Proteins Clam-shaped globular

Filament Assembly from a Clam-shaped Globular Protein... 

Adapting the Clam-shaped Globular Protein Motif to Approach a Sliding Filament Element of Contraction... 

Figure 2.14. A Phosphorylation Driven Unfolding. A clam-shaped globular protein exhibits an opening fluctuation but closes due to the formation of too much hydrophobic hydration. Phosphorylation of the site near the mouth of the clam-shaped globular protein destructures so much hydrophobic hydration...

Figure 2.15. A primitive swinging cross-bridge/ sliding filament model of muscle contraction is introduced for the purpose of providing a conceptual bridge from the simple oil-like dissociation/assoda-tion for the opening/closing of a clam-shaped globular protein toward the more complex structural aspects of muscle contraction. Major limitations in...

The Process of Muscle Contraction Itself Can Be Viewed as a Variation on the Clam-Shaped Globular Protein Theme... 

Clam-Shaped Globular Proteins That Open and Close Due to Hydrophobic Association... 

The top part of Figure 10 shows a series of clam-shaped globular proteins strung together near the open end by elastic bands and maintained at fixed extension. In this isometric state, there is depicted an equilibrium between open and closed states. Obviously, shifting the equilibrium toward the closed state would increase the force measured at the force transducer, whereas shifting toward the open state would... 

Figure 10. Cartoon of the relationship between hydrophobic association and entropic elastic force development. Above A series of clam-shaped globular protein strung together by elastic bands with an equilibrium between open and hydrophobically associated closed states. Clearly, as the equilibrium shifts toward more closed states, the force, sustained by the interconnecting elastic segments, increases. Below Representation of the p-spiral structure of...

Opening and closing of the clam-shaped globular proteins of the upper part of Figure 10 (Urry, 1990) would be detectable under condi-... 

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