Hydrophobic collapse protein

AM Gutm, VI Abkevich, El Shakhnovich. Is burst hydrophobic collapse necessary for protein folding Biochemistry 34 3066-3076, 1995. 

Mok KH, Kuhn LT, Goez M, Day IJ, Lin JC, Andersen NH, Hore PJ (2007) A pre-existing hydrophobic collapse in the unfolded state of an ultrafast folding protein. Nature 447 106-109. 

Fernandez A, Kardos J, Goto Y. Protein folding could hydrophobic collapse be coupled with hydrogen-bond formation FEES Lett. 2003 536 187-192. 

However compelling, the scenario described above requires a rigorous justification that entails an understanding of the crossover behavior at a local level. This understanding prompts us to focus on the solvent environment of individual hydrogen bonds during the conformational exploration performed by the protein chain as the hydrophobic collapse takes place [12, 16, 17]. 

Woutersen, S. and Hamm, P. Isotope-edited two-dimensional vibrational spectroscopy of trialanine in aqueous solution, /. Chem. Phys., 114, 2727, 2001. Zhou, R.H., Huang, X.H., Margulis, C.J., Margulis, C.J., and Berne, B.J. Hydrophobic collapse in multidomain protein folding. Science, 305,1605, 2004. 

Finally, microcystin LY has a significantly larger stalk due to the parallel array of the Adda and Tyr side chains in a hydrophobic collapse-type interaction. If the size of this hydrophobic finger in the enzyme-bound state is conditioned by the size of the binding cleft of the protein phosphatases, dismption of the hydrophobic interaction between the Adda and Tyr side-chain is required for binding. The resulting large... 

In addition to the histogram methodology, this chapter has also described and applied overlap functions to analyze the structural behavior of the protein model during the cooling process. When applied in concert with the histogram calculations, the results indicate the system folds in two transitions. The first occurs at Tm 242 K, where the system undergoes a hydrophobic collapse to what could be referred to as a molten globule ... 

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