New Molecular Model for the Long-range Elasticity of Elastin

High resolutionq‐space imaging studies of water in elastin

“…Nevertheless, the mechanism resulting in the elasticity of hydrated elastin is still not well understood and several models have been put forward to account for the elastic behavior, all of which implicitly assume waters of hydration. [3][4][5][6] In this work, we focus on further understanding of the complex water-elastin interaction by probing the molecular dynamics of water within elastin fibers by q-space NMR imaging.…”

Steady or Unsteady? Uncovering the Aerodynamic Mechanisms of Insect Flight

“…In sensory neurobiology, he had shown that cephalic bristles in insects play an important mechanosensory role in the detection of air flow (Weis-Fogh, 1949). In cell mechanics, he had discovered a novel calcium-dependent contractile mechanism in the intracellular fibres (or spasmonemes) of protozoan vorticellid ciliates that powers the contraction of their stalks (Weis-Fogh and Amos, 1972). Because these discoveries were primarily experimental in nature, the techniques pioneered by WeisFogh helped launch several research programmes in their own right.…”

“…On the biomechanics front, he had discovered and physically characterized an elastic element in the locust tendon called resilin, which remains the most efficient rubber protein studied to date (Weis-Fogh, 1960) (see also BennetClark, 2007). He had also studied the molecular basis of the long-range elasticity of elastin, the vertebrate equivalent of resilin (Weis-Fogh and Andersen, 1970). In sensory neurobiology, he had shown that cephalic bristles in insects play an important mechanosensory role in the detection of air flow (Weis-Fogh, 1949).…”

Applications of solid state NMR to cardiolipin and elastin.

“…That elastomers can operate on the basis of interfacial forces was first suggested by Weis-Fogh and Andersen in 1970 [121]. Consider also that the dominant driving force of elastin's recoil is closely related to the dominant force of protein folding.…”

“…stretch reduces the protein's conformational entropy. The alternative view [121][122][123][124] is based on the hydrophobic effect and proposes that stretch increases water exposed hydrophobic surface area thereby increasing solvent order and lowering solvent entropy. This is the basis of the hydrophobic effect which is generally regarded as the dominant thermodynamic driving force in protein folding [125].…”