The first of a two semester course that will outline the structure, function, and chemical properties of biological molecules. Topics will include protein function, enzyme kinetics, bioenergetics, membrane transport, cell signalling pathways, DNA information technology, and central intermediate metabolism. Student majoring in Biology or Chemistry must earn a grade of C or higher. Cross-listed as CHEM 420. Prerequisites: BIOL 110 and CHEM 310. CHEM 312 is strongly encouraged.
Prerequisite(s) / Corequisite(s):
BIOL 110 and CHEM 310
Course Rotation for Day Program:
Most current editions of the following:
Most current editions of the following:
Lehninger Principles of Biochemistry
By Nelson, David M. & Michael M. Cox (Freeman) Recommended
Fundamental of Biochemistry: Life at the Molecular Level
By Voet, Donald, Judith G. Voet & Charlotte W. Pratt (Wiley) Recommended
By Berg, Jeremy M. & Tymoczko, John L. & Stryer, Lubert (Freeman) Recommended
To understand the structure and function of basic biomolecules in the cell as well as the macromolecules they form.
To understand the role buffering plays in chemical reactions of the cell.
To understand protein-substrate interactions and how to characterize these interactions.
To understand enzyme function and activity and characterize the type of enzyme by use of kinetics.
To understand the dynamic role biological membranes play in transport and investigate their coordination in biosignalling pathways.
To calculate free-energy changes and recognize the various types of biochemical reactions.
To examine the catabolic and anabolic reactions of central intermediate metabolism and apply these principles to the understanding of cellular status.
Explain the various roles of water in biological systems.
Utilize the Henderson-Hasselbach equation to determine buffering capacity of various biological molecules, what is salt and what is acid, and finally apply it to find the pH of a solution.
Model the buffering of various salts via a titration curve.
Identify and draw all 20 common amino acids based on the ionization state of their dissociable side chains.
Identify and draw peptides structures as well as their characteristic titration curves.
Identify the various secondary, tertiary, and quanternary structures and motifs associated with protein folding and function; be able to describe the intramolecular interactions these structures have between each other and how they dictate protein function.
Understand the basis for different protein purification techniques, analysis, and identification methodologies.
Describe the different models for protein-substrate interaction and the techniques used to analyze and model the binding of substrate.
Identify and describe the various categories of enzyme catalyzed reactions utlizing Michaelis-Menten kinetics and the double-reciprocal plot; understand and recognize the three forms of inhibition and model using the double reciprocal plot.
Name and draw various mono- and disaccharides; understand the importance of carbohydrates beyond a fuel source in glycobiology.
Draw and name the basic nucleotides; describe the formation of the DNA double helix and the properties of the nucleotides that allow for its characteristic shapes and bonding patterns.
Understand the concepts and techniques of DNA-based information technologies including: polymerase chain reaction, microarrays, DNA library formation, and the application and mechanisms of restriction endonucleases.
Name and draw the structure of common fatty acids and lipids found in membranes.
Understand the action of phospholipases on lipids.
Describe the fluid mosaic model of the membrane and understand the dynamics of the phospholipid bilayer including the proteins inserted in the membrane.
Understand how molecules are moved from one side of the membrane to the other utilizing the various transport systems.
Be able to describe and draw several classical signalling pathways including pathways based on hormonal signalling, GTPases, and kinase amplification pathways.
Be able to calculate the standard free energy change of a biochemical reaction and identify the type of biochemical reaction that took place.
Be able to name all enzymes, draw all intermediates, and name all cofactors in central intermediate metabolism including glycolysis, gluconeogenesis, and the citric acid cycle.
Understand the significance of central intermediate metabolism as being both catabolic and anabolic systems for the cell.
Understand the process of storing and degrading glucose in the form of glycogen in the liver and muscle tissue of mammalian systems.
Understand the role of pentose phosphate pathways and be able to draw and name all enzymes and intermediates in the pathway.
Understand the checkpoints of regulation and the types of regulation in central intermediate metabolism that dictate whether the system in catabolic or anabolic.
o Water, pH, and buffers
oAmino acids, peptides, and proteins
o Protein function and structure
oNucleotides, nucleic acids, and DNA information technologies
oLipids, biological membranes, transport, and biosignalling
o Bioenergetics and biochemical reaction types
oCentral Intermediate Metabolism: Glycolysis, gluconeogenesis, pentose phosphate pathway, and the citric acid cycle including structures, enzymes, and regulation of indicated pathways
Recommended maximum class size for this course: 25
NOTE: The intention of this master course syllabus is to provide an outline of the contents of this course, as specified by
the faculty of Columbia College, regardless of who teaches the course, when it is taught, or where it is taught. Faculty members teaching this
course for Columbia College are expected to facilitate learning pursuant to the course objectives and cover the subjects listed in the topical
outline. However, instructors are also encouraged to cover additional topics of interest so long as those topics are relevant to the course's
subject. The master syllabus is, therefore, prescriptive in nature but also allows for a diversity of individual approaches to course material.