A molten globule (MG) is a stable, partially folded protein structure found in mildly denaturing conditions such as low pH (generally pH = 2), mild denaturant, or high temperature. They are characterized by some native-like secondary structure but a dynamic tertiary structure as seen by far and near circular dichroism (CD) spectroscopy, respectively. These traits are similar to those observed in the trainsient intermediate states found during the folding of certain proteins and therefore the molten globule is believed to be analogous to protein folding intermediates. The MG structure is believed to lack most of the well packed amino acid side chains that characterize the native state (N) of a protein. The transition from a denatured (U) state to a molten globule may be a two state process A representation of the 3D structure of myoglobin, showing coloured alpha helices. ... In chemistry, an amino acid is any molecule that contains both amino and carboxylic acid functional groups. ... In biochemistry, the native state of a protein is its operative or functional form. ... In biochemistry, a compound that has been denatured has lost its native state, or in other words, no longer has the shape that is most compact and allows for optimal biological activity. ...
U ↔ MG
Or it may be a continuous transition, with no cooperativity and no apparent "switch" from one form to the other. In any event, a model that can be used in some proteins is a three step process: A cooperative (also co-operative or co-op) is an association of persons who join together to carry on an economic activity of mutual benefit, in an egalitarian fashion. ...
U ↔ MG ↔ N
One of the difficulties in de novo protein design is achieving the side chain packing needed to create a stable native state rather than a molten globules. Protein design is the design of new protein molecules from scratch. ...
These traits are similar to those observed in the trainsient intermediate states found during the folding of certain proteins and therefore the moltenglobule is believed to be analogous to protein folding intermediates.
Moreover, the moltenglobule states induced by adding HCI or NaCI to U^sub 1^ appear structurally different: in the A^sub 1^ state cyt-c is dimeric and less compact, whereas in the A^sub 2^ form the protein reverts to a globular-like conformation.
The moltenglobule is a compact denaturedprotein form, with a significantly native-like secondary structure but a largely flexible and disordered tertiary structure.
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