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Protein conformation in bacterial spinae
Author(s) -
Coombs R. W.,
Verpoorte J. A.,
Easterbrook K. B.
Publication year - 1976
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.1976.360151204
Subject(s) - antiparallel (mathematics) , chemistry , circular dichroism , protein secondary structure , globular protein , crystallography , biophysics , biochemistry , biology , physics , quantum mechanics , magnetic field
The far uv circular dichroism (CD) and infrared spectra of bacterial spinae are reported. Estimates of the protein secondary structure were obtained by three‐component curve‐fitting methods supplemented by rank and factor analysis of CD data matrices. Native spinae were shown to contain approximately 88% antiparallel β‐sheet, 7% α‐helix, and 5% unordered structure based on estimates using poly( L ‐lysine). Basis CD spectra derived from globular proteins were shown to give unreliable estimates.