NR AIFX

AU McPhie,P.

TI Circular dichroism studies on proteins in films and in solution: estimation of secondary structure by g-factor analysis.

QU Analytical Biochemistry 2001 Jun 1; 293(1): 109-19

PT journal article

AB Estimates of the secondary structure of a protein in solution are made by mathematical analyses of its circular dichroism (CD) spectrum below 240 nm. All current procedures require accurate determination of the concentration of the protein sample. Insoluble proteins, such as prions or amyloid, are examined as thin films or gels, but concentrations cannot be precisely defined. The ratio of a sample's CD and absorbance signals is the g-factor, an intensive property. The g-factor spectra of 19 soluble, unconjugated proteins of known structures were measured and used to derive basis spectra, characteristic of the four major structural elements, helix, sheet, turn, and remainder. Using these, the g-factor spectra of other unconjugated proteins, measured in solution or as films, can be analyzed by linear regression to give good estimates of their secondary structures when protein concentration cannot be determined.

MH Amino Acids/analysis; Animal; *Circular Dichroism; Comparative Study; Human; Mathematics; Models, Biological; *Protein Conformation; *Proteins/chemistry; Spectrophotometry, Ultraviolet

AD Peter McPhie, Laboratory of Biochemistry and Genetics, NIDDK, NIH, Building 8, Room 215, Bethesda, MD 20892-0830, USA

SP englisch

PO USA

EA pdf-Datei

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