Tongue-surface movement patterns during speech and swallowing

The tongue has been frequently characterized as being composed of several functionally independent articulators. The question of functional regionality within the tongue was examined by quantifying the strength of coupling among four different tongue locations across a large number of consonantal contexts and participants. Tongue behavior during swallowing was also described. Vertical displacements of pellets affixed to the tongue were extracted from the x-ray microbeam database. Forty-six participants recited 20 vowel-consonant-vowel (VCV) combinations and swallowed 10 ccs of water. Tongue-surface movement patterns were quantitatively described by computing the covariance between the vertical time-histories of all possible pellet pairs. Phonemic differentiation in vertical tongue motions was observed as coupling varied predictably across pellet pairs with place of articulation. Moreover, tongue displacements for speech and swallowing clustered into distinct groups based on their coupling profiles. Functional independence of anterior tongue regions was evidenced by a wide range of movement coupling relations between anterior tongue pellets. The strengths and weaknesses of the covariance-based analysis for characterizing tongue movement are considered

Evaluating Molecular Mechanical Potentials for Helical Peptides and Proteins

Multiple variants of the AMBER all-atom force field were quantitatively evaluated with respect to their ability to accurately characterize helix-coil equilibria in explicit solvent simulations. Using a global distributed computing network, absolute conformational convergence was achieved for large ensembles of the capped A21 and Fs helical peptides. Further assessment of these AMBER variants was conducted via simulations of a flexible 164-residue five-helix-bundle protein, apolipophorin-III, on the 100 ns timescale. Of the contemporary potentials that had not been assessed previously, the AMBER-99SB force field showed significant helix-destabilizing tendencies, with beta bridge formation occurring in helical peptides, and unfolding of apolipophorin-III occurring on the tens of nanoseconds timescale. The AMBER-03 force field, while showing adequate helical propensities for both peptides and stabilizing apolipophorin-III, (i) predicts an unexpected decrease in helicity with ALA→ARG+ substitution, (ii) lacks experimentally observed 310 helical content, and (iii) deviates strongly from average apolipophorin-III NMR structural properties. As is observed for AMBER-99SB, AMBER-03 significantly overweighs the contribution of extended and polyproline backbone configurations to the conformational equilibrium. In contrast, the AMBER-99φ force field, which was previously shown to best reproduce experimental measurements of the helix-coil transition in model helical peptides, adequately stabilizes apolipophorin-III and yields both an average gyration radius and polar solvent exposed surface area that are in excellent agreement with the NMR ensemble

Developing Rehabilitation Specific Training for Organized Stroke Care in Low and Middle-Income Countries: What is Needed and How to Implement

No abstract available

Bakel - Vlomanshof/Roessel 2a

Onderzoeksrappor