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. Author manuscript; available in PMC: 2024 Jun 20.
Published in final edited form as: J Chem Theory Comput. 2023 Jul 18;19(16):5609–5620. doi: 10.1021/acs.jctc.3c00190

Figure 6:

Figure 6:

Normalized local solvent-accessible surface area (SASA) using an eight-residue sliding window and a 10 Å probe size. Normalization is done using excluded volume (EV) reference simulations to account for side-chain-dependent differences in solvent accessibility. Amino acid residues are colored as in Fig 3. Distinct patterns of accessibility are observed across different proteins, indicating long- and short-range intramolecular interactions can influence the accessibility of local binding sites.