Science Advances

Supplementary Materials

This PDF file includes:

  • Crystallographic model of human BRCA1-BRCT protein
  • Fig. S1. Three-dimensional crystal structure of the BRCA1-BRCT protein.
  • Design and fabrication of device
  • Fig. S2. Top-down and bottom-up process fabrication.
  • Fig. S3. SEM images of different SSCs.
  • Theoretical comparison of ordered and disordered SSC device
  • Fig. S4. FDTD analysis of the role of disorder.
  • Complete peptide content of all the solutions resolved using the nanolens SERS device
  • Fig. S5. Nanolens matrix position of measurement points for the synthetic peptide solution.
  • Fig. S6. Nanolens matrix position of measurement points for the wild-type peptide solution.
  • Fig. S7. Nanolens matrix position of measurement points for the mutated peptide solution.
  • Table S1. Peptide fraction calculated for each measurement point in the grid of nanolens devices and x2 and r2 statistics for the synthetic peptide solution.
  • Table S2. Relative content of each peptide in the synthetic peptide solution.
  • Table S3. Peptide fraction calculated for each measurement point in the grid of nanolens devices and x2 and r2 statistics for the wild-type peptide solution.
  • Table S4. Relative content of each peptide in the wild-type peptide solution.
  • Table S5. Peptide fraction calculated for each measurement point in the grid of nanolens devices and x2 and r2 statistics for the mutated peptide solution.
  • Table S6. Relative content of each peptide in the mutated peptide solution.
  • List of synthetic peptides utilized in the work and corresponding IDs
  • Extraction of wild-type and mutated BRCA1-BRCT protein domain

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