Welcome to the

FINK RESEARCH GROUP

Department of Chemistry and Biochemistry, University of California, Santa Cruz, CA 95064

RECENT PUBLICATIONS

Fink, A. L. and Uversky, V. N., eds. (2006) “Protein misfolding, aggregation and conformational disease’ Part A”, Springer.

Fink, A. L (2006) The Aggregation and Fibrillation of a-Synuclein, Accts. Chem. Res. in press

Zhu, M., Qin, Z., Hu, D., Munishkina L. A. and Fink, A. L (2006) “a-Synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles” 45, 8135-42

Hong, D, Ahmad, A. and Fink, A. L.(2006) “Fibrillation of Human Insulin A and B-Chains” Biochemistry 45, 9342-53.

Zhou W, Zhu M, Wilson M.A, Petsko G.A, Fink A.L. (2006) The oxidation state of DJ-1 regulates its chaperone activity toward alpha-synuclein. J Mol Biol. 356, 1036-48

Dusa A, Kaylor J, Edridge S, Bodner N, Hong DP, Fink AL. (2006) Characterization of Oligomers during alpha-Synuclein Aggregation Using Intrinsic Tryptophan Fluorescence. Biochemistry, 45, 2752-60.

Fink, A. L. (2006) The aggregation and fibrillation of alpha-synuclein, Acc. Chem Res. 39, 628-634.

Zhu, M., Qin, Z. J., Hu, D., Munishkina, L. A., and Fink, A. L. (2006) Alpha-synuclein can function as an antioxidant preventing oxidation of unsaturated lipid in vesicles, Biochemistry 45, 8135-8142.

Fink, A. L. (2005). Natively unfolded proteins. Curr. Opin. Struct. Biol. 15, 35-41.

Glaser, C. B., Yamin, G., Uversky, V. N. & Fink, A. L. (2005). Methionine oxidation, alpha-synuclein and Parkinson's disease. Biochim. Biophys. Acta 1703, 157-169.

Hong, D. P. & Fink, A. L. (2005). Independent heterologous fibrillation of insulin and its B-chain Peptide. Biochemistry 44, 16701-16709.

Kaylor, J., Bodner, N., Edridge, S., Yamin, G., Hong, D. P. & Fink, A. L. (2005). Characterization of Oligomeric Intermediates in alpha-Synuclein Fibrillation: FRET Studies of Y125W/Y133F/Y136F alpha-Synuclein. J. Mol. Biol.

Liu, I. H., Uversky, V. N., Munishkina, L. A., Fink, A. L., Halfter, W. & Cole, G. J. (2005). Agrin Binds {alpha}-Synuclein and Modulates {alpha}-Synuclein Fibrillation. Glycobiology.

Uversky, V. N., Yamin, G., Munishkina, L. A., Karymov, M. A., Millett, I. S., Doniach, S., Lyubchenko, Y. L. & Fink, A. L. (2005). Effects of nitration on the structure and aggregation of alpha-synuclein. Brain Res. Mol. Brain Res. 134, 84-102.

Yamin, G., Munishkina, L. A., Karymov, M. A., Lyubchenko, Y. L., Uversky, V. N. & Fink, A. L. (2005). Forcing Nonamyloidogenic beta-Synuclein To Fibrillate. Biochemistry 44, 9096-9107.

Uversky, V. N., Yamin, G., Munishkina, L. A., Karymov, M. A., Millett, I. S., Doniach, S., Lyubchenko, Y. L., and Fink, A. L. (2005) Effects of nitration on the structure and aggregation of alpha-synuclein, Brain Res. Mol. Brain Res. 134, 84-102.

Li, J., Zhu, M., Rajamani, S., Uversky, V. N., and Fink, A. L. (2004) Rifampicin inhibits alpha-synuclein fibrillation and disaggregates fibrils, Chem. Biol. 11, 1513-1521.

Munishkina, L. A., Cooper, E. M., Uversky, V. N., and Fink, A. L. (2004) The effect of macromolecular crowding on protein aggregation and amyloid fibril formation, J. Mol. Recognit. 17, 456-464.

Munishkina, L. A., Fink, A. L., and Uversky, V. N. (2004) Conformational prerequisites for formation of amyloid fibrils from histones, J. Mol. Biol. 342, 1305-1324.

Uversky, V. N. and Fink, A. L. (2004) Conformational constraints for amyloid fibrillation: the importance of being unfolded, Biochim. Biophys. Acta 1698, 131-153.

Zhu, M., Rajamani, S., Kaylor, J., Han, S., Zhou, F., and Fink, A. L. (2004) The flavonoid baicalein inhibits fibrillation of alpha-synuclein and disaggregates existing fibrils, J. Biol. Chem. 279, 26846-26857.

Hokenson, M. J., Uversky, V. N., Goers, J., Yamin, G., Munishkina, L. A., and Fink, A. L. (2004) Role of individual methionines in the fibrillation of methionine-oxidized alpha-synuclein, Biochemistry 43, 4621-4633.

Li, J., Zhu, M., Manning-Bog, A. B., Di Monte, D. A., and Fink, A. L. (2004) Dopamine and L-dopa disaggregate amyloid fibrils: implications for Parkinson's and Alzheimer's disease, FASEB J. 18, 962-964.

Zhu, M., Han, S., Zhou, F., Carter, S. A., and Fink, A. L. (2004) Annular oligomeric amyloid intermediates observed by in situ atomic force microscopy, J. Biol. Chem. 279, 24452-24459.

Munishkina, L. A., Henriques, J., Uversky, V. N., and Fink, A. L. (2004) Role of protein-water interactions and electrostatics in alpha-synuclein fibril formation, Biochemistry 43, 3289-3300.

Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2004) Stimulation of insulin fibrillation by urea-induced intermediates, J. Biol. Chem. 279, 14999-15013.

Ahmad, A., Millett, I. S., Doniach, S., Uversky, V. N., and Fink, A. L. (2003) Partially folded intermediates in insulin fibrillation, Biochemistry 42, 11404-11416.

Khurana, R., Souillac, P. O., Coats, A. C., Minert, L., Ionescu-Zanetti, C., Carter, S. A., Solomon, A., and Fink, A. L. (2003) A model for amyloid fibril formation in immunoglobulin light chains based on comparison of amyloidogenic and benign proteins and specific antibody binding, Amyloid. 10, 97-109.

Zhu, M., Li, J., and Fink, A. L. (2003) The association of alpha-synuclein with membranes affects bilayer structure, stability, and fibril formation, J. Biol. Chem. 278, 40186-40197.

Khurana, R., Ionescu-Zanetti, C., Pope, M., Li, J., Nielson, L., Ramirez-Alvarado, M., Regan, L., Fink, A. L., and Carter, S. A. (2003) A general model for amyloid fibril assembly based on morphological studies using atomic force microscopy, Biophys. J. 85, 1135-1144.

Goers, J., Manning-Bog, A. B., McCormack, A. L., Millett, I. S., Doniach, S., Di Monte, D. A., Uversky, V. N., and Fink, A. L. (2003) Nuclear localization of alpha-synuclein and its interaction with histones, Biochemistry 42, 8465-8471.

Berriman, J., Serpell, L. C., Oberg, K. A., Fink, A. L., Goedert, M., and Crowther, R. A. (2003) Tau filaments from human brain and from in vitro assembly of recombinant protein show cross-beta structure, Proc. Natl. Acad. Sci. U. S. A 100, 9034-9038.

Souillac, P. O., Uversky, V. N., and Fink, A. L. (2003) Structural transformations of oligomeric intermediates in the fibrillation of the immunoglobulin light chain LEN, Biochemistry 42, 8094-8104.

Yamin, G., Glaser, C. B., Uversky, V. N., and Fink, A. L. (2003) Certain metals trigger fibrillation of methionine-oxidized alpha-synuclein, J. Biol. Chem. 278, 27630-27635.

Yamin, G., Uversky, V. N., and Fink, A. L. (2003) Nitration inhibits fibrillation of human alpha-synuclein in vitro by formation of soluble oligomers, FEBS Lett. 542, 147-152.

Uversky, V. N., Garriques, L. N., Millett, I. S., Frokjaer, S., Brange, J., Doniach, S., and Fink, A. L. (2003) Prediction of the association state of insulin using spectral parameters, J. Pharm. Sci. 92, 847-858.

Goers, J., Uversky, V. N., and Fink, A. L. (2003) Polycation-induced oligomerization and accelerated fibrillation of human alpha-synuclein in vitro, Protein Sci. 12, 702-707.

Zhu, M. and Fink, A. L. (2003) Lipid binding inhibits alpha-synuclein fibril formation, J. Biol. Chem. 278, 16873-16877.

Munishkina, L. A., Phelan, C., Uversky, V. N., and Fink, A. L. (2003) Conformational behavior and aggregation of alpha-synuclein in organic solvents: modeling the effects of membranes, Biochemistry 42, 2720-2730.

Denning, D. P., Patel, S. S., Uversky, V., Fink, A. L., and Rexach, M. (2003) Disorder in the nuclear pore complex: the FG repeat regions of nucleoporins are natively unfolded, Proc. Natl. Acad. Sci. U. S. A 100, 2450-2455.

Abramov, V. M., Vasiliev, A. M., Khlebnikov, V. S., Vasilenko, R. N., Kulikova, N. L., Kosarev, I. V., Ishchenko, A. T., Gillespie, J. R., Millett, I. S., Fink, A. L., and Uversky, V. N. (2002) Structural and functional properties of Yersinia pestis Caf1 capsular antigen and their possible role in fulminant development of primary pneumonic plague, J. Proteome. Res. 1, 307-315.

Uversky, V. N., Permyakov, S. E., Zagranichny, V. E., Rodionov, I. L., Fink, A. L., Cherskaya, A. M., Wasserman, L. A., and Permyakov, E. A. (2002) Effect of zinc and temperature on the conformation of the gamma subunit of retinal phosphodiesterase: a natively unfolded protein, J. Proteome. Res. 1, 149-159.

Li, J., Uversky, V. N., and Fink, A. L. (2002) Conformational behavior of human alpha-synuclein is modulated by familial Parkinson's disease point mutations A30P and A53T, Neurotoxicology 23, 553-567.

Uversky, V. N., Li, J., Bower, K., and Fink, A. L. (2002) Synergistic effects of pesticides and metals on the fibrillation of alpha-synuclein: implications for Parkinson's disease, Neurotoxicology 23, 527-536.

Goers, J., Permyakov, S. E., Permyakov, E. A., Uversky, V. N., and Fink, A. L. (2002) Conformational prerequisites for alpha-lactalbumin fibrillation, Biochemistry 41, 12546-12551.

Zhu, M., Souillac, P. O., Ionescu-Zanetti, C., Carter, S. A., and Fink, A. L. (2002) Surface-catalyzed amyloid fibril formation, J. Biol. Chem. 277, 50914-50922.

Uversky, V. N. and Fink, A. L. (2002) Amino acid determinants of alpha-synuclein aggregation: putting together pieces of the puzzle, FEBS Lett. 522, 9-13.

Denning, D. P., Uversky, V., Patel, S. S., Fink, A. L., and Rexach, M. (2002) The Saccharomyces cerevisiae nucleoporin Nup2p is a natively unfolded protein, J. Biol. Chem. 277, 33447-33455.

Uversky, V. N., Yamin, G., Souillac, P. O., Goers, J., Glaser, C. B., and Fink, A. L. (2002) Methionine oxidation inhibits fibrillation of human alpha-synuclein in vitro, FEBS Lett. 517, 239-244.

Kuznetsova, I. M., Stepanenko, O. V., Turoverov, K. K., Zhu, L., Zhou, J. M., Fink, A. L., and Uversky, V. N. (2002) Unraveling multistate unfolding of rabbit muscle creatine kinase, Biochim. Biophys. Acta 1596, 138-155.

Uversky, V. N., Cooper, M., Bower, K. S., Li, J., and Fink, A. L. (2002) Accelerated alpha-synuclein fibrillation in crowded milieu, FEBS Lett. 515, 99-103.

Uversky, V. N. and Fink, A. L. (2002) The chicken-egg scenario of protein folding revisited, FEBS Lett. 515, 79-83.

Souillac, P. O., Uversky, V. N., Millett, I. S., Khurana, R., Doniach, S., and Fink, A. L. (2002) Effect of association state and conformational stability on the kinetics of immunoglobulin light chain amyloid fibril formation at physiological pH, J. Biol. Chem. 277, 12657-12665.

Souillac, P. O., Uversky, V. N., Millett, I. S., Khurana, R., Doniach, S., and Fink, A. L. (2002) Elucidation of the molecular mechanism during the early events in immunoglobulin light chain amyloid fibrillation. Evidence for an off-pathway oligomer at acidic pH, J. Biol. Chem. 277, 12666-12679.

Cohlberg, J. A., Li, J., Uversky, V. N., and Fink, A. L. (2002) Heparin and other glycosaminoglycans stimulate the formation of amyloid fibrils from alpha-synuclein in vitro, Biochemistry 41, 1502-1511.

Uversky, V. N., Li, J., Souillac, P., Millett, I. S., Doniach, S., Jakes, R., Goedert, M., and Fink, A. L. (2002) Biophysical properties of the synucleins and their propensities to fibrillate: inhibition of alpha-synuclein assembly by beta- and gamma-synucleins, J. Biol. Chem. 277, 11970-11978.

Manning-Bog, A. B., McCormack, A. L., Li, J., Uversky, V. N., Fink, A. L., and Di Monte, D. A. (2002) The herbicide paraquat causes up-regulation and aggregation of alpha-synuclein in mice: paraquat and alpha-synuclein, J. Biol. Chem. 277, 1641-1644.

Uversky, V. N. Lee , H. J., Li, J., Fink, A. L. & Lee, S. J. (2001) Stabilization of Partially Folded Conformation During a-Synuclein Oligomerization in Both Purified and Cytosolic Preparations. J. Biol. Chem. 276, 43495-43498.

Uversky, V. N., Li, J. & Fink, A. L. (2001) Trimethylamine-N-Oxide-Induced Folding of a-Synuclein. FEBS Lett. 509, 31-35.

Manning-Bog, A. B., McCormack, A. L., Li, J., Uversky, V. N., Fink, A. L. and Di Monte, D. A. (2002) The Herbicide Paraquat Causes Upregulation and Aggregation of a-Synuclein in Mice. J. Biol. Chem. 277, 1641-1644.

Uversky, V. N. & Fink, A. L. (2001) Metal-Triggered Structural Transformations, Aggregation and Fibrillation of Human a-Synuclein. A Possible Molecular Link Between Parkinson’s Disease and Heavy Metal Exposure J. Biol. Chem. 276, 44284.

Nielsen, L., Khurana, R., Coats, A., Frokjaer, S., Brange, J., Vyas, S., Uversky, V. N. & Fink, A. L. (2001) Effect of environmental factors on the kinetics of insulin fibril formation: elucidation of the molecular mechanism. Biochemistry 40, 6036-6046.

Li, J., Uversky, V. N. & Fink, A. L. (2001) Effect of Familial Parkinson’s Disease Point Mutations A30P and A53T on the Structural Properties, Aggregation and Fibrillation of Human a-synuclein. Biochemistry 40, 11604-11613.

Uversky, V. N., Li, J. & Fink, A. L. (2001) Pesticides directly accelerate the rate of alpha-synuclein fibril formation: a possible factor in Parkinson's disease. FEBS Lett. 500 , 105-108.

Khurana, R. Gillespie, J. R., Talapatra, A., Minert, L. J. Ionescu-Zanetti, C., Millett, I. and Fink, A. L. (2001) Partially-folded intermediates as critical precursors of light chain amyloid fibrils and amorphous aggregates. Biochemistry 40, 3525-35.

Nielsen, L., Frokjaer, S., Brange, J., Uversky, V. N. & Fink, A. L. (2001) Probing the Mechanism of Insulin Fibril Formation with Insulin Mutants. Biochemistry 40, 8397-8409.

Uversky, V. N., Li, J. & Fink, A. L. (2001) Evidence for a Partially-Folded Intermediate in alpha-Synuclein Fibril Formation. J. Biol. Chem. 276, 10737-44.

Abramov, V. M., Vasiliev, A. M., Vasilenko, R. N., Kulikova, N. L., Kosarev, I. V., Khlebnikov, V. S., Ishchenko, A. T., MacIntyre, S., Gillespie, J. R., Khurana, R. et al. (2001) Structural and functional similarity between Yersinia pestis capsular protein Caf1 and human interleukin-1beta. Biochemistry 40, 6076-6084.

Nishimura, C., Uversky, V. N. & Fink, A. L. (2001) The Effect of Salts on the Stability and Folding of Staphylococcal Nuclease. Biochemistry 40, 2113-28.

Khurana, R., Uversky, V. N., Nielsen, L. & Fink, A. L. (2001) Is Congo Red an Amyloid-specific Dye? J. Biol. Chem. 276, 22715-22721.

Uversky, V. N., Gillespie, J. R., Millett, I. S., Khodyakova, A. V., Vasilenko, R. N., Vasiliev, A. M., Rodionov, I. L., Kozlovskaya, G. D., Dolgikh, D. A., Fink, A. L., Doniach, S., Permyakov, E. A. and Abramov, V. M. (2000) Zn²⁺-Mediated Structure Formation and Compaction of the “Natively Unfolded” Human Prothymosin. Biochemical and Biophysical Research Communications 267, 663–668.

Lietz, E. J., Truher, H., Kahn, D., Hokenson, M. J. & Fink, A. L. (2000) Lysine-73 is involved in the acylation and deacylation of beta- lactamase. Biochemistry 39, 4971-4981.

Khurana, R. & Fink, A. L. (2000) Do parallel beta-helix proteins have a unique Fourier transform infrared spectrum? Biophys. J. 78, 994-1000.

Frate, M. C., Lietz, E. J., Santos, J., Rossi, J. P., Fink, A. L. & Ermacora, M. R. (2000) Export and folding of signal-sequenceless Bacillus licheniformis beta-lactamase in Escherichia coli. Eur. J. Biochem. 267, 3836-3847.

Hokenson, M. J., Cope, G. A., Lewis, E. R., Oberg, K. A. & Fink, A. L. (2000) Enzyme-Induced Strain/Distortion in the Ground-State ES Complex in beta- Lactamase Catalysis Revealed by FTIR. Biochemistry 39, 6538-6545.

Nishimura, C., Riley, R., Eastman, P. & Fink, A. L. (2000) Fluorescence Energy Transfer Indicates Similar Transient and Equilibrium Intermediates in Staphylococcal Nuclease Folding. J. Mol. Biol. 299, 1133-1146.

Uversky, V. N. Gillespie, J. R. and Fink, A. L. (2000) Why are "natively unfolded" proteins unstructured under physiological conditions? Proteins: Structure, Function and Genetics, 41, 415-427.

Fezoui, Y., Hartley, D. M., Harper, J. D., Khurana, R., Walsh, D. M., Condron, M. M., Selkoe, D. J., Lansbury, P. T., Jr., Fink, A. L. & Teplow, D. B. (2000) An improved method of preparing the amyloid beta-protein for fibrillogenesis and neurotoxicity experiments. Amyloid. 7, 166-178.

Uversky, V. N. Gillespie, J. R, Millet, I. S., Khodyakova, A. V., Vasiliev, A. M., Chernovskaya, T. V., Vasilenko, R. N., Kozlovskaya, G. D., Dolgikh, D. A., Fink, A. L., Doniach, S. and Abramov, V. M. "Natively Unfolded" Human Prothymosin a Adopts Partially-Folded Conformation At Acidic pH. Biochemistry, 38, 15009-15016 (1999)

Uversky, V. N., Talapatra, A., Gillespie J. R. and Fink, A. L. (1999) Protein Deposits as the Molecular Basis of Amyloidosis: Part II. Localized amyloidosis and neurodegenerative disorders. Medical Science Monitor 5, 1238-1254, 1999.

Uversky, V. N., Talapatra, A., Gillespie J. R. and Fink, A. L. (1999) Protein Deposits as the Molecular Basis of Amyloidosis: Part I. Systemic amyloidosis. Medical Science Monitor 5, 1001-1012, 1999.

Segel, D. J., Uversky, V. N., Fink, A. L., Hodgson, K. O. and Doniach, S. (1999) Transient Dimer in the Refolding Kinetics of Cytochrome c Characterized by Small Angle X-ray Scattering. Biochemistry, 38, 15352-15359.

Ionescu-Zanetti, C., Khurana, R., Gillespie, J. R., Petrick, J., Trabachino, L. C., Minert, L. J., Carter, S. A. and Fink, A. L. (1999) Monitoring the assembly of Ig light-chain amyloid fibrils by atomic force microscopy. Proc. Nat. Acad. Sci. 96, 13175-13179.

Uversky,V.N., A.S.Karnoup, R.Khurana, D.J.Segel, S.Doniach, and A.L.Fink. 1999. Association of partially-folded intermediates of staphylococcal nuclease induces structure and stability. Protein Science 8:161-173.

Seshadri,S., R.Khurana, and A.L.Fink. 1999. FTIR Analysis of Protein Deposits. Methods in Enzymology 309:559-576.

Fink,A.L., S.Seshadri, R.Khurana, and K.A.Oberg. 1999. Determination of Secondary Structure in Protein Aggregates Using Attenuated Total Reflectance (ATR) FTIR. In Infrared Analysis of Peptides and Proteins. B.R.Singh, editor. pp. 132-144. Amer. Chemical Society, NY.

Fink,A.L. 1999. Chaperone-mediated protein folding. Physiol Rev. 79:425-449.

Chirico, W. J., Markey, M. L. and Fink, A. L. (1998) Conformational changes of an Hsp70 molecular chaperone induced by nucleotides, polypeptides, and N-ethylmaleimide. Biochemistry. 37, 13862-70.

Segel,D.J., A.L.Fink, K.O.Hodgson, and S.Doniach. (1998) Protein denaturation: a small-angle X-ray scattering study of the ensemble of unfolded states of cytochrome c. Biochemistry 37:12443-12451.

Chen, E., Wood, M. J., Fink, A. L. and Kliger, D. S. (1998) Time-resolved circular dichroism studies of protein folding intermediates of cytochrome c. Biochemistry 37, 5589-5598.

Uversky, V.N., Segel, D.J., Doniach, S. and Fink, A. L. (1998) Association-induced Folding of Globular proteins. Proc. Nat. Acad. Sci. 95, 5480-5483.

Uversky, V.N. & Fink, A.L. (1998). Anion-Induced Folding of Staphylococcal Nuclease: Characterization of Multiple Equilibrium Folding Intermediates. J. Mol. Biol. 278:4, 879-894.

Fink, A. L. (1998) Protein Aggregation: Folding aggregates, inclusion bodies and amyloid. Folding & Design, 3, R9-R23.

Oberg, K. A. and Fink, A. L. (1998) A New Attenuated Total Reflectance Fourier Transform Infrared Spectroscopy Method for the Study of Proteins in Solution. Anal. Biochem. 256, 92-106.

Veeraraghavan, S., Nall, B. T. and Fink, A. L. Effect of Prolyl Isomerase on the Folding Reactions of Staphylococcal Nuclease. Biochemistry, 36, 15134-15139 (1997).

Fink, A. L., Oberg, K. A. and Seshadri, S. Discrete intermediates vs. molten globule models of protein folding: Characterization of partially-folded intermediates of apomyoglobin. Folding & Design, 3, 19-25 (1997).

Fink, A. L. and Goto, Y. eds. Molecular Chaperones in the Life Cycle of Proteins: Structure, Function, and Mode of Action Marcel Dekker, pubs. New York, NY. 1997

Hardt, K., Joris, B., Lepage, S., Brasseur, R., Lampen, J. O., Frere, J-M., Fink, A. L. and Ghuysen, J-M. "The penicillin sensory-transducer BlaR involved in the inducibility of b-lactamase synthesis in B. licheniformis is embedded in the plasma membrane via a four-helix bundle" Molecular Microbiol. 23, 935-944 (1997).

Lewis, E. R., Winterberg, K. M. and Fink, A. L., "A Point Mutation Leads to Altered Product Specificity in b-Lactamase Catalysis", Proc. Native. Acad. Sci. US. 94, 443-447 (1997).

Reid, K. L. and Fink, A. L. "Physical Interactions between members of the DnaK Chaperone Machinery: DnaK and GrpE", Cell Stress and Chaperones, 1, 127-137 (1996).

Li Shi, Mikio Kataoka and Anthony L. Fink, "Conformational characterization of DnaK and its complexes by small-angle-X-ray scattering", Biochemistry, 35, 2997-3308 (1996).

Fink, A. L. "Compact Intermediate States in Protein Folding." Annual Reviews of Biophysics and Biomolecular Structure, 24, 495-522 (1995).

Palleros, D. R., Shi, L., Reid, K., and Fink A. L. "Hsp70-protein complexes: Their characterization by size-exclusion HPLC." In Techniques in Protein Chemistry VI., ed. J. W. Crabb, Academic Press, Inc. 467-474 (1995).

Fink, A. L., "Molten Globules." Methods in Molecular Biology: Protein Stability and Folding, ed. Bret A. Shirley, vol. 40, 343-360 (1995).

Osuna, J., Viadiu, H., Fink, A. L. and Soberón, X., "Substitution of Asp for Asn at position 132 in the active site of TEM-b-lactamase: activity towards different substrates and effects of neighboring residues." J. Biol. Chem. 270, 781-787 (1995).

Viadiu, H., Osuna, J., Fink, A. L. and Soberón, X., "A new TEM-b-lactamase double mutant with broadened specificity reveals substrate dependent functional interactions." J. Biol. Chem. 270, 775-780 (1995).

Oberg, K. A. And Fink, A. L. Methods for Collecting and Analyzing Attenuated Total Reflectance FTIR Spectra of Proteins in Solution. In Techniques in Protein Chemistry VI., ed. J. W. Crabb, Academic Press, Inc. (1995) 475-484.

Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T. and Palleros, D. R., "Classification of Acid Denaturation of Proteins: Intermediates and Unfolded States." Biochemistry, 33, 12504-12511 (1994).

Escobar, W. A., Miller, J. and Fink, A. L., "Effects of Site-Specific Mutagenesis of Tyrosine 105 in a Class A b-Lactamase." Biochem. J. 303, 555-558 (1994).

Escobar, W. A., Tan, A. K., Lewis, E. R. and Fink, A. L., "Site Directed Mutagenesis of Glutamate-166 in b-Lactamase Leads to Branched Path Mechanism." Biochemistry 33, 7619-7626 (1994).

Shi, L., Palleros, D. R. and Fink, A. L., "Protein Conformational Changes Induced by bis-ANS: Preferential Binding to the Molten Globule of DnaK." Biochemistry 33, 7536-7546 (1994).

Fink, A. L., "Compact Intermediates States in Protein Folding." Sub-cellular Biochemistry: Protein structure, function and engineering, ed. S. Roy, vol. 24, 27-53 (1994).

Palleros, D. R., Shi, L., Reid, K. L. & Fink, A. L. "Hsp70-Protein Complexes: Complex stability and Conformation of Bound Substrate Protein" J. Biol. Chem. 269, 13107-13114 (1994).

Seshadri, S., Oberg, K. A. and Fink, A. L., "Thermally Denatured Ribonuclease A Retains Secondary Structure as Shown by FTIR." Biochemistry 33, 1351-1355 (1994).

Oberg, K., Chrunyk, B. A., Wetzel, R. B., and Fink, A. L. "Native-Like Secondary Structure in Interleukin-1b Inclusion Bodies by Attenuated Total Reflectance FTIR." Biochemistry, 33, 2628-2634 (1994).

Palleros, D. R., Reid, K. L., Shi, L. and Fink, A. L. "DnaK ATPase activity revisited" FEBS Letts., 336, 124-128, 1993.

DeYoung, L. D., Fink, A. L. and Dill, K. A. "Aggregation of Globular Proteins" Accts. Chem. Res. 26, 614-620, 1993.

Palleros, D. R., Reid, K. L., Shi, L., Welch, W. J. and Fink, A. L., "ATP-induced protein-hsp70 complex dissociation requires K+ and does not involve ATP hydrolysis. " Nature, 365, 664-666 (1993).

Hamada, D., Hoshino, M., Kataoka, M., Fink, A. L. and Goto, Y., "Intermediate Conformational States of Apocytochrome c", Biochemistry, 32, 10351-10358 (1993).

Nakano, T., Antonino, L. C., Fox., R. O. and Fink, A. L. "Effect of Proline Mutations on the Stability and Kinetics of Folding of Staphylococcal Nuclease." Biochemistry 32, 2534-2541 (1993).

Palleros, D. R., Shi, L., Reid, K. L. and Fink, A. L. "Three-state denaturation of DnaK induced by guanidine hydrochloride. Evidence for an expandable intermediate." Biochemistry 32, 4314-4321 (1993).

Fink, A. L., Calciano, L. J., Goto, Y., Nishimura, M. and Swedberg, S. A. "Characterization of the Stable, Acid-Induced, Molten Globule-like State of Staphylococcal Nuclease." Protein Science 2, 1155-1160 (1993).

DeYoung, L. R., Dill, K. A. and Fink, A. L. "Aggregation and Denaturation of Apomyoglobin in Aqueous Urea Solutions." Biochemistry 32, 3877-3886 (1993).

Calciano, L. J., Escobar, W. A., Millhauser, G. L., Miick, S. M., Rubaloff, J., Todd, A P. and Fink, A. L. "Side-chain Mobility of the *-Lactamase A State Probed by Electron Spin Resonance Spectroscopy." Biochemistry 32, 5644-5649 (1993).

Knox, J. R., Moews, P. C., Escobar, W. A. and Fink, A. L. "A catalytically-impaired class A *-lactamase: 2 Å crystal structure and kinetics of the Bacillus licheniformis E166A mutant." Protein Engineering, 6, 11-18 (1993).

Hagihara, Y., Aimoto, S., Fink, A. L., and Goto, Y. "Guanidine Hydrochloride-induced Folding of Proteins." J. Mol. Biol. 231, 180-184 (1993).