drake29 - MUSCLE AND MOLECULAR MOTORS Medical Biochemistry,...

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MUSCLE AND MOLECULAR MOTORS Medical Biochemistry, Lecture 29
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Lecture 29, Outline Muscle proteins and structure Protein interactions involved with muscle contraction Structure of tubulin Microtubules and cilia
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Thick and Thin Filaments
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Thick Filaments – Myosin Composed of six highly conserved polypeptide chains Two 220 kDa heavy chains that have elongated globlular heads, and long fibrous helical tails. Each head region contains an ATP-binding site/ATPase function Two pairs of light chains, termed essential light chains and regulatory light chains. These interact with the globular heads of the heavy chains, and regulate ATPase functions depending on their phosphorylation status.
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Conserved Hydrophobic residues at positions a and d in the helices MYOSIN STRUCTURE ATPase
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Structure of Myosin Head Region
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Thin Filaments - Actin Exists as a monomer, termed G-Actin , at low ionic strength and can bind one ATP At physiological ionic strength (plus Mg 2+ ), the G-actin forms fibrous polymers termed F-actin . ATP hydrolysis occurs during this process and ADP remains bound to each F-actin subunit F-actin is the core of the thin filament, and each monomer is capable of binding one myosin globular head. The coil repeats at roughly every seventh actin unit.
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A c t i n T h F l a m e C o p s
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Actin Monomer Structure
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Thin Filaments: Troponin/Tropomyosin Tropomyosin : a two chain fibrous protein that attach to F-actin in the groove between its filaments Troponins : three protein components, troponin C , a calcium binding protein like calmodulin;
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drake29 - MUSCLE AND MOLECULAR MOTORS Medical Biochemistry,...

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