Outline of chemistry - Wikipedia

 

outline of biochemistry

A molecular simulation environment lets students explore the effect of molecular interactions on the biochemical properties of systems. Biochemistry is an introductory course, designed for both biology and chemical engineering majors. Learn about Open & Free OLI courses by visiting the “Open & Free features” tab below. Sep 19,  · Buy Schaum's Outline of Biochemistry, Third Edition (Schaum's Outlines) on hbpdfs.gq FREE SHIPPING on qualified orders/5(19). The following outline is provided as an overview of and topical guide to biochemistry. Biochemistry – study of chemical processes in living organisms, including living matter. Biochemistry governs all living organisms and living processes.


Biochemistry — Open & Free - OLI


A molecular simulation environment lets students explore the effect of molecular interactions on the biochemical properties of systems. Biochemistry is an introductory course, outline of biochemistry, designed for both biology and chemical engineering majors.

A consistent theme in this course is the development of a quantitative understanding of the interactions of biological molecules from a structural, thermodynamic, and molecular dynamic point of view. A molecular simulation environment provides the opportunity for you to explore the effect of molecular interactions on the biochemical properties of systems.

This course assumes that students have taken introductory chemistry, including basic thermodynamics, as well as introductory organic chemistry. An introductory biology course is not a prerequisite for the course, but students would benefit from some prior exposure to biology, even at the high school level. Required mathematical skills include simple algebra and differential calculus. The course begins with amino acids and transitions into protein structure and thermodynamics.

Protein-ligand binding is treated for both non-cooperative and cooperative binding using immunoglobulins and oxygen transport as examples. The enzymatic function of proteins is explored using serine and HIV proteases as examples. Enzyme kinetics is treated using steady-state kinetic analysis. Enzyme inhibition is treated outline of biochemistry, using HIV protease as a key example.

Carbohydrate and lipids are presented in sufficient depth to allow the student to fully understand major aspects of central metabolism. The discussion of metabolism is focused on energy generation, fermentation, and metabolic control. The course concludes with an extensive section on nucleic acid biochemistry. The focus of this section is to provide the student with sufficient background so that they are literate in the recombinant DNA technologies as they relate to protein production using recombinant methods.

After a treatment of molecular forces and solution properties, the course builds on molecular outline of biochemistry energetic descriptions of fundamental monomeric building blocks to develop a comprehensive understanding of the biological function of polymers and molecular assemblies at the outline of biochemistry and cellular level.

In addition to multiple case studies, the course concludes with a capstone exercise that leads students through the steps required to produce recombinant proteins for drug discovery. The major topics in the course are:. OLI system requirements, regardless of course :. Some courses include exercises with exceptions to these requirements, such as technology that cannot be used on mobile devices.

Watch the video to see how easily students can register with a Course Key. Free to independent learners. In-Depth Description The two main learning goals of the course are: Predicting how changes in structure affect function. Utilizing quantitative approaches to characterize structure-function relationships in biochemical systems. The major topics in the course are: Protein function, including oxygen transport, antibody function, outline of biochemistry, and enzyme catalyzed reactions.

Structure and function of carbohydrates and their importance in central metabolism. Lipids and biological membranes. Central aspects of metabolism and metabolic control.

Nucleic acid biochemistry, with emphasis on recombinant DNA technology. What students will learn By the time they finish this course, outline of biochemistry, students will learn about or be able to: Predict how changes in structure affect function. Utilize quantitative approaches to characterize structure-function relationships outline of biochemistry biochemical systems. Describe molecular orbitals.

Explain the molecular structure of Water. Identify hydrogen bond donors and acceptors. Predict the solubility of compounds in water, outline of biochemistry. Predict the strength of hydrogen bonds based on geometry. Provide a general overview of biochemistry based on component parts. Calculate the amount of an acid that is protonated at any given pH. Calculate the net charge on a molecule, at any pH.

Understand the relationship between the structure and acidity of an acid. Understand why solutions of weak acids resist pH changes. Module 4: Protein Structure Characterize molecular forces between antibody and antigen. Define the terms antigen, epitope, and hapten. Describe the process of antibody production by Outline of biochemistry. Determine the interaction of each amino acid with water.

Distinguish between primary, secondary, tertiary and quaternary structure. Draw the structure of all amino acids. Generate the primary sequence from sequencing data. Identify chiral centers on amino acids. Outline of biochemistry two amino acids into a dipeptide. Predict the result of treating a protein with different cleavage reagents. Predict the secondary structure of a residue from the Outline of biochemistry plot Relate thermodynamic forces to the stability of super-secondary structures.

Understand conformational entropy. Understand consequences of orbital overlap on the configuration of the peptide bond. Understand dominant enthalpic forces that stabilize proteins. Understand geometrical properties of linear polymers.

Understand the relationship between primary, tertiary, and quaternary structure of antibodies. Understand the role of hydrogen bonds in the stability of secondary structures. Understand the role of the hydrophobic effect in protein folding. Understand outline of biochemistry trans peptide bonds are more stable. Module 5: Binding Calculate amount of oxygen delivered from binding curves. Compare and contrast outline of biochemistry and heterotropic allosteric effectors.

Compare and contrast structures and binding curves of myoglobin and hemoglobin. Construct Hill plot and obtain KD and Hill coefficient. Describe how the amount of ligand bound is affected by the ligand concentration, both at low and high [L], outline of biochemistry. Determine the dissociation constant, KD directly from binding data. How allosteric activators and inhibitors affect binding. Interpret KD in terms of inter-molecular interactions. Relate the Hill coefficient to the molecular behavior of the system.

Understand role of allosteric modulators in oxygen delivery. Understand the molecular basis of oxygen transport. Module 6: Enzymes Be able to describe how the substrate concentration affects the rate of enzymatic reactions. Be able to obtain kinetic parameters from experimental data Calculate the rate enhancement due to transition state stabilization, outline of biochemistry. Compare and contrast the structure and mechanism of HIV protease outline of biochemistry serine proteases, outline of biochemistry.

Define steady-state conditions Describe the factors that contribute to stabilization of the transition state. Determine the dissociation constant for inhibitors. Distinguish between enthalpic and entropic stabilization of the transition state. Explain the difference between competitive and non-competitive inhibitors, outline of biochemistry.

Identify steps in viral replication that are suitable for inhibition with drugs. Interpret KI values within the context of molecular interactions. Understand the basis of substrate specificity. Understand the difference between reaction rates and KM and kcat. Understand the mechanism of serine proteases. Understand the relationship between substrate concentration and the rate of product formation.

Module 7: Protein Purification and Structure Determination Calculate and interpret specific activity. Determine quaternary structure of a protein. Develop a purification scheme.

Distinguish between molecular weight determination methods. Distinguish between the importance of amplitude and phase in X-ray structure determination. Understand the principles of separation techniques.

Module 8: Carbohydrates Compare and contrast the structure of glycogen and cellulose Describe how ring structures of saccharides are formed.

Describe the structure of bacterial cell walls, outline of biochemistry. Draw and name disaccharides, outline of biochemistry.

Draw the chemical structure of aldoses and ketoses. Identify the anomeric carbon in cyclic monosaccharides. Module 9: Lipids Calculate the energetics of membrane-protein interactions. Describe the thermodynamics of self-assembly of membranes. Draw the structure of Phospholipids.

 

 

outline of biochemistry

 

CHEM Online Biochemistry course outline. Medical Biochemistry is a four-credit hour course designed to lay the foundation for other basic and clinical medical sciences. The goal of this course is to learn the core concepts of biochemistry that apply to human health and disease and to cite specific examples of their application. A molecular simulation environment lets students explore the effect of molecular interactions on the biochemical properties of systems. Biochemistry is an introductory course, designed for both biology and chemical engineering majors. Learn about Open & Free OLI courses by visiting the “Open & Free features” tab below. The following outline is provided as an overview of and topical guide to biochemistry. Biochemistry – study of chemical processes in living organisms, including living matter. Biochemistry governs all living organisms and living processes.