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• W2155242510 abstract "A molecular model of collagen hydration is used to validate centrifugal dehydration force (CDF) and re-hydration isotherm (RHI) methods to measure and characterize hydration compartments on bovine tendon. The CDF method assesses fluid flow rate from flexor and extensor tendons expressed in (g-water/g-dry mass-minute) and hydration capacity of compartments in (g-water/g-dry mass). Measured water compartment capacities agree with the molecular model of collagen hydration [Fullerton GD, Rahal A. Collagen structure: the molecular source of tendon magic angle effect. J Mag Reson Imag 2007;25:345–361; Fullerton GD, Amurao MR. Evidence that collagen and tendon have monolayer water coverage in the native state. Cell Biol Int 2006;30(1):56–65]. Native tendon hydration has monolayer coverage on collagen h m= 1.6 g/g which divides into primary hydration on polar surfaces hpp= 0.8 g/g and secondary hydration hs= 0.8 g/g bridging over hydrophobic surfaces. Primary hydration is hydrogen bonded tocollagen polar side chains hpsc= 0.54 g/g with small free energy or to the protein main chain hydration hpmc= 0.26 g/g with greater free energy of binding. The CDF method replaces the more time consuming water proton NMR spin-lattice dehydration (NMR titration) method, confirms the presence ofthree non-bulk water compartments on collagen (hpmc= 0.26 g/g, hpp= 0.8 g/g and hm= 1.6 g/g). This CDF method provides the most reproducible experimental measure of total tissue non-bulk water (TNBW). The re-hydration isotherm method, on the other hand, provides the most accurate measure of the Ramachandran water-bridge capacity hRa= 0.0656 g/g. The only equipment needed are: microfilterfuge tubes, a microcentrifuge capable of 14,000 × g or 4 MPa, a vacuum drying oven, an accurate balance and curve fitting ability. The newly validated methods should be useful for characterizing multiple water compartments in biological and non-biological materials by allowing direct measurement of water compartment changes induced by pH, co-solute salt, glycation and protein cross-linking." @default.
• W2155242510 created "2016-06-24" @default.
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• W2155242510 date "2007-06-01" @default.
• W2155242510 modified "2023-10-12" @default.
• W2155242510 title "Verification of simple hydration/dehydration methods to characterize multiple water compartments on Tendon Type 1 Collagen" @default.
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• W2155242510 doi "https://doi.org/10.1016/j.cellbi.2006.11.020" @default.
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