Mechanism of the interactions of aliphatic alcohols with bovine serum albumin in the ternary systems—1H n.m.r. study: 1. Aqueous solutions BSA-alcohols-urea

Role of aliphatic alcohols on the stability of rat-tail tendon (RTT) collagen fiber

“…6,7 The binding of aliphatic alcohols and water to hair keratin and bovine tendon collagen have been investigated by Bell and Breuer. 8 The mechanism of the interaction of aliphatic alcohols with bovine serum albumin was studied using 1 H-NMR technique by Soltysik-Resek et al 9 In type I collagen, many hydrophobic amino acids occur in clusters. 10,11 In an aqueous environment repulsive forces between water and nonpolar side chains can be expected to favor the ordering of structure of water as well as intermolecular assemblies in collagenous tissues.…”