Molecular Properties V2

Molecular Properties, Volume II is a collection of papers that deals with the physical and chemical properties of iron-sulfur proteins, with emphasis on the theory and application of physicochemical techniques related to metalloproteins. One paper describes the chemical properties of simple iron-sulfur proteins focusing on chloroplast, bacterial-type ferredoxins, and the nature of the active site in the ferredoxins. Another paper notes that rubredoxin sequences can offer phylogenetic, evolutionary, or genetic data. The paper shows that rubredoxins from aerobic and anaerobic bacteria have originated from some common ancestor. One paper analyzes the chemical and physical properties of rubredoxin and the way they relate to the structure resulting from an X-ray diffraction. The investigator can use electron paramagnetic resonance (EPR), electron nuclear double resonance (ENDOR) spectroscopy, or nuclear magnetic resonance (NMR) to determine the structural and functional features of simple and conjugated iron-sulfur proteins. He can also use a proton magnetic resonance (PMR) spectroscopy to study the structures and interactions of proteins in solution, such as ribonuclease, lysozyme, and the heme proteins (hemoglobins or myoglobins). Cellular biologists, micro-biologists, bio-chemists, and scientists involved in biological systems research will find this collection very informative.

Molecular Properties, Volume II is a collection of papers that deals with the physical and chemical properties of iron-sulfur proteins, with emphasis on the theory and application of physicochemical techniques related to metalloproteins. One paper describes the chemical properties of simple iron-sulfur proteins focusing on chloroplast, bacterial-type ferredoxins, and the nature of the active site in the ferredoxins. Another paper notes that rubredoxin sequences can offer phylogenetic, evolutionary, or genetic data. The paper shows that rubredoxins from aerobic and anaerobic bacteria have originated from some common ancestor. One paper analyzes the chemical and physical properties of rubredoxin and the way they relate to the structure resulting from an X-ray diffraction. The investigator can use electron paramagnetic resonance (EPR), electron nuclear double resonance (ENDOR) spectroscopy, or nuclear magnetic resonance (NMR) to determine the structural and functional features of simple and conjugated iron-sulfur proteins. He can also use a proton magnetic resonance (PMR) spectroscopy to study the structures and interactions of proteins in solution, such as ribonuclease, lysozyme, and the heme proteins (hemoglobins or myoglobins). Cellular biologists, micro-biologists, bio-chemists, and scientists involved in biological systems research will find this collection very informative.