Li + d nuclear reaction

The Circular Dichroism Spectrum and Structure of Unordered Polypeptides and Proteins

“…However, they have more in common with each other, in that they represent broad samplings of..p, t/J space, than they do with charged PGA, which represents a narrower distribution in conformational space [18,46J. This variability makes it highly unlikely that a single CD spectrum of a "random" polypeptide chain can be usefully assumed in analyzing for secondary structure in globular proteins, despite recent attempts to achieve this [47][48][49]. An important consequence of this is that, if we recognize the possible presence of unordered as well as EH states in polypeptide systems [43] (as well as ex and (3, of course), a variety of intermediate states is possible, with an associated span of CD spectra.…”

Protein conformation in bacterial spinae

“…The current utilization of CD data to interpret the conformational changes of globular proteins in solution is based upon two polemical assumptions: 1) that there are three components contributing to the observed CD spectrum; 2) that the CD contributions of these three components are linearly additive. [8][9][10] The linear addition of CD spectral components means that the observed CD spectrum may be described, at any given wavelength, by a linear combination of a-helix, 0-sheet, and unordered structure (unordered structure may in fact be more aptly described as remainder? since its calculation from three-component least squares fitting is as a remainder, r = 1a -0).…”