title: Collagen structure: the molecular source of the tendon magic angle effect.
abstract: This review of tendon/collagen structure shows that the orientational variation in MRI signals from tendon, which is referred to as the "magic angle" (MA) effect, is caused by irreducible separation of charges on the main chain of the collagen molecule. These charges are held apart in a vacuum by stereotactic restriction of protein folding due in large part to a high concentration of hydroxyproline ring residues in the amino acids of mammalian collagen. The elevated protein electrostatic energy is reduced in water by the large dielectric constant of the highly polar solvent (kappa approximately 80). The water molecules serve as dielectric molecules that are bound by an energy that is nearly equivalent to the electrostatic energy between the neighboring positive and negative charge pairs in a vacuum. These highly immobilized water molecules and secondary molecules in the hydrogen-bonded water network are confined to the transverse plane of the tendon. Orientational restriction causes residual dipole coupling, which is directly responsible for the frequency and phase shifts observed in orientational MRI (OMRI) described by the MA effect. Reference to a wide range of biophysical measurements shows that native hydration is a monolayer on collagen h(m) = 1.6 g/g, which divides into two components consisting of primary hydration on polar surfaces h(pp) = 0.8 g/g and secondary hydration h(s) = 0.8 g/g bridging over hydrophobic surface regions. Primary hydration further divides into side-chain hydration h(psc) = 0.54 g/g and main-chain hydration h(pmc) = 0.263 g/g. The main-chain fraction consists of water that bridges between charges on the main chain and is responsible for almost all of the enthalpy of melting DeltaH = 70 J/g-dry mass. Main-chain water bridges consist of one extremely immobilized Ramachandran water bridge per tripeptide h(Ra) = 0.0658 g/g and one double water bridge per tripeptide h(dwb) = 0.1974 g/g, with three water molecules that are sufficiently slowed to act as the spin-lattice relaxation sink for the entire tendon.
authors.affiliation: Radiology Department, University of Texas Health Science Center at San Antonio, San Antonio, Texas 78229, USA. fullerton@uthscsa.edu
authors.forename: Gary D
authors.initials: GD
authors.lastname: Fullerton
authors.forename: Andrés
authors.initials: A
authors.lastname: Rahal
mesh_terms: D000818:Animals; D001696:Biomechanical Phenomena; D055592:Biophysical Phenomena; D001703:Biophysics; D003094:Collagen / Q000737:chemistry*; D018360:Crystallography, X-Ray; D006801:Humans; D006860:Hydrogen Bonding; D008279:Magnetic Resonance Imaging / Q000379:methods*; D008958:Models, Molecular; D015394:Molecular Structure; D013710:Tendons / Q000033:anatomy & histology / Q000737:chemistry* / Q000502:physiology; D013816:Thermodynamics; D014867:Water / Q000737:chemistry
chemical_list: D014867:Water; D003094:Collagen