Contraction-Induced Changes in Hydrogen Bonding of Muscle Hydration Water.

ABSTRACT: Protein-water interaction plays a crucial role in protein dynamics and hence function. To study the chemical environment of water and proteins with high spatial resolution, synchrotron radiation-Fourier transform infrared (SR-FTIR) spectromicroscopy was used to probe skeletal muscle myofibrils. Observing the OH stretch band showed that water inside of relaxed myofibrils is extensively hydrogen-bonded with little or no free OH. In higher-resolution measurements obtained with single isolated myofibrils, the water absorption peaks were relatively higher within the center region of the sarcomere compared to those in the I-band region, implying higher hydration capacity of thick filaments compared to the thin filaments. When specimens were activated, changes in the OH stretch band showed signif

SUBMITTER: Yoo H 

PROVIDER: S-EPMC3985702 | biostudies-literature | 2014 Mar

REPOSITORIES: biostudies-literature