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CHEM203: Bioinorganic Chemistry

Unit 2: An Overview of Characterization Methods in Bioinorganic Chemistry   The structures of the metal-containing residues in biological molecules can be discovered by using a variety of spectroscopy methods and techniques.  Methods used for structural elucidation, as well as mechanistic studies, include: X-Ray crystallography; nuclear magnetic resonance (NMR) spectroscopy; vibrational spectroscopies, such as infrared (IR) and Raman spectroscopies; and electronic spectroscopies, such as ultraviolet-visible (UV-Vis) spectroscopy and electron paramagnetic resonance (EPR) spectroscopy. In this unit, you will review the basic principles of these analytical techniques and explore their application to inorganic biomolecules.

Unit 2 Time Advisory
This unit should take you approximately 3.5 hours to complete.

☐    Subunit 2.1: 1 hour    

☐    Subunit 2.2: 0.5 hour

☐    Subunit 2.3: 0.5 hour

☐    Subunit 2.4: 0.5 hour

☐    Subunit 2.5: 0.5 hour

☐    Subunit 2.6: 0.5 hour

Unit2 Learning Outcomes
Upon successful completion of this unit, the student should be able to: - Explain the different methods of X-Ray crystallography that may be used to determine the structures of proteins and binding sites. - Discuss the utilization of NMR and paramagnetic NMR. - Describe how vibrational and electronic spectroscopy can be used to probe binding sites. - Predict the behavior of biomolecules based on biomimetic molecules and metal substitutions.

2.1 X-Ray Crystallography: Resolving Protein Structures   - Reading: Wells College: Special Topics in Inorganic Chemistry: Bioinorganic Chemistry: Dr. Christopher T. Bailey’s “Analytical Methods” The Saylor Foundation does not yet have materials for this portion of the course. If you are interested in contributing your content to fill this gap or aware of a resource that could be used here, please submit it here.

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  • Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “X-Ray Crystallography” and “X-Ray Absorption Spectroscopy” The Saylor Foundation does not yet have materials for this portion of the course. If you are interested in contributing your content to fill this gap or aware of a resource that could be used here, please submit it here.

    Submit Materials

2.2 Nuclear Magnetic Resonance (or Paramagnetic NMR) Spectroscopy   Note: Some of the material you need to know for this subunit is covered in the first reading assigned beneath subunit 2.1 of this course, in particular slides 4 and 5 of Dr. Bailey’s PowerPoint presentation.  You may find it helpful to refer back to those slides as you complete the reading below.

  • Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Nuclear Magnetic Resonance Spectroscopy” The Saylor Foundation does not yet have materials for this portion of the course. If you are interested in contributing your content to fill this gap or aware of a resource that could be used here, please submit it here.

    Submit Materials

2.3 Electronic Spectroscopy (UV-Vis Spectroscopy and Magnetic Circular Dichroism)   Note: Some of the material you need to know for this subunit is covered in the first reading assigned beneath subunit 2.1 of this course, in particular slides 6 and 7 of Dr. Bailey’s PowerPoint presentation.  You may find it helpful to refer back to those slides as you complete the reading below.

  • Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Magnetic Circular Dichroism (MCD) Spectroscopy” The Saylor Foundation does not yet have materials for this portion of the course. If you are interested in contributing your content to fill this gap or aware of a resource that could be used here, please submit it here.

    Submit Materials

2.4 Vibrational Spectroscopy (Infrared (IR), Raman, and Resonance Raman)   Note: Some of the material you need to know for this subunit is covered in the first reading assigned beneath subunit 2.1 of this course, in particular slide 8 of Dr. Bailey’s PowerPoint presentation.  You may find it helpful to refer to that slide as you complete the reading below.

  • Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Resonance Raman Spectroscopy” The Saylor Foundation does not yet have materials for this portion of the course. If you are interested in contributing your content to fill this gap or aware of a resource that could be used here, please submit it here.

    Submit Materials

2.5 Mössbauer Spectroscopy   Note: Some of the material you need to know for this subunit is covered in the first reading assigned beneath subunit 2.1 of this course, in particular slides 9 and 10 of Dr. Bailey’s PowerPoint presentation.  You may find it helpful to refer back to those slides as you complete the reading below.

  • Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Mössbauer Spectroscopy” Link: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Mössbauer Spectroscopy” (HTML)
     
    Instructions: Please click on the link above to access and read the webpage in its entirety for an overview of Mössbauer spectroscopy.  This material gives you a concise summary of the application of Mössbauer spectroscopy to the study of bioinorganic systems. 
     
    This reading should take you approximately 30 minutes to complete.
     
    Terms of Use: Please respect the copyright and terms of use displayed on the webpage above.

2.6 Electron Paramagnetic Resonance (EPR) Spectroscopy   - Reading: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Electron Paramagnetic Resonance (EPR) Spectroscopy” and “ENDOR Spectroscopy” Link: The University of Georgia’s Center for Metalloenzyme Studies: MRIL Biophysics Module’s “Electron Paramagnetic Resonance (EPR) Spectroscopy” and “ENDOR Spectroscopy” (HTML)
 
Instructions: Please click on the links above to access and read both webpages in their entirety for an overview of electron paramagnetic resonance (or EPR) spectroscopy.  ENDOR is a specific application of EPR spectroscopy.  This material gives you a concise summary of the uses of these techniques in studying bioinorganic systems. 
 
This reading should take you approximately 30 minutes to complete.
 
Terms of Use: Please respect the copyright and terms of use displayed on the webpages above.