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Ninfa/Ballou/Benore is a solid biochemistry lab manual, dedicated to developing research skills in students, allowing them to learn techniques and develop the organizational approaches necessary to conduct laboratory research. Ninfa/Ballou/Benore focuses on basic biochemistry laboratory techniques with a few molecular biology exercises, a reflection of most courses which concentrate on traditional biochemistry experiments and techniques. The manual also includes an introduction to ethics in the laboratory, uncommon in similar manuals. Most importantly, perhaps, is the authors' three-pronged approach to encouraging students to think like a research scientist: first, the authors introduce the scientific method and the hypothesis as a framework for developing conclusive experiments; second, the manual's experiments are designed to become increasingly complex in order to teach more advanced techniques and analysis; finally, gradually, the students are required to devise their own protocols. In this way, students and instructors are able to break away from a "cookbook" approach and to think and investigate for themselves.
Suitable for lower-level and upper-level courses; Ninfa spans these courses and can also be used for some first-year graduate work.
Fundamental Laboratory Approaches for Biochemistry and Biote
Chapter 1: Getting Started in Scientific Research. 1.1 The Difference Between Experiments and Demonstration. 1.2 Philosophy and Design of Experiments. 1.3 Designing Informative Experiments. 1.4 Ethics in Science. 1.5 Keeping a Laboratory Notebook. 1.6 Laboratory Reports. 1.7 Presentation and Analysis of Data. 1.8 The Minisymposium. Chapter 2: Basic Procedures in the Biochemistry Laboratory. 2.1 Laboratory Safety. 2.2 Special Safety Procedures Are Required for Using Radioactive Materials and Operating the Autoclave. 2.3 Measurement of Weights, Volumes, and pH. 2.4 Various Instruments Used. 2.5 Other General Techniques. 2.6 Solutions and Dilutions. 2.7 Buffers and pH. 2.8 Appendix Calculating Titration Curves for Polyprotic Acids and Other Multiple Binding Site Receptors. 2.9 Equipment Used in This Course. Chapter 3: Spectroscopic Methods. 3.1 Introduction. 3.2 Design and Properties of Spectrophotometers. 3.3 Effects of Spectral Bandpass and Stray Light. 3.4 Recording Spectrophotometers. 3.5 Fluorescence Spectroscopy. 3.6 Chromogenic and Fluorogenic Reactions Used for Analysis. 3.7 Other Spectroscopic Techniques. 3.8 Mass Spectrometry (MS). Experiments 3-1 to 3-3. Reagents Needed for Chapter 3. Chapter 4: Quantification of Protein Concentration. 4.1 Purposes of Protein Quantification. 4.2 Factors to Consider in Choosing an Assay. 4.3 Non-Colorimetric Procedures for Quantification of Proteins. 4.4 Colorimetric Procedures for Quantification of Proteins. Experiment 4-1. Reagents Needed for Chapter 4. Chapter 5: Chromatography. 5.1 Introduction. 5.2 Gel-Filtration (Size Exclusion or Gel-Permeation) Chromatography. 5.3 Affinity Chromatography. 5.4 Ion-Exchange Chromatography. 5.5 Hydrophobic Interaction Chromatography. Experiments 5-1 and 5-2. Reagents Needed for Chapter 5. Chapter 6: Gel Electrophoresis of Proteins. 6.1 Process of Electrophoresis. 6.2 Polyacrylamide Gels. 6.3 SDS-Polyacrylamide Gel Electrophoresis (SDS-PAGE) of Proteins. 6.4 Detection of Proteins in SDS-Polyacrylamide Gels. 6.5 Applications of SDS-PAGE. Experiments 6-1 and 6-2. Reagents Needed for Chapter 6. Chapter 7: Overview of Protein Purification. 7.1 Introduction. 7.2 Development of a Suitable Assay Procedure. 7.3 Time, Temperature, and Yield. 7.4 Selection of the Best Source Material. 7.5 Solubilization of the Protein. 7.6 Initial Steps of Purification. 7.7 Developing a Series of High-Resolution Chromatographic Steps. 7.8 Methods Used to Change Buffer and Concentrate Protein Samples. 7.9 A Logical Series of Steps. 7.10 Storage of the