational freedom about covalent bonds. , rotation angle around the C – NH bond , rotation angle around the C – CO bond 4. Because of this rotational freedom, on- ovalent bonding is necessary to non covalent bonding is necessary to stabilize a regularly-folded protein structure (e.g. hydrogen bonding between the amino hydrogen on one Copyright University of Florida. All Rights Reserved 5 AA and a carbonyl oxygen on another).
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Lecture 5 Steric Hindrance of Peptide Planes
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This note was uploaded on 03/15/2010 for the course BCH 4024 taught by Professor Allison during the Spring '08 term at University of Florida.

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BCH4024 - Mareci Lecture 5 - Lecture 5 Course Subsection...

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