How are troponin, tropomyosin and g-actin molecules put together?
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They form the engine for protein movement along the actin filiment-usually discussed regarding muscular movement.  There are a number of excellent illistrations of the exact interactions between them-The link provided gives one:
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1. At the neuromuscular juncture, ACh released by the synaptic terminal binds to receptors on the sarcolemma.\n\n2. The resulting change in the transmembrane potential of the muscle fiber leads to the production of action petential that spreads across the entire surface of the muscle fiber and along the T tubules.\n\n3.The sarcoplasmic reticulum releases stored calcium ions, increasing the calcium concentration of the sarcoplasm in and around the sarcomeres.\n\n4. Calcium ions bind to triponin, producing a change in the orientation of the troponin-tropomyosin complex that exposes active sites on the thin filaments (actin). Cross-bridges form when myosin heads bind to the active sites on F actin.\n\n5. The contraction begins as repeated cycles of cross-bridge binding, pivoting, and detatchment occur, powered by the hydrolysis of ATP. These events produce filament sliding, and the muscle fiber shortens.
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proteins-amino acids, nucleic acids-nucleotides, carbohydrates (sugars)-glucose, and lipids-gylcerol and fatty acids
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I could copy the answer, but I have some good links instead. \nSkeletal muscle fibers are multinucleated and fusiform, and basically contain myofibrills. See details at the link:\nhttp://training.seer.cancer.gov/module_anatomy/unit4_2_muscle_structure.html\n\nPay special attention to the myofibrils, the mitochondria and the sarcoplasmic reticulum :-)\n\nIllustrations of structure at different levels (I wish these pictures had been around years ago when I studied this!):\nhttp://www.agen.ufl.edu/~chyn/age2062/lect/lect_19/179.gif\nhttp://www.mhhe.com/biosci/esp/2001_gbio/folder_structure/an/m5/s5/assets/images/anm5s5_1.jpg
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From respiration: Here, glucose molecules in the cell are broken down; the molecules have strong bond between them and so when they are broken, energy is provided(by mitochondria) and when new molecules are formed, energy is released, which the cell uses for various processes.\n\nFrom protein synthesis: It occurs on the ribosomes in the cytoplasm, and aminoacids are combined to form proteins and this releases energy.\n\nFrom ATP(adenosine tri-phosphate): The ATP molecule is a packet of energy which stores the energy released during any process going on in the cell and then releases the energy as and when required by the cell.
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nucleotides make up nucleic acids
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proteins\ncarbohydrates\nfats\nnucleic acids like dna and rna\nare the major biomolecules.
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Picture a string of beads- the beads are different sizes and shapes. \n\nNow, "proteins" are basically like a string of beads that could be a very long string or a short string. AND instead of beads, there are amino acids- with different shapes and sizes. \n\nBut these strings don't lie flat. Depending upon the amino acids and other factors, the protein strings bend and fold in certain ways. So the string may become more like a ball or other strange shapes; this affects the way the protein works and interacts with other protein or chemicals. \n\nHope that mental picture helps answer your question...
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This search:\n\nhttp://www.google.com/search?sourceid=navclient&ie=UTF-8&rls=RNWE,RNWE:2004-20,RNWE:en&q=%22Z+line%22+actomyosin\n\nmay help you, eg:\n\nhttp://72.14.235.104/search?q=cache:tdm7-RoSXMIJ:www.dentistry.leeds.ac.uk/biochem/thcme/muscle.html+%22Z+line%22+actomyosin&hl=en&ct=clnk&cd=4\n\nAccording to this one:\n\nhttp://72.14.235.104/search?q=cache:ea3xzJMj0nsJ:www.neuro.wustl.edu/neuromuscular/mother/myosin.htm+%22Z+line%22+actomyosin&hl=en&ct=clnk&cd=11\n\n"Z-line: Capping proteins inhibit polymerization at the most active, barbed (plus) end \nOther actin filament associated proteins \nActin bundling proteins: Plastins  \nα-actinin"\n\nand that leads to another 2 links....\n\n:-)
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I answered that same question yesterday:\nThe impulse reaches the terminal end of the motor neuron and breaks open the synaptic vesicles, releasing the neurotransmitter acetylcholine into the synaptic cleft.\nACh then binds to receptor molecules in the motor end plate of the muscle fiber.\nThe action potential is started in sarcolemma and passes along the membrane until it reaches the sarcoplasmic reticulum releasing calcium. Calcium diffuses in sarcoplasm and binds to the troponin in the thin filaments.\nThe binding sites on the actin molecules are freed, allowing\nthe heads of myosin (thick filaments) to attach on the binding sites forming the cross-bridges connections.\nThe cross-bridges shift their angle causing the thin filaments to slide over the thick filaments; this produces the contraction.\nATP is needed for the last step. ATP is bound to myosin; calcium activates ATP breakdown into ADP and phosphate.\nPart of the energy produced is used to move bridges, the other part is released as heat, increasing the body temperature.\nMore ATP breaks the bond between thick and thin filaments in the cross bridge; calcium returns to thesarcoplasmic reticulum and the thin filaments return to their original position, closing off the binding site to cross bridges and causing the muscle to relaxe.
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1. Nucleus\n2. Food Vacuole\n3. Contractile Vacuole\n4. Cytoplasm\n5. Psedopod\n6. Cell membrane
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1) proteins are made of amino acids\n2)carbohydrates made of monosaccharides \n3) lipids made of fatty acids\n4) nucleic acids made of nucleotides\n\npolymers are made of monomers
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That is because heat destroys the structure of a functional protein.\nproteins are long chains of amino acids. This chain of amino acid folds up into a 3 dimensional structure via intramolecular forces. like you can fold up a long, blown-up balloon into a giraffe or a dog. With this structure, proteins are able to perform its functions. but when you heat the protein, you break the bonds in the amino acid chain, unfolding it and destroying its 3 dimensional structure. (IE, breaking the giraffe back to a long baloon, obviously it doesn't look like a giraffe anymore) and the protein cannot perform its functions.
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those are largely hydrophobic amino acids. which means they won't want to be near water, so they will be on the inside of the protein fold. to answer this question they want you to know the properties of amino acids.\n\ncytoplasmic proteins are the ones inside the cell- resident of the cytoplasm.\n\nproteins are made of amino acids. the amino acid sequence makes up the primary structural features. secondary structure is made up by the string of amino acids interacting with itself to find the lowest energy state. it can form alpha helices, beta sheets, and coils. tertiary structure is the folding together of these helices and sheets into a more compact molecule. quaternary structure is the interaction of different protein chains with tertiary structures to create a functional protein. not all proteins have quaternary structure. for example, g protein coupled receptors consist of only one amino acid chain with tertiary structure. N type calcium channels are composed of multiple subunits, and each subunit is a different protein chain. the interaction of these protein chains makes the protein work. therefore N type calcium channels have quaternary structure.
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Cells  store energy in the hooking of that third phosphate changing Adenosene-DiPhosphate to Adenosyne-TriPhosphate.\n\nThat terminal bond is the high energy one. Breaking it is what releases the spendable energy needed for protein synthesis. A good place to spend your money if you are a cell.\n\nThe terminal phosphate group is usually not just sloughed off but may be attached to other molecules in the cell.\n\nW + ATP -----> W~P + ADP where W is any compound, for example:\n\nglucose + ATP -----> glucose~P + ADP\n\nThis process is called phosphorylation.
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It is very simple. Last band gives you that answer. You need to see G=G bond and it is follow by TAG. It is definatly eukaryotic.
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1 ribosomes\n2 stimuli\n3 enzyme\n4 cytoplasm