Mohanram H
Structure of a consensus chitin-binding domain revealed by solution NMR
Chitin-binding proteins (CBPs) are a versatile group of proteins found in almost every organism on earth. CBPs are involved in enzymatic carbohydrate degradation and also serve as templating scaffolds in the exoskeleton of crustaceans and insects. One specific chitin-binding motif found across a wide range of arthropods' exoskeletons is the "extended Rebers and Riddiford" consensus (R&R), whose mechanism of chitin binding remains unclear.
ReadDisorder-Order Interplay of a Barnacle Cement Protein Triggered by Interactions with Calcium and Carbonate Ions: A Molecular Dynamics Study
Barnacles strongly adhere to immersed solid substrates using a mixture of cement proteins (CP) that self-assembles into a permanently bonded layer and binds the barnacles’ shells to foreign surfaces.
ReadThree-dimensional structure of Megabalanus rosa Cement Protein 20 revealed by multi-dimensional NMR and molecular dynamics simulations
Barnacles employ a protein-based cement to firmly attach to immersed substrates. The cement proteins (CPs) have previously been identified and sequenced. However, the molecular mechanisms of adhesion are not well understood, in particular, because the three-dimensional molecular structure of CPs remained unknown to date. Here, we conducted multi-dimensional nuclear magnetic resonance (NMR) studies and molecular dynamics (MD) simulations of recombinant Megabalanus rosa Cement Protein 20 (rMrCP20).
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