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October 1, 1969Biochemistry

Computed circular dichroism spectra for the evaluation of protein conformation

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Authors

NGNorma J. GreenfieldGFGerald D. Fasman

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Overview

Biophysical analysis demonstrates computed circular dichroism spectra quantify protein secondary structure, highlighting a computational approach for conformation evaluation.

Key Points

  • To develop a computational method using circular dichroism (CD) spectra for quantitatively estimating protein secondary structure conformations.
  • Generated reference circular dichroism spectra corresponding to pure alpha-helical, beta-sheet, and disordered random coil conformations.
  • Applied mathematical curve-fitting to compare computed spectral mixtures against experimentally observed circular dichroism spectra of characterized proteins.
  • Demonstrates that linear combinations of reference secondary structure spectra reliably reconstruct experimental protein circular dichroism curves.
  • Establishes a quantitative framework to determine the fractional composition of alpha-helices, beta-sheets, and random coils in solution.

Cite This Study

Greenfield et al. (1969) studied this question.

synapsesocial.com/papers/6a1311e7257f24f1de9ec969https://doi.org/10.1021/bi00838a031
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