Fig 1 - uploaded by Siddharth Rath
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Amino Acid pKa and corresponding protonation states at low, medium, and 119 high pH in WT-GrBP5 and M9 peptides. (A) Sequence of combinatorically selected 120 peptide that self-assembles at room temperature, neutral pH: WT-GrBP5, with charged 121 residues circled. Net charge of the peptide at low pH (pH<2.24), medium pH 122 (4.15<pH<9.6) and high pH (9.6<pH<10.10) are also shown to be +1, -2 and -3 123 respectively; (B) Sequence of charge neutral mutant of WT: M9-GrBP5, with mutated 124 residues circled. Net charge of the peptide at low pH (pH<2.24), medium pH 125 (2.24<pH<9.6) and high pH (9.6<pH<10.10) are also shown to be +1, 0 and -1 126 respectively; (C) pKa and protonation sites for N-terminus (Isoleucine), C-terminus 127 (Tyrosine) and charged residues (Aspartic Acid and Glutamic Acid); and (D) Protonation 128
Source publication
Spontaneous self-organization of solid-binding peptides on single-layer atomic materials offers enormous potential in employing these systems for practical technological and medical applications. Molecular self-organization of peptides depends highly on their sequences which, in turn, affect their conformational behavior under aqueous conditions. T...
