Association-induced folding of globular proteins.

It has generally been assumed that the aggregation of partially folded intermediates during protein refolding results in the termination of further protein folding. We show here, however, that under some conditions the association of partially folded intermediates can induce additional structure leading to soluble aggregates with many native-like properties. The amount of secondary structure in a monomeric, partially folded intermediate of staphylococcal nuclease was found to double on formation of soluble aggregates at high protein or salt concentrations. In addition, more globularity, as determined from Kratky plots of small-angle x-ray scattering data, was also noted in the associated states.

[1]  A. Fink.  Protein aggregation: folding aggregates, inclusion bodies and amyloid. , 1998, Folding & design.

[2]  F. Marston.  The purification of eukaryotic polypeptides synthesized in Escherichia coli. , 1986, The Biochemical journal.

[3]  Ken A. Dill,et al.  Aggregation of globular proteins , 1993 .

[4]  Y. Amemiya,et al.  Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. , 1996, Journal of Molecular Biology.

[5]  D. Shortle,et al.  The equilibrium folding pathway of staphylococcal nuclease: identification of the most stable chain-chain interactions by NMR and CD spectroscopy. , 1995, Biochemistry.

[6]  A. Fink,et al.  Classification of acid denaturation of proteins: intermediates and unfolded states. , 1994, Biochemistry.

[7]  Eaton E. Lattman,et al.  One-step evolution of a dimer from a monomeric protein , 1995, Nature Structural Biology.

[8]  E. Kaiser,et al.  Amphiphilic secondary structure: design of peptide hormones. , 1984, Science.

[9]  M. Manning,et al.  In vivo pathways of degradation and strategies for protein stabilization , 1992 .

[10]  A. Fink,et al.  Nativelike secondary structure in interleukin-1 beta inclusion bodies by attenuated total reflectance FTIR. , 1994, Biochemistry.

[11]  R. Jaenicke.  Folding and Association Versus Misfolding and Aggregation of Proteins , 1995 .

[12]  D Eisenberg,et al.  3D domain swapping: A mechanism for oligomer assembly , 1995, Protein science : a publication of the Protein Society.

[13]  N J Greenfield,et al.  Circular dichroism and optical rotatory dispersion of proteins and polypeptides. , 1973, Methods in Enzymology.

[14]  A. Fink,et al.  Characterization of the stable, acid‐induced, molten globule‐like state of staphylococcal nuclease , 1993, Protein science : a publication of the Protein Society.

[15]  M. Kataoka,et al.  Molten globule of cytochrome c studied by small angle X-ray scattering. , 1993, Journal of molecular biology.

[16]  P. Pedersen,et al.  Defective protein folding as a basis of human disease. , 1995, Trends in biochemical sciences.

[17]  M. Goldberg,et al.  Renaturation of Escherichia coli tryptophanase after exposure to 8 M urea. Evidence for the existence of nucleation centers. , 1974, European journal of biochemistry.

[18]  O. Glatter,et al.  19 – Small-Angle X-ray Scattering , 1973 .

[19]  A. Fink.  Compact intermediate states in protein folding. , 1995, Annual review of biophysics and biomolecular structure.

[20]  O. Ptitsyn,et al.  Molten globule and protein folding. , 1995, Advances in protein chemistry.

[21]  R. Jaenicke,et al.  Reconstitution of lactic dehydrogenase. Noncovalent aggregation vs. reactivation. 1. Physical properties and kinetics of aggregation. , 1979, Biochemistry.

[22]  K. Kuwajima,et al.  The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure , 1989, Proteins.

[23]  T. Noguti,et al.  Protein anatomy: spontaneous formation of filamentous helical structures from the N-terminal module of barnase. , 1993, Biochemistry.

[24]  A. Fink,et al.  Mechanism of acid-induced folding of proteins. , 1990, Biochemistry.

[25]  H. Orland,et al.  Partially folded states of proteins: characterization by X-ray scattering. , 1995, Journal of molecular biology.

[26]  P. S. Kim,et al.  Intermediates in the folding reactions of small proteins. , 1990, Annual review of biochemistry.