Protein, spectroscopy

Sreerama, N., Venyaminov, S.Y., and Woody, R.W. 1999b. Estimation of the number of a-helical and -strand segments in proteins using circular dichroism spectroscopy. Protein Sci. 8 370-380. 

Amazaki TY, Hinck AP, Wang XY, Nicholson LK, Torchia DA, Wingfield P, Stahl SJ, Kaufman JD, Chang CH, Domaille PJ, Lam PY, Three-dimensional solution structure of the HIV-1 protease complexed with DMP323, a novel cyclic urea-type inhibitor, determined by nuclear magnetic resonance spectroscopy, Protein Sci., 5 495-506, 1996. 

Prestrelski SJ, Byler DM, Liebman MN. Generation of a substructure library for the description and classification of protein secondary structure. II. Application to spectrastructure correlations in Fourier transform infrared spectroscopy. Proteins 1992 14 440-450. 

Zhang, X., Boyar, W., Toth, M. J., Wennogle, L., and GonneUa, N. C. (1997). Structural definition of the C5a G terminus by two-dimensional nuclear magnetic resonance spectroscopy. Proteins 28, 261-267. 

J. Xu, K. W. Plaxco and S. J. Allen, Probing the Collective Vibrational Dynamics of a Protein in Liquid Water by Terahertz Absorption Spectroscopy. Protein Sci., 15(5), 1175-1181 (2006). 

D-Fluorescence spectroscopy. Protein solutions (BSA/Fg) were mixed with 0.3 mM ONOO and a series of CuS04 and Co(Ac)2 solutions with different concentrations, preparing for 3D fluorescence experiments. The fluorescence intensities were recorded with a F-4500 fluorescence spectrophotometer (Hitachi, Japan). Results are reported for the mean of at least three separate experiments. 

X-ray Photoelectron Spectroscopy. Protein films without plasticizer and uncoated from the glass plates were studied by XPS, using an Escalab MK II spectrometer with an A1 X-ray source (1486.6 eV of photon energy) and a three channel detector. Measurements were taken at an angle of 90°. 

Bechinger, B. Zasloff, M. Opella, S.J. "Structure and orientation of the antibiotic peptide magainin in membranes by solid-state nuclear magnetic resonance spectroscopy", Protein Sci., 1993,2,2077-2984. 

In some ways it is easier to obtain protein structures by NMR spectroscopy. Proteins need not be crystallized, just purified and dissolved. Would it be desirable to use NMR to learn about the structure of the active site of an enzyme, to design an inhibitor Why or why not ... 

Keywords APSY Automated peak picking Automated resonance assignment GAPRO NMR Projection spectroscopy Protein backbone Protein side chains... 

Mapping alpha-helical induced folding within the intrinsically disordered C-terminal domain of the measles virus nucleoprotein by site-directed spin-labeling EPR spectroscopy. Proteins 73 973-988... 

Li Y, Berthold DA, Gennis RB et al (2008) Chemical shift assignment of the transmembrane helices of DsbB, a 20-kDa integral membrane enzyme, by 3D magic-angle spinning NMR spectroscopy. Protein Sci 17 199-204... 

Mechanics, Classical Molecular Electronics Photoelectron Spectroscopy Protein Structure Quantum Chemistry Quantum Mechanics... 

B. Czarruk-Matusewicz, K. Murayama, R. Tsenkova, Y. Ozaki. Analysis of near-infrared spectra of complicated biological fluids by two-dimensional correlation spectroscopy protein and fat concentration-dependent spectral changes of mUk..Appl Spectrosc 53 1582,... 

Austin, J.C., Kuliopulos, A., Mildvan, A.S., Spiro, T.G. Substrate polarization by residues in A -3-ketosteroid isomerase probed by site-directed mutagenesis and UV resonance Raman spectroscopy. Protein Sci. 1, 259-270 (1992)... 

See also Cells Studied By NMR In vivo NMR, Applications, NMR Pulse Sequences Nuclear Over-hauser Effect Nucleic Acids Studied Using NMR Nucleic Acids and Nucleotides Studied Using Mass Spectrometry Parameters in NMR Spectroscopy, Theory of Perfused Organs Studied Using NMR Spectroscopy Proteins Studied Using NMR Spectroscopy Two-Dimensional NMR Methods. 

Solvent suppression has been one of the rich areas in biological NMR research. The driving force comes from in vivo and in vitro proton NMR spectroscopy, protein structure determination, metabolic and toxicological studies of biofluids, and medical and functional magnetic resonance imaging. New methods could emerge from the following two fundamental techniques ... 

See also Biochemical Applications of Raman Spectroscopy Biomacromolecular Applications of Circular Dichroism and ORD Carbohydrates Studied by NMR Circularly Polarized Luminescence and Fluorescence Detected Circular Dichroism Induced Circular Dichroism Magnetic Circular Dichroism, Theory Nucleic Acids and Nucleotides Studied Using Mass Spectrometry Organometallics Studied Using Mass Spectrometry Polymer Applications of IR and Raman Spectroscopy Proteins Studied Using NMR Spectroscopy Vibrational CD Spectrometers Vibrational CD, Theory. 

Three major classes of biomacromolecules have been studied by normal (nonresonance) Raman spectroscopy proteins, nucleic acids, and lipids and membranes. The type of information obtained for each class can be summarized as follows. 

---