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Unravelling the Working of the Animal Body: A Biophysical Approach David A D Parry Institute of Fundamental Sciences Massey University New Zealand
[object Object],[object Object],[object Object],[object Object],The Role of Fibrous Molecules
Replication
Replication X-ray pattern of DNA Maurice Wilkins Double-Helical Structure
Protection and Shape
Wool and Hair
Hair Follicle ,[object Object],[object Object],[object Object]
Molecular Structure of the Hair  Keratin Molecule
Crosslinking Methodology ,[object Object],[object Object],[object Object],[object Object]
Positions of the Characterised Crosslinks in Trichocyte Keratin
Axial Parameters Defining IF Structure K1/5/10/14 Reduced   -keratin Oxidised   -keratin No linkers fixed L1, L12 and L2 Fixed z a 79.74 78.15 50.00 z b 110.71 112.18 133.30 Repeat 301.16 302.51 316.61 Overlap 7.03  5.67 -8.43 A 12 -0.70 3.30 6.98 A 11 -111.41 -108.88 -126.32 A 22 189.75 193.63  190.28 L1 14.84 14.84 14.84 L12 12.57 12.57  12.57 L2 4.77 4.77  4.77 Δz(1BU, 1BD) -3.91 -1.38 -18.82 Δz(2BU, 2BD) 2.56 6.45 3.10 Δz(1BU, 2D) -50.54 -46.54 -42.86
Hair Keratin STEM Data 32 chains in cross-section
Key Physical Parameters in Hair Keratin Reduced 3.5 nm/wet/cryo-em 3.5 nm/wet/X-rays 44.92 nm/wet/crosslinks Oxidised 3.0 nm/wet/X-rays 2.9 nm /dry/X-rays 47.0 nm/wet/X-rays Radius of Electron-dense ring Axial Repeat r (8 + 0) r (7 + 1) Protofibrils contain four chains (two molecules) in cross-section
Models for the “Reduced” and “Oxidised” Hair Keratin IF Reduced (8 + 0) Oxidised (7 + 1)
Locomotion
Components of Connective Tissues  in Mature Animals
Sequence of Collagen Type I Chain
Interaction Maxima Between Parallel Molecules
Molecular Arrangement in Collagen Fibrils
Passive and Active Skins Greyhound Skin Guinea Pig Footpad Skin Trout Skin
Cross-sections of Common Digital Extensor Tendon top) and Suspensory Ligament (Bottom) from  a 5 Year Old Horse
Collagen Fibril Diameter Distributions in Horse Tendon and Ligament
X-ray Picture of Relaxed and Contracting Muscle a  b Low-angle X-ray diffraction patterns from ( a ) relaxed and ( b ) active molluscan smooth muscle (anterior byssus retractor muscle from  Mytilus edulis ). The actin pattern in ( a ) shows a clear third layer line but a missing second layer line, whereas ( b ) shows a second layer line (2) almost as strong as the third (3).  From Vibert et al. [3].
Cross-section Of Muscle Thin Filament Calculated X-Ray Intensities on the Second and Third Layer Lines of the Thin Filament
Regulation Model for Vertebrate Skeletal Muscle
Actin Filament Structure Actin plus tropomyosin structure determined by electron microscopy of isolated actin filaments  in the on and off states. Reconstructions by Lehman, Craig,Vibert et al.
Vision
Ultrastructure of Cornea
Corneal Fibril Diameters
Ultrastructure of Cornea and GAGs Parfitt et al. 2010 J. Struct. Biol., 170, 392-397
Corneal Transparency ,[object Object],[object Object],[object Object],[object Object]
[object Object],[object Object],Corneal Transparency
Unraveling the Working of the Animal Body: A Biophysical Approach (From left to right) Andrew Miller, David Parry, Barbara Brodsky, Bruce Fraser,  Tom MacRae, Eikichi Suzuki
David Hulmes Alan Craig John Squire Carolyn Cohen Tammy Lynch Peter Steinert

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