Term
| Cells are made up of four families of carbon compounds |
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Definition
| Sugars, fatty acids, amino acids, nucleotides |
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Term
| 4 types of amino acids based on their side chains |
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Definition
| acidic, basic, uncharged polar, nonpolar |
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Definition
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| Amino Acids are linked together in |
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| Proteins are long _____ of ______ |
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| Proteins are always written with the ___ terminus on the left and the ___ terminus to the right |
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Term
| The negative log of the acid ionization constant (pKa) is defined as |
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Definition
| the ability of an ionizable group of an organic compound to donate a proton (H+) in an aqueous media |
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Term
| When a protein is in a solution where the pH is below the pKa of a particular amino acid |
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Definition
| residue in that protein, the amino acid is protonated |
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Term
| pH of human body is around |
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Definition
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Term
| When the pH is lower than the pKa |
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Definition
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Term
OH is ______and makes amino acids that contain them _______. OH group can be phosphorylated
OH group (Ser, Thr).... |
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Definition
| reactive, reactive. , mechanism for regulation of activity, site for attachment of carbohydrates – called O-linked |
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Term
| Uncharged polar side chains |
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Definition
| Asparagine, glutamine, serine, theronine, tyrosine |
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Term
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Definition
| alanine, valine, leucine, isoleucine, proline, phenylalanine |
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Term
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Definition
| almost always) first amino acid translated (AUG codon = Met) |
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Term
Cys can form _____ bond by ________
( -C-S-S-C- ) |
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Definition
| covalent disulfide, oxidation |
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Term
| Protein folding depends on _________, interactions of ________ and _________ ____. |
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Definition
| primary structure, polar side chains, non polar side chains. |
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Term
| hydrophobic core regions contains________. _____________ on the outside of the molecule can form ________ _______ to water. They have a folded _________ in an _______ ____ |
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Definition
| non polar side chains. Polar side chains, hydrogen bonds. Conformation, aqueous environment. |
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Term
| Modifications to ________ also affect protein interactions – often ________ modifications made |
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Definition
| amino acids, post translation |
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Term
| Proteins are not long linear molecules of amino acids. The structure is determines by- |
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Definition
| Ionic bonds, hydrogen bonds, van der waals interactions, hydrophobic forces. |
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Term
| Levels of protein structures |
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Definition
| Primary- amino acids, secondary- alpha or beta helix sheets, Tertiary- overall shape on an individual molecule, quaternary- combination of molecules together. |
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Term
C-reactive protein Five identical subunits -
Form donut-
Functions- |
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Definition
one polypeptide chain each
Bind to one another, two sides with two different activities, in immune defense. |
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Term
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Definition
Right handed helix
Hydrogen bonds between backbone carbonyl and NH of residue N+4
Dipole with positive N-terminal
Amphipathic |
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Term
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Definition
| fold of intestinal fatty acid binding proteins. |
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Term
| Proteins share similar structures domains = |
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Definition
| sequence of amino acids with particular structure/function |
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Term
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Definition
| – depicted as something on top of backbone |
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Term
May add domains-
Changes in _______ and ______(natural selection) change structure and function somewhat |
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Definition
over course of time (often see duplications)
nucleotides and amino acids |
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Term
May add domains-
Changes in _______ and ______(natural selection) change structure and function somewhat |
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Definition
over course of time (often see duplications)
nucleotides and amino acids |
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Term
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Definition
| binds polyproline regions (---P-P-P-P----) |
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Term
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Definition
| binds phosphorylated tyrosine residues (---Yp---) |
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Term
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Definition
| - phosphorylates proteins (can be a tyrosine kinase or a ser/thr kinase) or lipids |
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Term
| a protein with multiple domains and how they might function together |
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Definition
| Kinase domain and a tyrosine- phosphat removal, loosens structure. |
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Term
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Definition
| which binds a phosphorylated tyrosine, another molecule can bind |
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Term
| Binding also occurs through |
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Definition
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Term
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Definition
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Term
| This binding activates the |
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Definition
| orange kinase domain to phosphorylate a tyrosine residue |
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Term
| Phosphorylation of Tyr residue causes |
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Definition
| loop to move causing full activation of kinase |
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Term
| Kinase can now phosphorylate |
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Definition
| tyrosine to self-activate |
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Term
| How Protein Structure regulates activity |
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Definition
| - temporal and spatial activation (when and where to act) depending on the structure |
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Term
| Protein structure Specificity of activity - |
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Definition
| act on the “correct” substrates (with whom to act) based on structure |
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Term
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Definition
| amphipathic (amphiphilic) has a hydrophobic head and hydrophylic tail |
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Term
| Phospholipids will spontaneously form lipid bilayer in ______ ________. The bilayer structure has ________ embedded |
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Definition
| aqueous environment. proteins |
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Term
One hydrocarbon tail is usually _________
why is the Length important?
Phase transition? -
________ and_______ important |
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Definition
unsaturated, which allows for mobility.One hydrocarbon tail is usually unsaturated (allows for mobility)
allowing for specialized membrane structures to form.
liquid to crystalline dependent on temp and lipids. Hydrophobic forces, van der waals |
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Term
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Definition
Phosphatidylcholine (PC)
Phosphatidylethanolamine (PE)
Phosphatidylserine (PS) - **negative charge
Sphingomyelin |
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