13 Jun Bio 202 – What is a “typical” cell size for bacteria
Question
Summer 2014 Cell Bio 202
These are “study questions”that cover the first week of class. They cover all the material emphasized, and the content of the first portion of exam 1. If you can answer these without help, you should do well on that part of the exam.
What is a “typical” cell size for bacteria? For eukaryotes?
What cell structures are characteristic of eukaryotes vs. prokaryotes? Animals vs. plants? What features are present in all cells?
What is cell theory?
How can we see cells? Individual cells? Cells in solid tissues?
What are the different types of light microscopy, how do preparations for each differ, and what are the advantages or uses of each?
What limits the features observable in LM? How can we identify smaller object?
How are solid tissue samples prepped for LM? For TEM?For SEM? What are the differences between LM and TEM tissue preparations? (steps, dimensions, staining?)
How does confocal LM differ from “standard” (including fluorescence) LM, in terms of results?
Why does EM have higher resolution than LM?
How is SEM different from TEM? What are the advantages of each?
How can you obtain 3D descriptions of cells with LM? With EM?
What kinds of magnifications (LM or EM) are needed to see or describe/measure various cell features?
What are archaea?
What are the characteristic features and general purposes of nuclie? Rough ER? Smooth ER? Golgi? Lysosomes? Vesicles? Cytoskeleton? Mitochondria?
What are exocytosis and endocytosis?
What are the major components of cell?
How do most macromolecules interact with each other?
What are noncovalent interactions? How are they affected by their environment?
How are macromolecules made? What kind of reaction? How are they broken down?
– What are the reactions that make macromolecules and other needed molecules in cells?
– What are the dual purposes of catabolism?
Why are polysaccharides made in cells?
What are organic molecules, and what their source?
How is energy obtained from organic molecules? What are the forms of that energy? How is each type stored? How is each type of energy used in the cell?
What are activated carriers? What changes in them (in ADP and NAD+) to make them activated?
What kinds of bonds couple phosphates in ATP? What are the phosphates used to do in cells?
What are the structural and functional differences between NADH and NADPH?
What is the function of Coenzyme A in cells?
What is the general structure of the building blocks of proteins? How are they combined, and what kind of bond do they form?
What are the classes of amino acids? Be able to identify the class of any AA from its structure.
What are the functional differences of the AA’s in terms of the interactions in which they can participate?
What are the types of H-bonds that can occur in a polypeptide?
Which ones are used to make secondary structures?
What are the differences between alpha and beta structures? The similarities?
What makes a polypeptide a protein?
What is the overall arrangement of most proteins? What interactions are present in different parts? How does that influence the strength of the interacitons?
– How is a membrane-spanning protein different?
How can alpha helical structure be used to tightly couple two proteins?
Where are the sidechains in helices and in sheets? Mainchain bonds?
What are unstructured domains, and why do some proteins have them?
How do proteins fold (as well as we know the process)?
What makes them unfold? What experimental treatment is usually used, and why that one?
What kind(s) of secondary structure is found in filamentous proteins? Where are filamentous proteins found? What kinds of properties can they have?
What is meant by alternative structures for proteins?
What are protein families, and why do they exist?
What is a ligand? How is it different from a substrate? How does it interact with a protein?
What is an allosteric enzyme inhibitor, and how is it different from a substrate or product?
What is a disulfide bond, where does it form, and what is its purpose?
What is the purpose of an antibody? How is an IgG organized (components and interactions)?
How does an antibody bind a molecule? What is the bond molecule called, specifically for an antibody?
Which parts of the IgG determine its specificity?
What do enzymes do to a reaction energetics (e.g., in an energy diagram)?
What are general mechanisms of enzyme action?
What is the difference between an enzyme’s binding site and its active site? How are they related?
What is a cofactor for an enzyme or other protein?
How does feedback inhibition work in a metabolic pathway? What kind of inhibition is it? (allosteric)
What is a protein kinase? What is its effect on the structure and function a protein? How is its action reversed?
Are there kinases that are not protein kinases? What do they do?
What kinds of covalent modifications can occur to proteins?
What are G-proteins? What do they do? How are they activated and deactivated?
If motor proteins can move without input of energy, what is ATP hydrolysis used for?
How is chromatography different from electrophoresis?
What are the major types of column chromatography, and what physical principle or interaction is each based on?
What is SDS gel electrophoresis used for? What are the chemicals that are added to protiens for SDS gels, and what are their purposes?
What is the nature of the information gained by X-ray crystallography and structural NMR? What are the limitations of each method?
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