Water scaffolding in collagen: Implications on protein dynamics as revealed by solid‐state NMR

Abstract

ABSTRACT:Solid-state NMR studies of collagen samples of various origins confirm that the amplitude of collagen backbone and sidechain motions increases significantly on increasing the water content. This conclusion is supported by the changes

Adsorption of C.I. Natural Red 4 onto Spongin Skeleton of Marine Demosponge

“…The 13 C CP/MAS NMR spectrum of H. communis spongin indicates the presence of aliphatic carbon (saturated alkanes), as well as carbon bonded to nitrogen (C–NR 2 ) and to oxygen (C–OH and C–OR) with signals in the 20–80 ppm range. There is also a marked signal at δ = 174.3, which is characteristic of carbon occurring in a carboxyl group or its derivatives [30,52]. Marine sponge spongin has an inexact chemical structure, where each resonance represents not just one but a range of chemical environments.…”

Study of H/D exchange rates to derive the strength of intramolecular hydrogen bonds in halo substituted organic building blocks: An NMR spectroscopic investigation

“…There are number of chemical reactions in which the transfer of one or more protons (viz., hydride ions or hydrogen atoms) takes place in the rate determining step. [30][31][32][33][34] The reaction kinetics depend on several factors, which also include the strength of intramolecular hydrogen bond and the electronic effects caused by the substituents that can be monitored by hydrogen/deuterium (H/D) exchange, a technique which is widely employed for understanding the protein conformation, and dynamics [35][36][37][38][39][40][41] in aqueous media. The inter-and the intramolecular hydrogen bonds can affects the rate of H/D exchange in a particular molecule.…”

Mechanistic Insights into the Structural Stability of Collagen-Containing Biomaterials Such as Bones and Cartilage

“…Collagen is the most abundant structural component in the ECM of these connective tissues, which forms a scaffold to provide strength and structure, known for its wide range of functions, including local storage, entrapment, delivery of growth factors, tissue morphogenesis, and tissue repair. , The most common natural occurrence in all connective tissues and a broad range of functional behaviors make it a widely studied biological system. Most of the studies had been done using extracted collagen, model peptides, and molecular dynamics simulation. − The absolute native environment of collagen in connective tissues is formed with other ECM components and interactions among them and hence responsible for different structural arrangements than the extracted form of collagen . The collagen protein possesses a triple helical structure, which is a polypeptide chain primarily consisting of a unique amino acid (AA) sequence of glycine (Gly), proline (Pro), and hydroxyproline (Hyp) as repeating units .…”