Tag Archives: protein folding
Molecular origins of convergence and uniqueness of protein structures!
Protein folding, tagged as an NP hard problem is the process by which a protein sequence acquires its biologically functional native structure, with a high-fidelity rate. Proteins are essential components of all body tissues, muscles and act
How fast do proteins break apart with light?
Proteins are microscopic machines that perform diverse functions in nature from transporting materials, to carrying out chemical reactions in the cell, to transmitting signals throughout the body. To do these tasks, the long protein chains must wrap
How do chaperones save protein folding?
Protein folding both in vitro and in vivo goes via formation of intermediate states. These “molten globule”-like states fluctuate, expose their hydrophobic sites and therefore easily aggregate. This retards or even inhibits formation of protein native structures,
With a little help from friends: how plastids aid the ER to deal with misfolded proteins
Almost a third of all proteins in eukaryotic cells are synthesized and folded in the endoplasmic reticulum (ER) before being secreted and redistributed to other organelles, such as the Golgi apparatus, lysosomes, and the plasma membrane. To
Cold denaturation
Most proteins can be thought like beady chains which form compact well-ordered coils whose surface protects the greasy-like interior from the contact with water molecules. We are studying what are the forces which keep the coil compact.
Two views on the protein folding puzzle
Protein chain folding is a miracle. The protein chain is gene-encoded and initially has no structure (Fig. 1, left panel). Its intricate structure (Fig. 1, right), with every atom in its unique position, results from spontaneous folding.
