Collagen type I amide I band infrared spectroscopy

Correction: Insulin dimer dissociation and unfolding revealed by amide I two-dimensional infrared spectroscopy.

Correction for 'Insulin dimer dissociation and unfolding revealed by amide I two-dimensional infrared spectroscopy' by Ziad Ganim et al., Phys. Chem. Chem. Phys., 2010, 12, 3579-3588.

Amide I two-dimensional infrared spectroscopy: methods for visualizing the vibrational structure of large proteins.

Network layouts are introduced as a method to visualize couplings between local amide I vibrations in proteins. The method is used to identify groups of strongly coupled oscillators to block-diagonalize the Hamiltonians, considerably reducing the expense associated with computing infrared spectra of large proteins. The quality of linear and nonlinear spectra generated from block-diagonal Hamilt...

Insulin Dimer Dissociation and Unfolding Revealed by Amide I Two-Dimensional Infrared Spectroscopy

Nanomechanics of Type I Collagen.

Type I collagen is the predominant collagen in mature tendons and ligaments, where it gives them their load-bearing mechanical properties. Fibrils of type I collagen are formed by the packing of polypeptide triple helices. Higher-order structures like fibril bundles and fibers are assembled from fibrils in the presence of other collagenous molecules and noncollagenous molecules. Curiously, howe...

Simulation of vibrational energy transfer in two-dimensional infrared spectroscopy of amide I and amide II modes in solution.

Population transfer between vibrational eigenstates is important for many phenomena in chemistry. In solution, this transfer is induced by fluctuations in molecular conformation as well as in the surrounding solvent. We develop a joint electrostatic density functional theory map that allows us to connect the mixing of and thereby the relaxation between the amide I and amide II modes of the pept...