Circular dichroism spectroscopy proteins

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. 

The protein-containing colloidal solutions of water-in-organic solvents are optically transparent. Hence, absorption spectroscopy, circular dichroism spectroscopy and fluorescence spectroscopy are found to be convenient for studying biocatalysis [53]. The reversed micelles are interesting models for studying bioconversion, since the majority of the enzymes in vivo act inside or on the surface of biological membranes. 

Wallace, B. A., and Janes, R. W. (2001). Synchrotron radiation circular dichroism spectroscopy of proteins Secondary structure, fold recognition and structural genomics. Curr. Opin. Chem. Biol. 5, 567-571. 

Optical Spectroscopy General principles and overview, 246, 13 absorption and circular dichroism spectroscopy of nucleic acid duplexes and triplexes, 246, 19 circular dichroism, 246, 34 bioinorganic spectroscopy, 246, 71 magnetic circular dichroism, 246, 110 low-temperature spectroscopy, 246, 131 rapid-scanning ultraviolet/visible spectroscopy applied in stopped-flow studies, 246, 168 transient absorption spectroscopy in the study of processes and dynamics in biology, 246, 201 hole burning spectroscopy and physics of proteins, 246, 226 ultraviolet/visible spectroelectrochemistry of redox proteins, 246, 701 diode array detection in liquid chromatography, 246, 749. 

Johson, W.C. (1988). Secondary structure of proteins through circular dichroism spectroscopy. Ann. Rev. Biophys. Biophys. Chem., 17 145-166. 

Manning, M.C. 1989. Underlying assumptions in the estimation of secondary structure content in proteins by circular dichroism spectroscopy—a critical review. J. Pharmacol. Biomed. Anal. 7 110.3-1119. 

The coiled-coil motif is an ideal model system for the following reasons there is only one type of secondary structure present (the a-helix) the a-helical structure can be easily monitored by circular dichroism spectroscopy the two-stranded coiled coil contains two subunits stabilized by both intrachain and interchain interactions and, lastly, its small size reduces the potential complexity in the analysis and interpretation of results encountered in the analysis of globular proteins, which have multiple elements of secondary structure (a-helix, (3-sheet, (3-turns, loops, and regions of undefined structure). 

Bioactive macromolecules like peptides, proteins, and nucleic acids have been successfully embedded in planar LbL films. An important question is the retention of the bioactivity of the film-embedded biomolecules. The structural properties and stability of the LbL films formed from synthesized polypeptides of various amino acid sequences were recently reported [50]. The authors showed that control over the amino acid sequence enables control over non-covalent interpolypeptide interaction in the film, which determines the film properties. Haynie and coworkers showed by circular dichroism spectroscopy that the extent of adsorption of poly(L-glutamic acid) (PGA) and poly(L-lysine) (PLL) in the LbL films scales with the extent of secondary structure of the polypeptides in solution [51]. Boulmedais demonstrated that the secondary structure of the film composed of these polypeptides is the same as the peptide structure in the complex formed in solution [52], as found by Fourier transform IR spectroscopy (FUR). 

Polverino deLaureto, P., Frare, E., Gottardo, R., VanDael, H., andFontana, A. 2002. Partly folded states of members of the lysozyme/lactalbumin superfamily A comparative study by circular dichroism spectroscopy and limited proteolysis. Protein Sci 11( 12) 2932—2946. 

Analysis of protein structure by circular dichroism spectroscopy... 

Circular dichroism (CD) spectroscopy is a sensitive analytical tool for assessing protein structure. It can detect changes in both the secondary and tertiary structure of proteins, as well as provide information regarding prosthetic groups, bound ligands and co-factors. The origin of circular dichroism in proteins is described and various applications of CD spectroscopy to the study of protein structure, function, and folding is discussed. 

Navea, S., de Juan, A., and Tauler, R., Detection and resolution of intermediate species in protein folding processes using fluorescence and circular dichroism spectroscopies and multivariate curve resolution, Anal. Chem., 64, 6031-6039, 2002. 

Fig. 5. Circular dichroism spectroscopy of peptide (120-189) fused to a 6xHis-tag. The circular dichroism spectrum of 6xHis-rCla h6 (120-189) (protein concentration was 27 piMin salt-free water) was recorded on a Jasco spectropolarimeter (J-810) at 185-260nm. Computer-assisted analysis of the data showed that the peptide is folded with 11% helix, 35% (3-sheet, 27% loop and 26% random structural elements.

We can now examine the behavior of albumin adsorbed on quartz. Albumin was coated onto the four surfaces of a double compartment cell allowed to incubate for about 15 min, rinsed, filled with doubly distilled water, and then examined by accumulation circular dichroism spectroscopy. The spectra are shown in Figure 4. Although the protein cannot definitely be... 

Due to the fundamental importance of the adsorbed protein film, many methods have been used to characterize its nature. These methods include ellipsometry (3,A), Fourier transform infrared spectroscopy (FTIR) (5,6), multiple attenuated internal reflection spectroscopy (MAIR) (7,8) immunological labeling techniques (9), radioisotope labeled binding studies (j ), calorimetric adsorption studies (jj ), circular dichroism spectroscopy (CDS) (12), electrophoresis (j ), electron spectroscopy for chemical analysis (ESCA) (1 ), scanning electron microscopy (SEM) (15,16,9), and transmission electron microscopy (TEM) (17-19). 

In recent years, circular dichroism spectroscopy has been widely applied in investigations concerning the molecular structure of chiral polymers. It is a powerful tool for revealing the secondary structures of biological macromolecules, for instance of polypeptides, proteins, and nucleic acids in solution. An... 

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