Native molten globules are the most folded kind of intrinsically disordered proteins. Little is known about the mechanism by which native molten globules bind to their cognate ligands to form fully folded complexes. The nuclear coactivator binding domain (NCBD) of CREB binding protein is particularly interesting in this respect as structural studies of its complexes have shown that NCBD folds i...

Proteins with highly specific binding properties constitute the basis for many important applications in biotechnology and medicine. Immunoglobulins have so far been the obvious choice but recent advances in protein engineering have provided several novel constructs that indeed challenge antibodies. One class of such binding proteins is based on the 58 residues three-helix bundle Z domain from ...

www.sciencemag.org SCIENCE VOL 323 20 FEBRUARY 2009 973 COVER Maltose binding protein (translucent), shown suspended in its molten globule state with chaperone protein SecB (yellow), destined for transport across the cellular membrane. The Gordon Research Conference on Visualization in Science & Education will be held 26 to 31 July 2009 at Magdalen College, Oxford, UK. The schedules for the 200...

The equilibrium properties of proteins are studied by Monte Carlo simulation of two simplified models of protein-like heteropolymers. These models emphasize the polymeric entropy of the fluctuating polypeptide chain. Our calculations suggest a generic phase diagram that contains a thermodynamically distinct "molten globule" state in addition to a rigid native state and a nontrivial unfolded sta...

When were they discovered? As early as the 1960s, there was evidence that under certain conditions protein molecules might have properties intermediate between the rigid native and fully unfolded states. The concept of such a protein as an intermediate in protein folding was suggested by the late Oleg Ptitsyn in the 1970s. A compact, partly folded protein was first observed experimentally in th...

We present entropy estimates based on molecular dynamics simulations of models of the molten globule state of the protein alpha-lactalbumin at low pH. The entropy calculations use the covariance matrix of atom-positional fluctuations and yield the complete configurational entropy. The configurational entropy of the entire protein and of each of its side chains is calculated. Exposed side chains...