Protein Folding
From Biomatics.org
"Biological protein-protein interactions differ from the more general class of physical interactions; in a biological interaction, both proteins must be in their proper states (e.g. covalently modified state, conformational state, cellular location state, etc.). Also in every biological interaction, one or both interacting molecules undergo a transition to a new state. This regulation of protein states through protein-protein interactions underlies many dynamic biological processes inside cells.
Therefore, understanding biological interactions requires information on protein states. "
The Basic construction of the model protein is shown where C-alpha atoms are numbered as 1, 2, 3, etc., whereas the side residues are shown by 1', 2', 3' etc. Note the varying size of the side residues.
Finite state model
The process of the folding of a protein can be described in terms of Finite State Machine(FSM) theory, one of the mathematical underpinnings of Computer Science.
Smart molecules
The Amino Acid Code
The Histone Code
Chaperone proteins
Chaperone proteins within the endoplasmic reticulum play an essential role in facilitating the folding of newly synthesized proteins and in recognizing and segregating misfolded proteins, thereby preventing their transit to the Golgi.
Protein Folding at Stanford
Protein Motors
Interactome.org
Folding by Rotation about Single Bonds:
Since bond length and angles are fairly invariant in the known protein structures, the key to protein folding lies in the torsion angles of the backbone.
A torsion angles is defined by 4 atoms, A, B, C and D.
When atoms A, B, C and D are mainchain atoms (ie. the carboxylic carbon, C1; the alpha carbon, C2 or C-alpha; and the amide group nitrogen, N), There are THREE repeating torsion angles along the backbone chain called phi, psi and omega.
http://www.bmb.uga.edu/wampler/tutorial/prot2.html
Prion Diseases
Prion diseases or transmissible spongiform encephalopathies (TSEs) are a family of rare progressive neurodegenerative disorders that affect both humans and animals. They are distinguished by long incubation periods, characteristic spongiform changes associated with neuronal loss, and a failure to induce inflammatory response.
The causative agent of TSEs is believed to be a prion. A prion is an abnormal, transmissible agent that is able to induce abnormal folding of normal cellular prion proteins in the brain, leading to brain damage and the characteristics signs and symptoms of the disease. Prion diseases are usually rapidly progressive and always fatal.
