Computed circular dichroism spectra for the evaluation of protein conformation
NJ Greenfield, GD Fasman - Biochemistry, 1969 - ACS Publications
NJ Greenfield, GD Fasman
Biochemistry, 1969•ACS PublicationsCircular dichroism curves of poly-L-lysine con-taining varying amounts of a helix,/3-
pleatedsheet, and random coil segments have been computed in the 190-250-µ region. The
application of these curves for determining protein conformation is discussed. The circular
dichroism curves of several proteins, whose three-dimensional structures are known from X-
ray diffraction studies, have been fitted by a linear combination of the threereference
structures in the 208-240-µ region. Theresults show that these computed
pleatedsheet, and random coil segments have been computed in the 190-250-µ region. The
application of these curves for determining protein conformation is discussed. The circular
dichroism curves of several proteins, whose three-dimensional structures are known from X-
ray diffraction studies, have been fitted by a linear combination of the threereference
structures in the 208-240-µ region. Theresults show that these computed
Circular dichroism curves of poly-L-lysine con-taining varying amounts of a helix,/3-pleatedsheet, and random coil segments have been computed in the 190-250-µ region. The application of these curves for determining protein conformation is discussed. The circular dichroism curves of several proteins, whose three-dimensional structures are known from X-ray diffraction studies, have been fitted by a linear combination of the threereference structures in the 208-240-µ region. Theresults show that these computed
ACS Publications