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Interestingly, these glycyl residues are located at the boundaries of the consensual alpha-helix, thus not alterating the predominant secondary structure of the 28-residue unit, showing that structural constrains are imposed on the secondary structure of the LRRs.
With increasing the length of alkyl side groups or raising the temperature, the predominant secondary structure gradually changed from α-helix to β-sheet conformation.
The as-cast SF-F matrix formed a mainly β-sheet structure that was similar to the SF-M matrix, whereas the as-spun SF-N matrix had a random coil conformation as the predominant secondary structure.
This suggests the presence of a more compact conformation but without any predominant secondary structure elements.
Circular dichroism analysis suggested that the predominant secondary structure of rP11-4 at physiological pH (pH 7.4) was antiparallel β-sheet, as has been observed for rP11-4/rP11-4 (hsl) [18] and for cP11-4 [13].
Represented by the blue curve in Figure 2a, the IgG sample has an amide I band peaking at 1637 cm–1, representative of proteins with a secondary structure comprising mainly β-sheets, which is the predominant secondary structure as determined by X-ray crystallography.
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We analyzed possible relationships among the group of proteins that could not crystallize, such as pI or predominant predicted secondary structure, but could not find any common trend among them.
As depicted in Figure 2(d), Bm-iPGM has two negative peaks around 222 nm and 208 nm and a stronger positive peak near 190 nm, which is a characteristic of predominant α-helical protein secondary structure [ 25].
The analysis predicted a predominant pattern of random coil, beta sheet and beta turn secondary structure for BSM after carbohydrate and amino acid spectral subtraction in agreement with other methods.
The minima at 208 and 222 nm, and the maximum at 192 nm in the CD spectrum showed the high α-helical secondary structure content of the recombinant proteins LipL40, MPL36 and rLIC12922, while rLIC12238 showed a predominant signal of β-strands, with minimum ellipticity around 215 nm (data not shown).
secondary structure.
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