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Martin's paper on the Trypsin + SPINK1 complex is published

The reaction coordinate as observed in one TRY1-N34S SPINK1 molecular dynamics simulation (cf. (C) black curve). Blue and orange labels indicate amino acids from TRY1 and SPINK1, respectively. The amino acids in stick representation are colored by their supposed functions, red binding pocket, orange key, pink steric barrier and green amino acids that have to pass the barrier. (B) Conformational state in relation to the reaction coordinate for SPINK1 in solution for WT and N34S mutant. The colors black, blue and red relate to three independent simulations. (C) Same as (B), but for SPINK1 in complex with TRY1 in state II (cf. Figure 1). (D) Conformational state in relation to the reaction coordinate of structures for the TRY1-SPINK1 complex in state II (cf. Figure 1) observed during a replica exchange simulation.

A novel hypothesized mechanism for chronic pancreatitis caused by the N34S mutation on SPINK1

Martins's paper on A Hypothesized Mechanism for Chronic Pancreatitis Caused by the N34S Mutation of Serine Protease Inhibitor Kazal-Type 1 Based on Conformational Studies is published in Journal of Inflammation Research. Congratulations Martin

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