Monitoring Protein Folding Using Time-Resolved Biophysical Techniques

Many of the biophysical techniques developed to characterize native proteins at equilibrium have now been adapted to the structural and thermodynamic characterization of transient species populated during protein folding. Recent advances in these techniques, the use of novel methods of initiating refolding, and a convergence of theoretical and experimental approaches are leading to a detailed understanding of many aspects of the folding process.

[1]  S. Radford,et al.  Probing the structure of folding intermediates , 1994 .

[2]  J. Markley,et al.  Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. , 1995, Biochemistry.

[3]  C. Dobson,et al.  Tertiary interactions in the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. , 1994, Biochemistry.

[4]  T. Oas,et al.  Submillisecond folding of monomeric lambda repressor. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[5]  V. Muñoz,et al.  Submillisecond kinetics of protein folding. , 1997, Current opinion in structural biology.

[6]  J. Widom,et al.  Kinetics of compaction during lysozyme refolding studied by continuous-flow quasielastic light scattering. , 1994, Biochemistry.

[7]  C. Dobson,et al.  Insights into protein folding using physical techniques: studies of lysozyme and alpha-lactalbumin. , 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[8]  C. Dobson,et al.  Protein folding kinetics from magnetization transfer nuclear magnetic resonance , 1984 .

[9]  I. Campbell,et al.  Rapid refolding of a proline-rich all-beta-sheet fibronectin type III module. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[10]  J. Baum,et al.  Real-time NMR investigations of triple-helix folding and collagen folding diseases. , 1997, Folding & design.

[11]  C. Dobson,et al.  Stopped-Flow Photo-CIDNP Observation of Protein Folding , 1997 .

[12]  H. Nicholson,et al.  Folding kinetics of T4 lysozyme and nine mutants at 12 degrees C. , 1992, Biochemistry.

[13]  B Balko,et al.  High resolution mixer for the study of the kinetics of rapid reactions in solution. , 1968, The Review of scientific instruments.

[14]  M. Engelhard,et al.  Experimental investigation of sidechain interactions in early folding intermediates. , 1996, Folding & design.

[15]  J. Hofrichter,et al.  Laser temperature jump study of the helix<==>coil kinetics of an alanine peptide interpreted with a 'kinetic zipper' model. , 1997, Biochemistry.

[16]  J. Onuchic,et al.  Toward an outline of the topography of a realistic protein-folding funnel. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[17]  F. Schmid Mechanism of folding of ribonuclease A. Slow refolding is a sequential reaction via structural intermediates. , 1983, Biochemistry.

[18]  C M Dobson,et al.  Collapse and cooperativity in protein folding. , 1996, Current opinion in structural biology.

[19]  Richard S. Johnson,et al.  Mass spectrometric measurement of protein amide hydrogen exchange rates of apo‐ and holo‐myoglobin , 1994, Protein science : a publication of the Protein Society.

[20]  H. Dyson,et al.  Characterization of a folding intermediate of apoplastocyanin trapped by proline isomerization. , 1993, Biochemistry.

[21]  P. Anfinrud,et al.  Time-resolved mid-infrared spectroscopy: methods and biological applications. , 1997, Current opinion in structural biology.

[22]  C. Dobson,et al.  A magnetization-transfer nuclear magnetic resonance study of the folding of staphylococcal nuclease. , 1989, Biochemistry.

[23]  M. J. Parker,et al.  Amide backbone and water-related H/D isotope effects on the dynamics of a protein folding reaction. , 1997, Biochemistry.

[24]  M. J. Parker,et al.  The development of tertiary interactions during the folding of a large protein. , 1996, Folding & design.

[25]  R. A. Goldbeck,et al.  Nanosecond time-resolved spectroscopy of biomolecular processes. , 1997, Annual review of biophysics and biomolecular structure.

[26]  L. Kay,et al.  Comparison of the backbone dynamics of a folded and an unfolded SH3 domain existing in equilibrium in aqueous buffer. , 1995, Biochemistry.

[27]  The Mass Spectrometry of Helical Unfolding in Peptides , 1994, Journal of the American Society for Mass Spectrometry.

[28]  C M Dobson,et al.  Protein Folding Monitored at Individual Residues During a Two-Dimensional NMR Experiment , 1996, Science.

[29]  E. Shakhnovich,et al.  Conserved residues and the mechanism of protein folding , 1996, Nature.

[30]  Nature of the early folding intermediate of ribonuclease A. , 1995 .

[31]  D. Naumann,et al.  Refolding of thermally and urea-denatured ribonuclease A monitored by time-resolved FTIR spectroscopy. , 1996, Biochemistry.

[32]  Christopher M. Dobson,et al.  Following protein folding in real time using NMR spectroscopy , 1995, Nature Structural Biology.

[33]  M Karplus,et al.  Theoretical studies of protein folding and unfolding. , 1995, Current opinion in structural biology.

[34]  Zhongqi Zhang,et al.  Probing the non-covalent structure of proteins by amide hydrogen exchange and mass spectrometry. , 1997, Journal of mass spectrometry : JMS.

[35]  M. Desmadril,et al.  Characterization of an intermediate in the folding pathway of phosphoglycerate kinase: chemical reactivity of genetically introduced cysteinyl residues during the folding process. , 1993, Biochemistry.

[36]  K. Hodgson,et al.  The Radius of Gyration of an Apomyoglobin Folding Intermediate , 1995, Science.

[37]  T. Oas,et al.  Microsecond protein folding through a compact transition state. , 1996, Journal of molecular biology.

[38]  P. A. Evans,et al.  Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates , 1995, Protein science : a publication of the Protein Society.

[39]  Zhongqi Zhang,et al.  Determination of amide hydrogen exchange by mass spectrometry: A new tool for protein structure elucidation , 1993, Protein science : a publication of the Protein Society.

[40]  C. Dobson,et al.  Investigation of protein folding by mass spectrometry , 1996, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[41]  H. Roder Structural characterization of protein folding intermediates by proton magnetic resonance and hydrogen exchange. , 1989, Methods in enzymology.

[42]  A. Fersht,et al.  Mapping the structures of transition states and intermediates in folding: delineation of pathways at high resolution. , 1995, Philosophical transactions of the Royal Society of London. Series B, Biological sciences.

[43]  Y. Kawata,et al.  Use of fluorescence energy transfer to characterize the compactness of the constant fragment of an immunoglobulin light chain in the early stage of folding. , 1991, Biochemistry.

[44]  A. Fersht,et al.  Formation of electrostatic interactions on the protein-folding pathway. , 1996, Biochemistry.

[45]  J. Hofrichter,et al.  Submillisecond protein folding kinetics studied by ultrarapid mixing. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[46]  A. Fersht,et al.  Single versus parallel pathways of protein folding and fractional formation of structure in the transition state. , 1994, Proceedings of the National Academy of Sciences of the United States of America.

[47]  P. Song,et al.  A conformational change associated with the phototransformation of Pisum phytochrome A as probed by fluorescence quenching. , 1994, Biochemistry.

[48]  A. Fersht,et al.  The refolding of cis- and trans-peptidylprolyl isomers of barstar. , 1993, Biochemistry.

[49]  M. Kataoka,et al.  X-ray solution scattering studies of protein folding. , 1996, Folding & design.

[50]  Carl Frieden,et al.  NMR and protein folding: Equilibrium and stopped‐flow studies , 1993, Protein science : a publication of the Protein Society.

[51]  J. L. Bailey,et al.  Techniques in protein chemistry , 1989 .

[52]  A. Fersht,et al.  Negative activation enthalpies in the kinetics of protein folding. , 1995, Proceedings of the National Academy of Sciences of the United States of America.

[53]  R. Dyer,et al.  Fast events in protein folding: relaxation dynamics of secondary and tertiary structure in native apomyoglobin. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[54]  C. Dobson,et al.  Detection of residue contacts in a protein folding intermediate. , 1997, Proceedings of the National Academy of Sciences of the United States of America.

[55]  M. Gruebele,et al.  Direct observation of fast protein folding: the initial collapse of apomyoglobin. , 1996, Proceedings of the National Academy of Sciences of the United States of America.

[56]  C. M. Jones,et al.  Fast events in protein folding initiated by nanosecond laser photolysis. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[57]  H. Gray,et al.  Protein Folding Triggered by Electron Transfer , 1996, Science.

[58]  Watching protein folding unfold , 1995, Nature Structural Biology.

[59]  F. Poulsen,et al.  Modification of a specific tyrosine enables tracing of the end‐to‐end distance during apomyoglobin folding , 1995, FEBS letters.

[60]  R. L. Baldwin Pulsed H/D-exchange studies of folding intermediates , 1993 .

[61]  Peggy A. Thompson,et al.  Laser temperature jump for the study of early events in protein folding , 1997 .

[62]  A. Fersht,et al.  Structure of the transition state for folding of a protein derived from experiment and simulation. , 1996, Journal of molecular biology.

[63]  T. Kiefhaber,et al.  Kinetic traps in lysozyme folding. , 1995, Proceedings of the National Academy of Sciences of the United States of America.