Experimental and theoretical foundations for femtosecond time-resolved circular dichroism (TRCD) spectroscopy of excitonic systems are presented. In this method, the system is pumped with linearly polarized light signal...

Binding and proximity relationships of hydrophobic ligands on human serum albumin have been studied using absorption, fluorescence, circular dichroism, and electron paramagnetic resonance spectroscopy. The ligands studied were bilirubin, two conjugated linear polyene fatty acids, cis-parinaric acid and cis-eleostearic acid, and three nitroxide derivatives of stearic acid with doxyl groups at po...

Circular dichroism and optical rotation are crucial for the characterization of chiral molecules and are of importance to the study of pharmaceutical drugs, proteins, DNA, and many others. These techniques are based on the different interactions of enantiomers with circularly polarized components of plane wave light that carries spin angular momentum (SAM). For light carrying orbital angular mo...

We have examined the secondary structures of human class I and class II histocompatibility antigens in solution by Fourier transform infrared spectroscopy and circular dichroism in order to compare the relative amounts of alpha-helix, beta-sheet, and other structures, which are crucial elements in the comparison of the protein structures. Quantitation of infrared spectra of papain-solubilized H...

recombinant proteins are tending to be the most favorable vaccine-candidates against botulism. recombinant carboxy-terminal of botulinum neurotoxin serotype e (rbont/e-hcc) has been introduced as an efficient vaccine against botulism type e. in this report, we made an effort to investigate the effect of different ph on protein structure to assess if rbont/e-hcc could be used as a vaccine for or...

Vibrational structure in the near-UV circular dichroism (CD) spectra of proteins is an important source of information on protein conformation and can be exploited to study structure and folding. A fully quantitative theory of the relationship between protein conformation and optical spectroscopy would facilitate deeper interpretation of and insight into biophysical and simulation studies of pr...

We determine the magnetic properties of individual Co atoms adsorbed on graphene (G) with x-ray absorption spectroscopy and magnetic circular dichroism. The magnetic ground state of Co adatoms strongly depends on the choice of the metal substrate on which graphene is grown. Cobalt atoms on G/Ru(0001) feature exceptionally large orbital and spin moments, as well as an out-of-plane easy axis with...

A series of transition metal complexes involving non-innocent o-dithiolene and o-phenylenediamine ligands has been characterized in detail by various spectroscopic methods like magnetic circular dichroism (MCD), absorption (abs), resonance Raman (rR), electron paramagnetic resonance (EPR), and sulfur K-edge X-ray absorption spectroscopies. A computational model for the electronic structure of t...

Interactions between enamel matrix proteins are important for enamel biomineralization. In recent in situ studies, we showed that the N-terminal proteolytic product of ameloblastin co-localized with amelogenin around the prism boundaries. However, the molecular mechanisms of such interactions are still unclear. Here, in order to determine the interacting domains between amelogenin and ameloblas...