Reference no: EM133458558

Chapter 1

1. Describe and differentiate features of living organisms
2. Summarize the Structure and function of the parts of the cell
3. Identify and describe the Roles of small and large biomolecules
4. Discuss Energy transformation in living organisms
5. Identify and explain Regulation of metabolism & catalysis
6. Describe the importance of the Coding of genetic information in DNA
7. Discuss how the Role of mutations & selection in evolution

Chapter 2

1. Describe the kind of interactions that occur between molecules
2. Discuss why water is a good medium for life
3. Identify why nonpolar moieties aggregate in water
4. Describe how dissolved molecules alter properties of water
5. Explain how weak acids and bases behave in water
6. Identify how buffers work and why we need them
7. Summarize how water participates in biochemical reactions

Chapter 3

1. List and name the 20 amino acids that commonly occur in proteins and classify them according to chirality, polarity, size, and charge.
2. Describe the bonds and forces (peptide, disulfide, and hydrogen bonds; hydrophobic, dipole-dipole, van der Waals and electrostatic interactions) that contribute to the conformation of proteins and the interaction of proteins with other biomolecules.
3. List & match the ONE letter codes identifying amino acids, including selenocysteine with their respective amino acid.
4. Define and discuss the following terms: peptide bond, peptide backbone, N-terminus, C-terminus, disulfide bridges, α-helices, β-sheets, β -strands, β -turns.
5. Discriminate between primary, secondary, tertiary, and quaternary protein structure.
6. Integrate the forces in (#2) above with the structure considerations in (#5) above.
7. Propose reasons why folded proteins have a finite number of conformations.
8. Compare and contrast the difference between conservative and non-conservative amino acid substitutions and be able to identify and assess invariant positions.
9. Using the information in #s 6, 7, 8, and 9, evaluate the relationship of structure to function for the proteins myoglobin and hemoglobin.
10. Explain the formation of coiled-coils and protein fibrils and compare and contrast structure-function of fibrillar proteins to globular proteins.
11. Define and explain the role of membrane proteins.
12. Compare and contrast peripheral versus integral membrane proteins.
13. List, explain, and evaluate the role of each of the terms below with regard to membrane structure: phospholipids, membrane spanning α-helices, membrane β-barrels, membrane anchors (hydrophobic amino acids, myristic acid, prenyl groups, and glycophosphatidylinositol (GPI) anchor).
14. Use the following diseases as examples of how abnormal protein structure causes disease and be able to propose the mechanisms of abnormal function: Sickle cell anemia (β-globin), Alzheimer's disease (β-amyloid), Crutzfeldt-Jacob/ Kuru/Mad Cow disease (prion proteins), Huntington disease (poly-glutamine repeat diseases), Parkinson disease (α-synuclein), osteogenesis imperfecta (Collagen), Erlers Danlos Syndrome (Collagen).

Chapter 8

1. Summarize the central dogma of molecular biology, and cite exceptions to the original model.
2. Compare and contrast prokaryotic and eukaryotic gene structure.
3. Compare and contrast the structure of DNA and RNA, explaining the difference between the constituent bases, sugars, nucleosides and nucleotides.
4. Identify and draw the structures of DNA and RNA bases plus nucleosides, nucleotides and polynucleotides including ribose and deoxyribose
5. Compare and contrast the different types of RNA.
6. Integrate the terminology and defining structural features that distinguish different classes of nucleotide metabolites (such as purine vs. pyrimidine, bases vs. nucleoside vs. nucleotide, and ribo- vs. deoxyribo-).
7. Describe the double-stranded, helical, and antiparallel chain structure of DNA and how it relates to the processes of DNA replication, transcription, recombination and repair.
8. Describe how DNA and DNA processes can be used as therapeutic targets (e.g. anticancer and antibacterial drugs).
9. Use the genetic code to predict the amino acid sequence of a protein for a given nucleic acid sequence and demonstrate how nucleotide mutations can lead to alterations in the primary structure of a protein.

Chapter 9

1. Describe how recombinant DNA technology is used to clone and express genes.
2. Define clone, restriction enzyme, cDNA, genomic DNA & DNA libraries. Discuss different DNA libraries and their uses
3. Discuss the purpose & methods of molecular & DNA cloning and identification of bacterial colonies containing specific DNA sequences
4. Explain the process of the Polymerase Chain Reaction (PCR) as well as list modified PCR & state their different uses
5. Describe protein expression & purification and the role of mutagenic studies
6. List, discuss, and evaluate the major techniques used in separating proteins, including: solubility; size, dialysis, sodium dodecyl sulfate polyacrylamide electrophoresis (SDS-PAGE); charge- ion exchange chromatography, size and charge- (two-dimensional gels); specific ligand binding - affinity chromatography, antigen-antibody recognition (Western Blot, ELISA); mass spectrometry of peptides and proteomics.
7. Define DNA microchips and the various ways on how it can be used
8. Discuss the process and uses of electrophoresis, Southern blotting, Northern blotting, Western blotting, RFLP, DNA sequencing, DNA microarray & Fluorescence In Situ hybridization (FISH)
9. Explain the Sanger Method and be able to read a sequence from a gel
10. Describe the various ways that SNPs are being used
11. Summarize the Human genome project