User:Elizabeth Yowell/ SandboxFinal: Difference between revisions
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Within all four binding sites, we see two spike protein residues interacting with all four minibinders: K417 and Q493. This suggests that these resides are critical for binding. | Within all four binding sites, we see two spike protein residues interacting with all four minibinders: K417 and Q493. This suggests that these resides are critical for binding. | ||
Furthermore, an interesting difference between the two methodologies is revealed in the locations of hydrogen bonding. In the de novo designed minibinders, we see the main interactions occurring in the center of the RBD, whereas ACE2 and AHB2 reveal hydrogen bonding interactions throughout the length of the helices. | Furthermore, an interesting difference between the two methodologies is revealed in the locations of hydrogen bonding. In the de novo designed minibinders, we see the main interactions occurring in the center of the RBD, whereas ACE2 and AHB2 reveal hydrogen bonding interactions throughout the length of the helices. Shown below is a sequence alignment between ACE2 and the three minibinders. | ||
[[Image:Comparison.jpeg|400 px|left|thumb|The sequence differences between ACE2, AHB2, LCB1, and LCB3.]] | |||
[[Image:Comparison.jpeg|400 px|left|thumb|The sequence differences between ACE2, AHB2, | |||
