Raman Spectroscopic Studies on the Gel Formation of the Bovine Growth Hormone Releasing Factor
Quigley, Paul T.
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The results obtained in this study have confirmed that gelling is occurring in both of the peptides studied, but there is a definite lack of evidence that they are gelling in the same fashion. Both, though, do consist of similiar "average" secondary 1686, and 1703 cm-1. They differed slightly though in the percentages of each. The first consisted of 37.68% helix, 32.19% sheet, 17.98% turn, and 12.15% random, whereas the second was 34.6, 28.02, 21.18, and 16.20%,respectively. Unfortunately, there was not enough data taken on the secondpeptide (U-90699F), so it is not known what structural changes may occur later. From the data which was collected, the U-90699F does not follow the same gelling mechanism as the synthetic peptide. The U-90699F did not exhibit a quick change in structure once it went into solution like the other did, and it gained random coil as the other lost it.The B-sheet content in U-90699F may increase with more heating which would support the theory of its presence in gelling, but that data will not be available for this report. From what has been shown, it appears possible that the random coil is capable of aiding in gelling in certain gelformations. If thisis true, then the coil must aggregate in a fashion that allows itself to pack in close like the B-sheet has been shown ascapable of doing. Another possibility is that for the U-90699F to begin forming a gel through increasing its B-sheet content, it may have to firstreach a certain amount of the random coil. If this were true, it would be interesting to see if the random coil would stay where it was or begin to be depleted into sheets. Nevertheless, more analysis needs to be done on the actual U-90699F peptide.