Dear Deeksha Sugunan

I see a number of options for you to check:

-You could dilute the protein solution with the highest concentration that would enable you to compare both samples at the same concentration. Do realize that the various deconvolution programs all have their limitations, see for more info:

https://www.researchgate.net/post/Loss_of_alpha-helical_dip_at_208_nm_observed_for_a_protein_thermal_melt_using_Circular_Dichroism

https://www.researchgate.net/post/Circular_dichroism_deconcolution_problem

https://www.researchgate.net/post/Can-anyone-suggest-some-software-to-calculate-the-percentage-of-alpha-helix-and-beta-sheet-from-circular-dichroism-data?

-You could use secondary structure prediction programs to see if any change in secondary structure is to be expected. See for more info (Table 2):

Article The role and significance of potential lipid-binding regions...

-You could check for example a program like Heliquest and use the so-called Eisenberg plot approach to see if the mutant version of the protein is more hydrophobic (or better contains more potential lipid binding regions) that might influence the overall solubility. See for more info:

Article New User-Friendly Approach to Obtain an Eisenberg Plot and I...

The things is that potentially a higher concentration of a protein can cause (unwanted) aggregation and in most cases give rise to higher beta-sheet and lower helix content. Using the above steps might confirm or eliminate this phenomenon.

Best regards.