Lecture 13 - N terminus: globular, where ATP gets...

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Lecture 13 Molecular motor Chemical energy -> Motion Skeletal Muscle Many // myofibers o Giant multinucleated cells o Each run ~ entire muscle length o Each 10-100 micro-meter in diameter o Each myofiber is composed of myofibrils 100 – 1000/myofiber, 1mm diameter
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Sacromere Myofilaments o Actin: thin, zones/bands o Myosin: thick I band: light, actin Z disc: bisects I band, anchors actin, attach myofibrils together A band: dark, myosin/actin overlap M line: organize myosin
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Sacromere – functional unit of contraction Actin + myosin > 90% of muscle mass
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Myosin 540,000 Molecular Weight 6 subunits 2 heavy chains, 4 light chains o C terminus: α helical, fibrous coiled-coil – tail domain o
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Unformatted text preview: N terminus: globular, where ATP gets hydrolyzed head domain/motor domain Actin Abundant Monomers (G) -> Filaments (F) Actin monomers binds specifically to 1 myosin head -> weak interactions Muscle contraction 1. Myosin bound tightly to actin rigor conformation 2. ATP binds myosin -> conformational change in actin binding site -> decreases affinity of myosin/actin -> bound actin released 3. ATP hyrolyzes -> conformational change -> protein into high energy state ADP +Pi still bound 4. Myosin binds weakly at new F-actin site Inorganic Pi released Tight binding of myosin to actin Triggers power stroke (ADP released)...
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This note was uploaded on 01/02/2010 for the course BIBC BIBC 100 taught by Professor Buehler during the Fall '09 term at UCSD.

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Lecture 13 - N terminus: globular, where ATP gets...

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