Unformatted text preview: Chemistry 420 Instrumental Methods of Chemical Characterization Fall 2008 M, W: 12:00 ‐ 12:50 PM 217 Noyes Laboratory Instructor: Prof. Ryan C. Bailey T.A.: Callie Croushore Office: 44 Roger Adams Laboratory Office: 59 Roger Adams Laboratory Office hours: M, W, 1‐2 PM Office hours: T 9‐10 AM, R noon‐1 PM and by appointment and by appointment e‐mail: [email protected] e‐mail: [email protected] Textbook: Skoog, Holler, and Crouch, Principles of Instrumental Analysis, 6th Edition Course website: https://compass.uiuc.edu/webct/logon/460845621061 Course objectives: From the surface of distant planets to the tiny crevices of a catalyst particle, instrumental techniques facilitate the chemical characterization or a range of systems. Every day cutting edge analytical tools are allowing researchers to peer inside a single cell, counting individual DNA molecules and analyzing small biochemical modifications to proteins that are responsible for human disease. Right now, three machines containing a wide array of analytical instruments are operating over 35 million miles from the Earth, surveying the surface of Mars in search of water and other signs of life. Beyond these more cutting edge and exotic applications, instruments play an extremely imporant role in the analysis of food, drinking water, air quality, etc.—substances that we each encounter and rely upon everyday. This class is designed to provide an overview of instrumental methods of chemical analysis. We cannot “see” molecules and therefore we must utilize instrumentation to illuminate Ångstrom scale events in order to answer questions such as “What is it?” and “How much is there?”. An amazing number and diversity of instruments exist, each bringing inherent advantages and disadvantages to the analysis of a given system. The purpose of this class is to provide each student with an understanding of what instruments can measure, how the measurements are made, and how best to determine which instrument to use to solve a given challenge. Rather than describe each technique in extraordinary detail, this course will survey some of the most common classical, modern, and emerging approaches to instrumental analysis of complex chemical and biomolecular systems. Given this background, students should be well prepared to analyze a real‐world challenge, select the appropriate instrumental method, and then seek out greater detail from method‐specific literature in order to solve the problem at hand. Course outline: Date Topic Reading Problem Sets/Notes August 25 August 27 September 1 September 3 Course introduction: Importance of instruments in analysis Selecting the right measurement, statistical Skoog, Chapter 1, distributions, precision & accuracy Appendix 1 No Class Digital & analog signals, noise, signal to noise ratio Skoog, Chapter 5 Assign PS 1 Labor Day September 8 September 10 September 15 September 17 September 22 September 24 September 29 October 1 October 6 October 8 October 13 October 15 October 20 October 22 October 27 October 29 November 3 November 5 November 10 November 12 November 17 November 19 November 24‐26 December 1 December 3 December 8 December 10 December 11 December 17 1:30‐4:30 PM Optical spectroscopy: Light sources Optical spectroscopy: Behavior of light— refraction, diffraction, interference, & total internal reflection Optical spectroscopy: Photodetectors Atomic optical spectroscopy: absorbance, fluorescence, & emission Skoog, Chapter 7 Skoog, Chapter 7 PS 1 due Assign PS 2 NIH Pioneer Symposium Class cancelled Molecular optical spectroscopy: UV‐visible absorption Molecular optical spectroscopy: Applications of UV‐visible absorption Molecular optical spectroscopy: Luminescence (Fluorescence & Phosphorescence) Molecular optical spectroscopy: Vibrational spectroscopy (Infrared & Raman) Hour Exam #1 Overview of electroanalytical methods Introduction to separations Gas chromatography Liquid chromatography Capillary electrophoresis Mass spectrometry: Methods of generating ions Mass spectrometry : Methods of detecting ions Applications of mass spectrometry I: Atomic and molecular analysis Applications of mass spectrometry II: Biomolecular analysis Hour Exam #2 Materials characterization via surface spectroscopies : XPS, Auger, etc. Materials and biomaterials analysis via scanning probe microscopy: AFM, STM, etc. Skoog, Chapter 7 Skoog, Chapters 8‐10 Skoog, Chapter 13 Skoog, Chapter 14 Skoog, Chapter 15 Skoog, Chapters 16‐18 Skoog, Chapters 22‐25 Skoog, Chapter 26 Skoog, Chapter 27 Skoog, Chapter 28 Skoog, Chapter 30 Skoog, Chapter 11 and Chapter 20 Skoog, Chapter 11 and Chapter 20 Skoog, Chapter 11 and Chapter 20 Skoog, Chapter 21 A‐D Skoog, Chapter 21 G Skoog, Chapter 21 F PS 2 due Assign PS 3 PS 3 due/ Assign PS 4 PS 4 due Assign PS 5 Fall Break PS 5 due No class Nanotechnology: Characterization & applications of nanomaterials The fruits of the analytical chemists’ labor: Genomics, transcriptomics, proteomics, and metabolomics Non‐MS‐based protein analysis: Western blot, Immunoassays, and Surface plasmon resonance Bailey’s choice Reading Day Comprehensive Final Exam Skoog, Chapter 21 E‐1 Grading scale: I do not have a set grading scale, but rather will adjust to accurately reflect the performance of the students in the course. That being said, a standard 90‐80‐70‐60 scale is GUARANTEED. Furthermore, I do use plus and minus grades. I also reserve the right to adjust grades to reflect natural breaks in the student distribution. In that case, the highest cluster will receive As, the next Bs, etc. with pluses and minuses assigned in a fair manner. The minimum GUARANTEED grading scale is given below: 100‐97.001 A+ 97.000‐92.001 A 92.000‐90.00 A‐ 89.999‐87.001 B+ 87.000‐82.001 B 82.000‐80.000 B‐ 79.999‐77.001 C+ 77.000‐72.001 C 72.000‐70.000 C‐ 69.999‐67.001 D+ 67.000‐62.001 D 62.000‐59.999 D‐ Deadlines and missed assignments/exams: Problem sets are due in class on the due date. Late problem sets will NOT be accepted, resulting in a grade of zero, unless an emergency absence is approved. If you know you will miss a class period when a problem set is due, you should turn in the assignment in advance of the absence. Late problem sets will only be accepted in the case of excused absences where the instructor is provided with a note from a medical doctor, emergency Dean, or a photocopy of an obituary. These cases will be handled on an individual basis. Exams will be administered at the listed time period only. Make up exams will not be administered under any conditions, even in the case of an excused absence (see above for instructor verification of excused absences). If you miss an exam due to an excused absence it will be assumed that you would have performed at the same level relative to your classmates as you have in the other semester exams. Therefore your average on other exams, relative to the entire class average, will be entered for the missed exam. If lighting strikes twice and excused absences keep you from taking two exams, you are encouraged to drop the course. Exams missed due to unexcused absences will result in a score of zero— drop the course. If a conflict exists with a final exam period, the situation will be handled according to University policy and on an individual basis. Academic Integrity and test accessories: All assignments are expected to be representative of your own effort and understanding of the course material. Students are assumed and encouraged to work together on problem sets, however, each student must turn in their own work and NOT a copy or substantially a copy of another student’s work. Any form of cheating on exams will automatically result in a score of zero. Additionally, students may also be subject to additional action in accordance with Part 4 of the University’s Student Code. Calculators are the only approved electronic devices allowed during exams. Laptop computers or any other device with spreadsheet or data transmitting functions are expressly prohibited. Each student may use one and only one piece of paper during each exam onto which they can write or print anything they please. ...
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- Spring '08
- Chemistry, Optical Spectroscopy, Roger Adams Laboratory Office, Molecular optical spectroscopy, human disease.