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| structural protein; has trihelical fiber that makes up most of the extracellular matrix of connective tissue; provides strength and flexiblity |
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| structural protein; most important role is to stretch and recoil like a spring |
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| structural protein; intermediate filament proteins in epithelial cell; makes up hair and nails |
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| structural protein; composes microfilaments and thin filaments in myofibrils. Most abundant protein in eukaryotic cells. Has positive and negative end to allow motor proteins to travel along it like one way street |
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| structural protein; makes up microtubules important for chromosome separation in mitosis and meiosis and intracellular transport with kinesin and dynein |
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| primary motor protein that interacts with actin and makes up the thick filament in a myofibril. each subunit is a single head and neck that moves during the power stroke of sarcomere contraction |
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Definition
associated with microtubules. Each has two heads, one of which is always attached to the microtubule.
Kinesins play a key role in aligning chromosomes during metaphase.
Dyneins are involved in sliding movement of cilia and flagella.
Kinesins and Dyneins move down the microtubules in opposite directions |
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| bind a specific substrate, either to sequester it in the body or hold its concentration at steady state |
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| What are cell adhesion molecules and what are the three major families? |
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Definition
Cell adhesion molecules allow cells to bind to other cells or surfaces
-cadherins
-integrins
-selectins |
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| cell adhesion molecule; mediate calcium dependent cell adhesion and often hold together similar types of cells |
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| cell adhesion molecule; have two membrane-spanning chains and permit cells to adhere to proteins in the extracellular matrix. Some also have signaling capabilities. important for WBC migration and anchoring to epithelia |
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| cell adhesion molecules; bind to carbohydrate molecules that project from other cell surfaces. Expressed in WBCs and endothelial cells lining blood vessels to grab WBCs for inflammation |
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| What are antibodies and what do they do? |
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Definition
aka immunoglobulins, made of two heavy and two light chains. Antigen binding region found at tips of the 'Y' and is specific to one antigen.
-neutralize antigen
-opsonize pathogen (mark for destruction)
-Agglutinate, clump together, on the antigen with other antibodies to be phagocytized |
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| unregulated pores that allow molecules to cross membrane down their gradient |
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| regulated by the membrane potential and open within a range of potential |
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| the binding of a specific substance to the channel causes it to open or close |
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| participate in cell signaling through extracellular ligand binding which activates a second messenger cascade |
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| G protein-coupled receptors |
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Definition
| contain 7 membrane spanning alpha helices. The ligand binding to the receptor increases the proteins affinity for a heterotrimeric G protein (GDP and GTP) which activate the receptor and cause a second messenger cascade |
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| separates proteins based on size and shape using their charge to move them. |
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| polyacrylamide gel electrophoresis (PAGE) separates proteins in their native states based on size and charge. proteins can be recovered |
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| sodium dodecyl sulfate polyacrylamide gel electrophoresis denatures the proteins and separates them based on mass alone. |
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| uses a gel with a pH gradient. As the proteins travel along they will become protonated and deprotonated. Once a protein reaches its pI and becomes neutral it will stop moving. Separates on basis of pI |
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Definition
| uses a stationary phase and mobile phase. The sample will move through the column based on its affinity for the stationary and mobile phases |
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| column is filled with beads that separate samples based on polarity and somewhat on size |
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| ion-exchange chromatography |
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Definition
| beads coated with a charge substance are used so they will bind something with the opposite charge. After all the sample as been run it can be eluted by washing the column with a salt gradient |
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| size-exclusion chromatography |
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Definition
| uses beads that contain pores of varying sizes. Smaller proteins will be able to access more pores making them move more slowly. Larger proteins will have access to fewer pores and will run more quickly. |
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| uses bound receptor or ligand on the column beads to bind protein of interest. eluent disrupts binding of protein to column but can sometimes remain bound to the protein and be difficult to remove |
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| uses cleavage to sequence proteins of up to 50 to 70 amino acids |
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| How can you determine the concentration of a protein? |
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Definition
| UV spectroscopy, colorimetric changes from assays ie Bradford protein assay |
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