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Final Exam Study Guide - Principles of Biology | BSCI 105, Exams of Biology

Material Type: Exam; Professor: Keller; Class: PRIN BIOL I; Subject: Biological Sciences Program; University: University of Maryland; Term: Fall 2010;

Typology: Exams

2010/2011

Uploaded on 10/11/2011

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Download Final Exam Study Guide - Principles of Biology | BSCI 105 and more Exams Biology in PDF only on Docsity! Biology Final Exam Study Guide Exam One 1. Characteristics of living things: o Organization o Self Regulation o Reproduction o Energy Consumption o Evolution o Interaction with Environment. 2. Unpaired valence electrons determine the reactivity of an element. 3. Atoms that complete their outer shells by sharing electrons are said to have covalent bonds. 4. These properties of water are a result of hydrogen bonding: o Cohesion o Adhesion o Surface Tension o Low Density as Solid 5. Many biological reactions involve polymerization of molecules by dehydration synthesis. Dehydration synthesis makes bonds and hydrolysis breaks bonds. 6. Amino acids and organic acids are considered acids because they can release a hydrogen ion in solution and both contain the carboxyl functional group. 7. Polysaccharides are polymers of monosaccharides linked by a glycosidic bond. 8. All lipids are hydrophobic. 9. Phospholipids form lipid bilayers because they are amphipathic. 10. Variation in the nitrogenous base of nucleic acids is the most important factor in their diversity and ability to encode information. 11. Parts of the endomembrane system: o Golgi Apparatus o Nuclear Envelope o Endoplasmic Reticulum o Lysosomes o Vacuoles o Vesicles o Plasma Membrane 12. Cells are able to change shape and move because of the dynamic sub-cortical cytoskeleton which is composed of a network of microfilaments. 13. Desmosomes form a strong connection between neighboring cells in tissues subjected to substantial stress, such as cardiac muscle. 14. According to the fluid mosaic model, integral membrane proteins may be mobile within the membrane. They are not cytoplasmic, loosely associated with the membrane, anchored to the cytoskeleton, or glycoproteins. 15. If you dropped a carrot in thick, sugary corn syrup, it would become lighter. 16. Ion channels are integral proteins that facilitate diffusion across a membrane because they provide a hydrophilic passage through the membrane. 17. Energy for active transport can come from direct or indirect sources. 18. Signaling between nearby cells in a tissue is called paracrine signaling. 19. G-protein coupled receptors induce activation of G-proteins through exchange of GDP for GTP. 20. Features of receptor tyrosine kinases: o Ligands are mostly growth factors o Activation requires dimerization o Receptor autophophorylation 21. Isomers are structural variations of molecules sharing the same component elements. 22. Highly stable protein tertiary structures involve covalent bonds between sulfhydryl functional groups. 23. The cell nucleus contains chromatin, which is a mixture of DNA and protein. 24. Plant cells are supported and separated by thick cell walls, yet cytoplasm of adjacent cells is connected by plasmodesmata. 25. If a solution outside of a cell has more solutes and results in water leaving the cell, it is said to be hypertonic relative to the cell. 26. Transport proteins that mediate cotransport of two different molecules into a cell are termed symport. 27. Every receptor binds a specific signaling molecule, called a ligand. 28. DAG, IP3, calcium ions, and cAMP are examples of secondary messengers. 29. Cells that use G-protein coupled receptors are able to recognize different ligands because of variation in receptors expressed and variation in target enzymes activated by G-proteins. They can have different responses to the same ligand because each receptor is different. Each receptor uses the ligand’s signal in the specific way that it needs to use it and therefore generates a different response. 30. Signal transduction is the process in which cells decode a received signal in order to generate a response specific to that signal. 31. The coiled parts of the protein are a secondary structure. Each coil represents an alpha helix. The entire polypeptide is a tertiary structure. Three types of chemical interactions that might stabilize the structure of this protein are hydrogen bonds, disulfide bridges, and Van der Waals forces. 32. The major function of the mitochondria is to create energy and ATP for the cell. The network of supporting molecules outside the cell membrane is the extracellular matrix. The difference between the rough ER and the smooth ER is that the rough has ribosomes because it is involved in the assembly of ribosomes and the smooth does not. 33. A phosphate group is a highly polar group on the phospholipid head. Amino groups are present in all amino acids but not organic acids. Hydroxyl groups are polar groups characteristic of alcohols and sugars. 34. Receptor mediated endocytosis is the internalization of circulating cholesterol by a cell at clatherin coated pits. Ribosomes are associated with the rough ER. A hypothesis is a question you can test. Osmosis is the movement of water across a membrane. Prokaryotes don’t have an endomembrane system. Active transport is moving solutes against a concentration gradient.
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