Literature DB >> 18294952

Concentration-independent estimation of protein secondary structure by circular dichroism: a comparison of methods.

Peter McPhie1.   

Abstract

Estimation of a protein's secondary structure from its circular dichroism spectrum usually requires accurate knowledge of the concentration and pathlength of the sample. Two recently described methods avoid this problem by analysis of g-factor spectra (McPhie, Anal. Biochem. 293, 109-119) or scaling of relative intensities (Raussens et al., Anal. Biochem. 319, 114-121). Application of the two methods to the same samples shows that they can have similar efficacies. Calculation with the latter method is more rapid, but the performance of the former is maintained over reduced wavelength ranges.

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Year:  2008        PMID： 18294952      PMCID： PMC2327255          DOI： 10.1016/j.ab.2008.01.024

Source DB:  PubMed          Journal:  Anal Biochem        ISSN： 0003-2697            Impact factor:   3.365


  9 in total

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

Authors:  P McPhie
Journal:  Anal Biochem       Date:  2001-06-01       Impact factor: 3.365

2.  Protein concentration is not an absolute prerequisite for the determination of secondary structure from circular dichroism spectra: a new scaling method.

Authors:  Vincent Raussens; Jean-Marie Ruysschaert; Erik Goormaghtigh
Journal:  Anal Biochem       Date:  2003-08-01       Impact factor: 3.365

3.  CD studies on films of amyloid proteins and polypeptides: quantitative g-factor analysis indicates a common folding motif.

Authors:  Peter McPhie
Journal:  Biopolymers       Date:  2004-10-05       Impact factor: 2.505

4.  Large systematic errors compromise quantitation of intrinsically unstructured proteins.

Authors:  E Szollosi; E Házy; Cs Szász; P Tompa
Journal:  Anal Biochem       Date:  2006-11-09       Impact factor: 3.365

5.  Comparison of and limits of accuracy for statistical analyses of vibrational and electronic circular dichroism spectra in terms of correlations to and predictions of protein secondary structure.

Authors:  P Pancoska; E Bitto; V Janota; M Urbanova; V P Gupta; T A Keiderling
Journal:  Protein Sci       Date:  1995-07       Impact factor: 6.725

Review 6.  Methods to estimate the conformation of proteins and polypeptides from circular dichroism data.

Authors:  N J Greenfield
Journal:  Anal Biochem       Date:  1996-03-01       Impact factor: 3.365

7.  Dictionary of protein secondary structure: pattern recognition of hydrogen-bonded and geometrical features.

Authors:  W Kabsch; C Sander
Journal:  Biopolymers       Date:  1983-12       Impact factor: 2.505

8.  Experimental errors and their effect on analyzing circular dichroism spectra of proteins.

Authors:  J P Hennessey; W C Johnson
Journal:  Anal Biochem       Date:  1982-09-01       Impact factor: 3.365

9.  Estimation of protein secondary structure from circular dichroism spectra: comparison of CONTIN, SELCON, and CDSSTR methods with an expanded reference set.

Authors:  N Sreerama; R W Woody
Journal:  Anal Biochem       Date:  2000-12-15       Impact factor: 3.365
  9 in total
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Journal:  J Biol Chem       Date:  2014-07-14       Impact factor: 5.157

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Authors:  Susan E Cellitti; Jennifer Shaffer; David H Jones; Tathagata Mukherjee; Meera Gurumurthy; Badry Bursulaya; Helena I Boshoff; Inhee Choi; Amit Nayyar; Yong Sok Lee; Joseph Cherian; Pornwaratt Niyomrattanakit; Thomas Dick; Ujjini H Manjunatha; Clifton E Barry; Glen Spraggon; Bernhard H Geierstanger
Journal:  Structure       Date:  2012-01-11       Impact factor: 5.006

5.  Cloning, expression, purification and characterization of human mitochondrial carbonic anhydrase VA.

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Journal:  3 Biotech       Date:  2016-01-07       Impact factor: 2.406

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  6 in total

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