Anion induced conformational preference of CαNN motif residues in functional proteins. Issue 12 (8th October 2017)

• Record Type: Journal Article
• Authors: Patra, Piya; Ghosh, Mahua; Banerjee, Raja; Chakrabarti, Jaydeb
• Is Part Of: Proteins. Volume 85:Issue 12(2017)
• Page Start: 2179
• Page End: 2190
• Publication Date: 2017-10-08
• Subjects: anion recognition -- conformational thermodynamics -- correlation plot -- molecular dynamics -- secondary structure; Proteins -- Periodicals; Proteins -- Periodicals; 572.6
• DOI: 10.1002/prot.25382
• Languages: English
• ISSNs: 0887-3585

Abstract

Abstract: Among different ligand binding motifs, anion binding C α NN motif consisting of peptide backbone atoms of three consecutive residues are observed to be important for recognition of free anions, like sulphate or biphosphate and participate in different key functions. Here we study the interaction of sulphate and biphosphate with C α NN motif present in different proteins. Instead of total protein, a peptide fragment has been studied keeping C α NN motif flanked in between other residues. We use classical force field based molecular dynamics simulations to understand the stability of this motif. Our data indicate fluctuations in conformational preferences of the motif residues in absence of the anion. The anion gives stability to one of these conformations. However, the anion induced conformational preferences are highly sequence dependent and specific to the type of anion. In particular, the polar residues are more favourable compared to the other residues for recognising the anion.