The extrusion parameters influenced changes in protein structure in the amide I and II regions and in beta sheet
and alpha helix composition.
The aggregation from the native monomeric proteins to beta sheet
containing amyloid structures involves the formation of different species - misfolded proteins, small soluble oligomers and finally formation of fibrils.
The step-by-step comparison begins with the primary building blocks of each item -- an amino acid and a sound wave -- and moves up to the level of a beta sheet
nanocomposite (the secondary structure of a protein consisting of repeated hierarchical patterns of protein assemblages) and a musical riff (a repeated pattern of notes or chords).
Edgerton Associate Professor in MIT's department of civil and environmental engineering, and his team recently used computer models to simulate exactly how the components of beta sheet
crystals move and interact with each other.
In the beta sheet
conformation, the polypeptides are parallel and the hydrogen bonds link the adjacent polypeptides (1).
Molecular dynamics results, which reproduce the measured quasielastic neutron spectra extremely well, show that the observed dynamic changes arise primarily from the particular region of the protein that forms a beta sheet
in the native state and unfolds to a random coil in the molten globule.
Another common structure seen in proteins is the beta sheet
In a beta sheet
, a string of amino acids folds accordion-fashion into parallel segments oriented in alternating directions to form a flat sheet.