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17 Cards in this Set
- Front
- Back
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Bonds important primary, secondary, tertiary, quanditrary
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1: peptide
2: hydrogen bonds make the chain fold into alfa-helix or beta-sheets 3: side group interactions, 3D structure, disulphide bonds, electrostatic/hydrophobic interactions 4: same as 3, but association of two or more tertiary structures |
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protein domain
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a part of a protein chain that forms independent, stable structures. specific tertiary structures with particular functions
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chaperons
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protein that helps an other protein to fold into right conformation and then detaches
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operon
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a functioning unit of genomic material containing a cluster of genes regulated by one single promotor. several genes must be co-transcribed AND co-regulated to define a operon, in both eu and pro
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structural proteins
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form mechanical support for the cells&tissues. Ex) actin, collagen, keratin
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Enzymes
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proteins with catalytic capacities. formation and breakage of covalent bonds
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motor proteins
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facilitates mobility of organelles within the cell and of the cell itself
Ex) dynein, kinesin, myosin |
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transport proteins
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transport small ions/atoms
Ex) hemoglobin, transferrin |
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storage proteins
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storage of ions/small atoms
Ex) ferritin, casein, ovalbumin |
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signalling proteins
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carry signals from cell to cell
ex) insulin, |
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receptor proteins
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detect outer signals
ex) insulin receptors, rhodopsin receptor |
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regulatory proteins
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regulate the function of other proteins, or macromolecules (ex DNA) by binding to them
Ex) cyclins, chaperons, transcription factors |
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Antibodies
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binds to antibodies in highly specific manners.
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protein transport across the membrane is realized by
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protein translocators. the transported protein must first unfold
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protein transport via vesicles
realized by enables |
realized by transport vesicles. enables transport between the endomembrane system (ER and golgi) and from these out of the cell
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allosteric regulation
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binding of an effector molecule to an enzyme can inhibit or activate the enzyme
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protein degradation
degraded by binds to |
proteins degraded in the cytosol is degraded by PROTEASOME. If a protein binds to a UBIQUITIN the proteasome will open for it and degrade it into peptides
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