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Protein, energy, etc
| Question | Answer |
|---|---|
| Protein: dry weight percentile | 50% |
| Proteios | primary importance |
| Protein: polymer of what | amino acid monomers |
| Protein: monomer or polymer or disaccharide | polymer |
| proteins contain: | carbon, hydrogen, oxygen, nitrogen, and may contain sulfur |
| types of protein | structural, storage, contractile, transport, and enzymes |
| Protein:structural | keratin(hair), collagen(skin), ligaments(connect bones) |
| Protein: Storage | for growth in seeds and eggs |
| contractile protein | contracts muscles, makes muscles work |
| transport protein | hemoglobin |
| enzyme protein | speeds up chemical reactions, critical for living organisms |
| protein: number of common amino acids | 20 |
| amino acid structure | central carbon, 2 hydrogen, carboxyl, amino, and r |
| r in amino acid | variable group, unique, gives special chemical properties |
| protein special chemical properties from: | variable group, side chain, R |
| Side chain other name | R, variable in amino acid |
| What is taken from protein in dehydration synthesis | hydrogen from amino and hydroxyl from carboxyl |
| amino acid endings | -ine |
| examples of typical amino acids | glycine, alanine, isoleucine, leucine |
| examples of odd amino acids | tryptophan, aspartic acid |
| protein synthesis syn | to join |
| dehydration synthesis reaction | polymerization reaction |
| what forms protein from amino acids | dehydration synthesis |
| what links amino acids | ribosomes |
| link between what | peptide between carbon and nitrogen |
| bond type between carbon and nitrogen | covalent |
| protein adds or removes water | removes |
| depeptide | two amino acids joined |
| polypeptide | long chain linked by peptide bonds |
| protein | one or more polypeptide chains precisely formed into three-dimensional shape needed for function |
| how can 20 types make most proteins | like the alphabet, the combination and sequence |
| what enables proteins to function | 3-d shape |
| what determines the shape of protein | number, type, and sequence of amino acids |
| how do proteins work | by recognizing and bonding with other molecules |
| how many protein groups | 2, fibrous and globular |
| what causes amino acids to create 3-d shape | side chains and synthesis |
| fibrous protein stable or unstable | stable |
| fibrous protein soluble or insoluble | insoluble |
| examples of fibrous protein | collagen muscles, keratin |
| fibrous protein structure | extended, strand like |
| globular protein structure | compact and spherical |
| globular protein soluble or insoluble | soluble |
| globular protein stable or unstable | unstable, easily misshapen |
| examples of globular protein | enzymes and antibodies |
| slight change can or can't in amino acid sequence affect protein's ability to function | can |
| what causes sickle-cell disease | substitution of one amino acid in hemoglobin |
| diseases formed by misfolded normal proteins | kuru, fatel weight loss in deer and elk |
| protein sensitive or not to environment | very sensitive |
| shape of protein maintained by what bonds | hydrogen? |
| hydrogen bonds | weak and fragile, broken by environmental factors |
| what environmental factors can denature protein | temp, pH, or salinity |
| example of denatured protein | egg being cooked, temp cause egg to become opaque |
| chemical reactions rate for life | fast, using enzymes |
| what causes reaction | colliding with enough energy, that bonds will break, atoms will rearrange, and bonds will form |
| factors that increase chemical reactions rate | higher temp, higher concentration, lower particle size, enzyme, |
| activation energy | energy needed to start a chemical reaction |
| what do catalysts do | lower the activation energy required, speeding up chemical reactions |
| enzymes | protein catalysts |
| catalyst definition | a chemical agent that accelerates a reaction without being permanently change in the reaction |
| enzymes are specific or inspecific | enzymes are specific for which reaction they will catalyze |
| are enzymes reusable | yes |
| what do enzymes typically en with | -ase |
| enzyme examples | sucrase, lactase, catalase |
| lower or upper line has enzymes | lower |
| substrate | the substance(reactant) an enzyme acts on |
| active site | the region of an enzyme molecule which binds to the substrate. it has a shape and chemistry that fits the substrate |
| induced fit | the entry of the substrate induces the enzyme to change shape slightly, making the fit between the substrate and the active site work |
| substrate+enzyme= complex= products + enzyme example | sucrose + sucrase = glucose +fructose+ sucrase |
| competitive inhibitors | chemicals that resemble an enzyme's normal substrate; they compete for the active site |
| matter | anything that has mass and takes up space |
| energy mass | none |
| energy space | none |
| measure of energy | how much it effects matter |
| en in energy | in |
| ergy in energy | work |
| energy literal translation | in work |
| energy | the ability to do work or put matter into motion |
| more or less energy causes more work to be done | the greater the energy, the more work done |
| kinetic energy | energy of motion, moves objects |
| potential energy | stored and inactive |
| what does potential energy come from | structure or location |
| laws of conservation of energy | energy is not created or destroyed |
| T/F Energy can only be converted | true |
| energy conversion efficiency | inefficient, creates heat |
| chemical energy stored where | in bonds |
| how is ATP released | bonds are broken |
| what do living organisms run on | ATP |
| ATP words | adenosine triphosphate |
| ATP consists of what | organic molecules, adenosine and tail of three phosphate grous |
| ATP to what when releasing energy | releases phosphate tail, creating phosphate group and ADP |
| ADP words | adenosine diphosphate |
| electrical energy | reflects the movement of moving matter |
| example of electrical energy | nerves |
| mechanical energy | energy involved in moving matter |
| mechanical energy example | riding a bike, pedaling |
| radiant energy example | light energy transformed in photosynthesis |
| chemical reaction | the making and/or breaking of chemical bonds |
| what do chemical reactions involve | rearranging of atoms, no atoms are created or destroyed in chemical reactions |
| are atoms created or destroyed in chemical reactions | no |
| how do chemical reactions occur | one or more substances change to produce one or more different substances |
| chemical equation | representation of a chemical reaction |
| shorthand of chemical reaction | chemical equation |
| reactents | starting materials |
| products | end materials |
| law of conservation of mass | atoms are neither created nor destroyed in chemical reactions so the mass must stay the same for chemical reactions to be possible and balanced |
| coefficients | numbers preceding molecular formula in a chemical reaction, reflect the relative amount of each substance required for the reaction, must be same on either side of the equation |
| energy absorbing reactions products | above reactants on graph, gain energy |
| energy releasing reactions products | below reactants on graph, release energy |
| activation energy | the energy needed for a reaction to go forward |
| EA reaction | endergonic, anabolism |
| anabolism | reactions that synthesize macromecules and absorb energy |
| ATP from ADP endergonic or exergonic | endergonic |
| ADP from ATP endergonic or exergonic | exergonic |
| exergonic | energy releasing, catabolism |
| catabolism | the reactions that break down molecules and release energy |
| metabolism | the su of all chemical reactions that take place in cells |
| proteins contain what elements | carbon, hydrogen, oxygen, and nitrogen |
| all amino acids have a | central carbon |
| amino group | -NH2 |
| carboxyl group | -CO2H |