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Comment
. 2003 Sep 30;100(20):11195-7.
doi: 10.1073/pnas.2035072100. Epub 2003 Sep 23.

Caging helps proteins fold

D Thirumalai  1 , Dmitri K Klimov, George H Lorimer
Affiliations
Comment

Caging helps proteins fold

D Thirumalai et al. Proc Natl Acad Sci U S A. .
No abstract available

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Figures

Fig. 1.
Fig. 1.
Schematic sketch of a protein in a crowded cellular environment. The crowding agents (ribosomes, RNAs, proteins, lipids, ions, etc.) are denoted by different shapes and colors. The polypeptide chain is effectively confined to a cavity, which is shown as a sphere. Confinement induces substantial native structure in proteins as indicated by partially formed β-strands and α-helix (17).
Fig. 2.
Fig. 2.
Idealized phase diagram of confined two-state proteins as a function of temperature T and cavity size L. Localization of the substrate protein in GroEL is an example of confinement. The cavity is characterized by a single length scale L. For L > N3/5b (N is the number of amino acids and b is the monomer size) there are only two states, namely, native and denatured coil. For N1/3b < L < N3/5b the native state remains intact, whereas confinement induces collapse of the unfolded polypeptide chain (denoted by denatured collapsed state). The thick black line indicates phase transition between denatured and native states and is given by T ∼ L–(15/4). For L < N1/3b the native state is perturbed. At high temperatures the structures are squeezed and flexible, whereas at low temperatures they are rigid. The boundary between the two phases for L < N1/3b is only suggestive. The folding temperature in the bulk (L → ∞) is formula image.
See this image and copyright information in PMC

Comment on

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