-
1
-
-
0005560065
-
Protein folding
-
Dobson CM, Fersht AR (Eds): Protein folding. Philos Trans R Soc Lond Biol 1995, 348:1-119. An extensive collection of 14 articles associated with a discussion meeting on protein folding held in October 1994. The topics include experimental, theoretical and in vivo studies.
-
(1995)
Philos Trans R Soc Lond Biol
, vol.348
, pp. 1-119
-
-
Dobson, C.M.1
Fersht, A.R.2
-
2
-
-
0027382315
-
Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: A critical test of the protein engineering method of analysis
-
Jackson SE, Elmasry N, Fersht AR: Structure of the hydrophobic core in the transition state for folding of chymotrypsin inhibitor 2: a critical test of the protein engineering method of analysis. Biochemistry 1993, 32:11270-11278.
-
(1993)
Biochemistry
, vol.32
, pp. 11270-11278
-
-
Jackson, S.E.1
Elmasry, N.2
Fersht, A.R.3
-
3
-
-
0029003514
-
Folding of a four-helix bundle: Studies of acyl-coenzyme a binding protein
-
Kragelund BB, Robinson CV, Knudsen J, Dobson CM, Poulsen FM: Folding of a four-helix bundle: studies of acyl-coenzyme A binding protein. Biochemistry 1995, 34:7217-7224. The refolding of a four-helix bundle is characterized by several stopped and quenched flow techniques as rapid (<5 ms at 25°C) and two-state. Refolding from guanidine hydrochloride and acid-denatured states was found to be closely similar. This behaviour was associated with the absence of slow reorganization steps in the folding process of this small protein.
-
(1995)
Biochemistry
, vol.34
, pp. 7217-7224
-
-
Kragelund, B.B.1
Robinson, C.V.2
Knudsen, J.3
Dobson, C.M.4
Poulsen, F.M.5
-
4
-
-
0029049321
-
Extremely rapid protein folding in the absence of intermediates
-
Schindler T, Herrler M, Marahiel MA, Schmid FX: Extremely rapid protein folding in the absence of intermediates. Nature Struct Biol 1995, 2:663-673. Equilibrium and kinetic studies over a wide range of denaturant conditions are consistent with two-state refolding behaviour of a five-stranded β barrel. Under optimal conditions, the folding is fast (<1.5 ms).
-
(1995)
Nature Struct Biol
, vol.2
, pp. 663-673
-
-
Schindler, T.1
Herrler, M.2
Marahiel, M.A.3
Schmid, F.X.4
-
5
-
-
0028958601
-
Characterizing transition states in protein folding: An essential step in the puzzle
-
Fersht AR: Characterizing transition states in protein folding: an essential step in the puzzle. Curr Opin Struct Biol 1995, 5:79-84. A review of the application of site-directed mutagenesis techniques to the exploration of protein folding. Particular attention is paid to the characterization of the transition state in barnase and Cl2.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 79-84
-
-
Fersht, A.R.1
-
6
-
-
0027948175
-
Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding
-
Otzen DE, Itzhaki LS, Elmasry NF, Jackson SE, Fersht AR: Structure of the transition state for the folding/unfolding of the barley chymotrypsin inhibitor 2 and its implications for mechanisms of protein folding. Proc Natl Acad Sci USA 1994, 91:10422-10425. The transition state of the two-state refolding of Cl2 is characterized by analyzing the kinetic and equilibrium effects of 74 mutations at 37 sites. Most mutations result in a significant decrease in the localized stability of the transition state compared to the folded protein. The transition state is interpreted as resembling an expanded form of the native protein structure.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10422-10425
-
-
Otzen, D.E.1
Itzhaki, L.S.2
Elmasry, N.F.3
Jackson, S.E.4
Fersht, A.R.5
-
7
-
-
0028037217
-
Single versus parallel pathways of protein-folding and fractional formation of structure in the transition-state
-
Fersht AR, Itzhaki LS, Elmasry N, Matthews JM, Otzen DE: Single versus parallel pathways of protein-folding and fractional formation of structure in the transition-state. Proc Natl Acad Sci USA 1994, 91:10426-10429.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10426-10429
-
-
Fersht, A.R.1
Itzhaki, L.S.2
Elmasry, N.3
Matthews, J.M.4
Otzen, D.E.5
-
8
-
-
0028143603
-
Characterization of the transition state of protein unfolding by use of molecular dynamics: Chymotrypsin inhibitor 2
-
Li AJ, Daggett V: Characterization of the transition state of protein unfolding by use of molecular dynamics: chymotrypsin inhibitor 2. Proc Natl Acad Sci USA 1994, 91:10430-10434. Molecular dynamics simulations of Cl2 in water were performed at elevated temperatures to characterize the unfolding of this protein. An analogue of experimentally determined φ values was developed and corresponded well with the experimental findings. A structural model of the transition state of this protein is put forward.
-
(1994)
Proc Natl Acad Sci USA
, vol.91
, pp. 10430-10434
-
-
Li, A.J.1
Daggett, V.2
-
9
-
-
0028868995
-
The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: Evidence for a nucleation-condensation mechanism for protein folding
-
Itzhaki LS, Otzen DE, Fersht AR: The structure of the transition state for folding of chymotrypsin inhibitor 2 analysed by protein engineering methods: evidence for a nucleation-condensation mechanism for protein folding. J Mol Biol 1995, 254:260-288. This study extends earlier work on Cl2 and notably draws attention to a possible nucleation site predicted independently in lattice model simulations.
-
(1995)
J Mol Biol
, vol.254
, pp. 260-288
-
-
Itzhaki, L.S.1
Otzen, D.E.2
Fersht, A.R.3
-
10
-
-
0028905560
-
Evidence for a molten globule-like transition state in protein folding from determination of activation volumes
-
Vidugiris GJA, Markley JL, Royer CA: Evidence for a molten globule-like transition state in protein folding from determination of activation volumes. Biochemistry 1995, 34:4909-4912. The folding and unfolding kinetics of nuclease A have been measured after jumps in pressure. The relationship between kinetics and pressure permit the relative activation volumes of native, unfolded and transition states to be determined. The results are taken to indicate a transition state which is enlarged compared to the native state, is loosely packed and excludes solvent.
-
(1995)
Biochemistry
, vol.34
, pp. 4909-4912
-
-
Vidugiris, G.J.A.1
Markley, J.L.2
Royer, C.A.3
-
12
-
-
0028944346
-
Is burst Hydrophobic collapse necessary for protein folding?
-
Gutin AM, Abkevich VI, Shakhnovich El: Is burst Hydrophobic collapse necessary for protein folding? Biochemistry 1995, 34:3066-3076. Two sets of lattice-model simulations of protein folding were performed that differed in the magnitude of attraction between the residues. In the case of strong attraction between residues, formation of the native conformation is preceded by collapse. For weak attraction, two-state transitions dominate.
-
(1995)
Biochemistry
, vol.34
, pp. 3066-3076
-
-
Gutin, A.M.1
Abkevich, V.I.2
Shakhnovich, El.3
-
13
-
-
0012197202
-
Effect of amino acid changes at the helix-sheet interface of ubiquitin on the thermodynamics and kinetics of folding
-
Khorasanizadeh S, Peters ID, Roder H: Effect of amino acid changes at the helix-sheet interface of ubiquitin on the thermodynamics and kinetics of folding. Protein Eng 1995, 8(suppl):21. Meeting abstract describing the effects on refolding of ubiquitin that result from mutations to residue 26 in the core of this protein. Highly destabilizing cavity-forming mutants (Val→Ala, Val→Gly) are reported to change the refolding kinetics from three-state to two-state.
-
(1995)
Protein Eng
, vol.8
, Issue.SUPPL.
, pp. 21
-
-
Khorasanizadeh, S.1
Peters, I.D.2
Roder, H.3
-
14
-
-
0028426938
-
Kinetic partitioning during protein folding yields multiple native states
-
Sinclair JF, Ziegler MM, Baldwin TO: Kinetic partitioning during protein folding yields multiple native states. Nature Struct Biol 1994, 1:320-326.
-
(1994)
Nature Struct Biol
, vol.1
, pp. 320-326
-
-
Sinclair, J.F.1
Ziegler, M.M.2
Baldwin, T.O.3
-
15
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings PA, Wright PE: Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin. Science 1993, 262:892-896.
-
(1993)
Science
, vol.262
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
16
-
-
0027190613
-
Kinetics of folding of the all β-sheet protein interleukin-1-β
-
Varley P, Gronenborn AM, Christensen H, Wingfield PT, Pain RH, Clore GM: Kinetics of folding of the all β-sheet protein interleukin-1-β. Science 1993, 260:1110-1113.
-
(1993)
Science
, vol.260
, pp. 1110-1113
-
-
Varley, P.1
Gronenborn, A.M.2
Christensen, H.3
Wingfield, P.T.4
Pain, R.H.5
Clore, G.M.6
-
17
-
-
0027394285
-
Pulsed H/D-exchange studies of folding intermediates
-
Baldwin RL: Pulsed H/D-exchange studies of folding intermediates. Curr Opin Struct Biol 1993, 3:84-91.
-
(1993)
Curr Opin Struct Biol
, vol.3
, pp. 84-91
-
-
Baldwin, R.L.1
-
18
-
-
0029653893
-
Insights into protein folding using physical techniques: Studies of lysozyme and α-lactalbumin
-
Radford SE, Dobson CM: Insights into protein folding using physical techniques: studies of lysozyme and α-lactalbumin. Philos Trans R Soc Lond Biol 1995, 348:17-25. Review including a schematic folding pathway for hen lysozyme on the basis of data from a wide variety of experimental techniques.
-
(1995)
Philos Trans R Soc Lond Biol
, vol.348
, pp. 17-25
-
-
Radford, S.E.1
Dobson, C.M.2
-
19
-
-
0026605509
-
A protein folding reaction under kinetic control
-
Baker D, Sohl JL, Agard DA: A protein folding reaction under kinetic control. Nature 1992, 356:263-265.
-
(1992)
Nature
, vol.356
, pp. 263-265
-
-
Baker, D.1
Sohl, J.L.2
Agard, D.A.3
-
20
-
-
0029114534
-
One sequence, two folds: A metastable structure of CD2
-
Murray AJ, Lewis SJ, Barclay AN, Brady RL: One sequence, two folds: a metastable structure of CD2. Proc Natl Acad Sci USA 1995, 92:7337-7341. The N-terminal domain of the lymphocyte cell-adhesion molecule CD2 was expressed recombinantly as part of a glutathione S-transferase fusion protein. A dimeric form of CD2, found as 15% of the expressed protein, was isolated and crystallized. Investigation of the structure revealed a dimer whose domains strongly resemble the native protein, although each domain contains chains from both monomers.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 7337-7341
-
-
Murray, A.J.1
Lewis, S.J.2
Barclay, A.N.3
Brady, R.L.4
-
21
-
-
0028286471
-
Kinetics versus thermodynamics in protein folding
-
Baker D, Agard DA: Kinetics versus thermodynamics in protein folding. Biochemistry 1994, 33:7505-7509.
-
(1994)
Biochemistry
, vol.33
, pp. 7505-7509
-
-
Baker, D.1
Agard, D.A.2
-
22
-
-
0028402689
-
The barriers in protein folding
-
Sosnick TR, Mayne L, Hilter R, Englander SW: The barriers in protein folding. Nature Struct Biol 1994, 1:149-156.
-
(1994)
Nature Struct Biol
, vol.1
, pp. 149-156
-
-
Sosnick, T.R.1
Mayne, L.2
Hilter, R.3
Englander, S.W.4
-
23
-
-
0029117494
-
Finding the right fold
-
Dobson CM: Finding the right fold. Nature Struct Biol 1995, 2:513-517. An overview of the evidence for misfolded states of proteins and their role in protein folding.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 513-517
-
-
Dobson, C.M.1
-
24
-
-
0029027663
-
Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution
-
Fisher AJ, Raushel FM, Baldwin TO, Rayment I: Three-dimensional structure of bacterial luciferase from Vibrio harveyi at 2.4 Å resolution. Biochemistry 1995, 34:6581-6586. The crystal structure of this heterodimer reveals that each monomer donates two helices to the formation of a parallel four-helix bundle at the dimer interface. This explains, in part, the propensity of one of the subunits to form a homodimer.
-
(1995)
Biochemistry
, vol.34
, pp. 6581-6586
-
-
Fisher, A.J.1
Raushel, F.M.2
Baldwin, T.O.3
Rayment, I.4
-
25
-
-
0001756859
-
Is there a single pathway for the folding of a polypeptide chain
-
Harrison SC, Durbin R: Is there a single pathway for the folding of a polypeptide chain. Proc Natl Acad Sci USA 1985, 82:4028-4030.
-
(1985)
Proc Natl Acad Sci USA
, vol.82
, pp. 4028-4030
-
-
Harrison, S.C.1
Durbin, R.2
-
26
-
-
0027770910
-
Detection of transient protein folding populations by mass spectrometry
-
Miranker A, Robinson CV, Radford SE, Aplin RT, Dobson CM: Detection of transient protein folding populations by mass spectrometry. Science 1993, 262:896-900.
-
(1993)
Science
, vol.262
, pp. 896-900
-
-
Miranker, A.1
Robinson, C.V.2
Radford, S.E.3
Aplin, R.T.4
Dobson, C.M.5
-
27
-
-
0028936119
-
Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride
-
Kotik M, Radford SE, Dobson CM: Comparison of the refolding of hen lysozyme from dimethyl sulfoxide and guanidinium chloride. Biochemistry 1995, 34:1714-1724. NMR spectra of denatured stales of hen lysozyme in guanidine hydrochloride and dimethyl sulphoxide are shown to be significantly different. However, the refolding properties of the protein in these two denaturants as monitored by pulse-labelled hydrogen exchange are indistinguishable provided the refolding media is identical.
-
(1995)
Biochemistry
, vol.34
, pp. 1714-1724
-
-
Kotik, M.1
Radford, S.E.2
Dobson, C.M.3
-
28
-
-
0026781019
-
Early steps in cytochrome c folding probed by time resolved circular dichroism and fluorescence spectroscopy
-
Elöve GA, Chaffotte AF, Roder H, Goldberg ME: Early steps in cytochrome c folding probed by time resolved circular dichroism and fluorescence spectroscopy. Biochemistry 1992, 31:6876-6883.
-
(1992)
Biochemistry
, vol.31
, pp. 6876-6883
-
-
Elöve, G.A.1
Chaffotte, A.F.2
Roder, H.3
Goldberg, M.E.4
-
29
-
-
0029115374
-
Kinetics of interaction of partially folded proteins with a hydrophobic dye: Evidence that molten globule character is maximal in early folding intermediates
-
Engelhard M, Evans PA: Kinetics of interaction of partially folded proteins with a hydrophobic dye: evidence that molten globule character is maximal in early folding intermediates. Protein Sci 1995, 4:1553-1562. The dye ANS, commonly used as an indicator of the molten globule state, is shown to perturb the refolding kinetics of two proteins. This work dramatically illustrates the differences in the apparent development of molten-globular characteristics in carbonic anyhydrase and a-lactalbumin depending on whether the dye is a component of the refolding medium, or is pulsed into the refolding mixture at specified time points.
-
(1995)
Protein Sci
, vol.4
, pp. 1553-1562
-
-
Engelhard, M.1
Evans, P.A.2
-
30
-
-
0028227296
-
Tertiary interactions in the folding pathway of hen lysozyme: Kinetic studies using fluorescent probes
-
Itzhaki LS, Evans PA, Dobson CM, Radford SE: Tertiary interactions In the folding pathway of hen lysozyme: kinetic studies using fluorescent probes. Biochemistry 1994, 33:5212-5220.
-
(1994)
Biochemistry
, vol.33
, pp. 5212-5220
-
-
Itzhaki, L.S.1
Evans, P.A.2
Dobson, C.M.3
Radford, S.E.4
-
31
-
-
0028925815
-
Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy
-
Jones BE, Beechem JM, Matthews CR: Local and global dynamics during the folding of Escherichia coli dihydrofolate reductase by time-resolved fluorescence spectroscopy. Biochemistry 1995, 34:1867-1877. Time-resolved fluorescence spectroscopy is used to measure anisotropy and fluorescence lifetimes of tryptophan residues and the bound hydrophobic reporter group ANS during the refolding of DHFR. Results are interpreted in terms of both localized and global changes to the size and dynamics of the protein during refolding.
-
(1995)
Biochemistry
, vol.34
, pp. 1867-1877
-
-
Jones, B.E.1
Beechem, J.M.2
Matthews, C.R.3
-
32
-
-
0029032691
-
Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering
-
Kataoka M, Nishii I, Fujisawa T, Ueki T, Tokunaga F, Goto Y: Structural characterization of the molten globule and native states of apomyoglobin by solution X-ray scattering. J Mol Biol 1995, 249:215-228. A detail solution X-ray scattering study of holo and apo forms of myoglobin. A bimodal distance distribution is also reported for the trichloroacetate-stabilized molten globule state of the apo protein and is interpreted as reflecting loose structure about a stable core.
-
(1995)
J Mol Biol
, vol.249
, pp. 215-228
-
-
Kataoka, M.1
Nishii, I.2
Fujisawa, T.3
Ueki, T.4
Tokunaga, F.5
Goto, Y.6
-
33
-
-
0028884580
-
The radius of gyration of an apomyoglobin folding intermediate
-
Eliezer D, Jennings PA, Wright PE, Doniach S, Hodgson KO, Tsuruta H: The radius of gyration of an apomyoglobin folding intermediate. Science 1995, 270:487-488. The compactness of an early intermediate in the refolding of apomyoblogin is measured directly using time-resolved X-ray scattering and found to be similar to that of the native state.
-
(1995)
Science
, vol.270
, pp. 487-488
-
-
Eliezer, D.1
Jennings, P.A.2
Wright, P.E.3
Doniach, S.4
Hodgson, K.O.5
Tsuruta, H.6
-
34
-
-
0027489831
-
NMR and protein folding: Equilibrium and stopped flow studies
-
Frieden C, Hoeltzli SD, Ropson IJ: NMR and protein folding: equilibrium and stopped flow studies. Protein Sci 1993, 2:2007-2014.
-
(1993)
Protein Sci
, vol.2
, pp. 2007-2014
-
-
Frieden, C.1
Hoeltzli, S.D.2
Ropson, I.J.3
-
35
-
-
0029123975
-
Following protein folding in real time using NMR spectroscopy
-
Balbach J, Forge V, Van Nuland NAJ, Winder SL, Hore PJ, Dobson CM: Following protein folding in real time using NMR spectroscopy. Nature Struct Biol 1995, 2:865-870. The refolding of apo α-lactalbumin is monitored in real time by NMR. The spectrum of the burst-phase intermediate closely resembles the spectrum of the equilibrium molten globule of this protein. Furthermore, all time-resolved spectra can be reconstructed from linear combinations of native and burst-phase spectra, suggesting a cooperative transition from the burst state to the native state with no evidence for intermediates (e.g. domains) having fully native-like packing.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 865-870
-
-
Balbach, J.1
Forge, V.2
Van Nuland, N.A.J.3
Winder, S.L.4
Hore, P.J.5
Dobson, C.M.6
-
36
-
-
0029001090
-
Direct NMR evidence for an intermediate preceding the rate limiting step in the unfolding of ribonuclease A
-
Kiefhaber T, Labhardt AM, Baldwin RL: Direct NMR evidence for an intermediate preceding the rate limiting step in the unfolding of ribonuclease A. Nature 1995, 375:513-515. Using rapid-mix techniques coupled with NMR, it is reported that in the unfolding of ribonuclease A, chemical-shift dispersion is lost within the dead time of the experiment followed by attainment of the unfolded state on a timescale consistent with monophasic unfolding measured by CD. This is reported as consistent with the unfolding process, having an initial intermediate which excludes solvent and is largely native-like, but has expanded enough to allow the motions necessary to remove chemical-shift dispersion.
-
(1995)
Nature
, vol.375
, pp. 513-515
-
-
Kiefhaber, T.1
Labhardt, A.M.2
Baldwin, R.L.3
-
37
-
-
0030027339
-
Investigation of protein folding by mass spectrometry
-
in press
-
Miranker A, Robinson CV, Radford SE, Dobson CM: Investigation of protein folding by mass spectrometry. FASEB J 1996, in press. A review of the recent and rapid developments in mass spectrometry which are relevant to the study of protein folding.
-
(1996)
FASEB J
-
-
Miranker, A.1
Robinson, C.V.2
Radford, S.E.3
Dobson, C.M.4
-
38
-
-
0028028126
-
Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme
-
Eyles SJ, Radford SE, Robinson CV, Dobson CM: Kinetic consequences of the removal of a disulfide bridge on the folding of hen lysozyme. Biochemistry 1994, 33:13038-13048. Removal of the terminal 6-127 disulphide bond resulted in a protein with a similar refolding rate to the native protein. However, the compact intermediate attributed to the largely α-helical domain seen in the refolding of the native species was completely absent. This suggested that formation of stable β-sheet structure is rate limiting for this protein.
-
(1994)
Biochemistry
, vol.33
, pp. 13038-13048
-
-
Eyles, S.J.1
Radford, S.E.2
Robinson, C.V.3
Dobson, C.M.4
-
39
-
-
0028878753
-
Detection of synthetic protein isomers and conformers by electrospray mass spectrometry
-
Muir TW, Williams MJ, Kent SBH: Detection of synthetic protein isomers and conformers by electrospray mass spectrometry. Anal Biochem 1995, 224:100-109. In the total chemical synthesis of the tenth type III module from fibronectin, a distinction between folded and misfolded products is made from both the charge distribution and the hydrogen-exchange properties detected by mass analysis.
-
(1995)
Anal Biochem
, vol.224
, pp. 100-109
-
-
Muir, T.W.1
Williams, M.J.2
Kent, S.B.H.3
-
40
-
-
0029151862
-
Cooperative elements in protein folding monitored by electrospray ionization mass spectrometry
-
Hooke SD, Eyles SJ, Miranker A, Radford SE, Robinson CV, Dobson CM: Cooperative elements in protein folding monitored by electrospray ionization mass spectrometry. J Am Chem Soc 1995, 117:7548-7549. The ability of mass spectrometry to separate on the basis of mass is used to compare the relative refolding properties of closely related lysozymes to a high level of accuracy. This approach guarantees that experiment and analysis conditions are identical.
-
(1995)
J am Chem Soc
, vol.117
, pp. 7548-7549
-
-
Hooke, S.D.1
Eyles, S.J.2
Miranker, A.3
Radford, S.E.4
Robinson, C.V.5
Dobson, C.M.6
-
41
-
-
0028053187
-
Understanding how proteins fold: The lysozyme story so far
-
Dobson CM, Evans PA, Radford SE: Understanding how proteins fold: the lysozyme story so far. Trends Biochem Sci 1994, 19:31-37.
-
(1994)
Trends Biochem Sci
, vol.19
, pp. 31-37
-
-
Dobson, C.M.1
Evans, P.A.2
Radford, S.E.3
-
42
-
-
0027163998
-
Protein folding and stability: The pathway of folding of barnase
-
Fersht AR: Protein folding and stability: the pathway of folding of barnase. FEBS Lett 1993, 325:5-16.
-
(1993)
FEBS Lett
, vol.325
, pp. 5-16
-
-
Fersht, A.R.1
-
43
-
-
0029643523
-
Protein folding intermediates: Native state hydrogen exchange
-
Bai YW, Sosnick TR, Mayne L, Englander SW: Protein folding intermediates: native state hydrogen exchange. Science 1995, 269:192-197. The folding of cytochrome c is characterized at equilibrium under strongly native conditions. By measuring hydrogen exchange as a function of denaturant at low concentrations of the latter, multiple cooperative domains in the native protein were identified as folding domains.
-
(1995)
Science
, vol.269
, pp. 192-197
-
-
Bai, Y.W.1
Sosnick, T.R.2
Mayne, L.3
Englander, S.W.4
-
44
-
-
0028917296
-
Structures of folding intermediates
-
Ptitsyn OB: Structures of folding intermediates. Curr Opin Struct Biol 1995, 5:74-78. A review of the thermodynamic characterization of molten and pre-molten globule states and their role in folding.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 74-78
-
-
Ptitsyn, O.B.1
-
45
-
-
0028966372
-
Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor
-
Ferrer M, Barany G, Woodward C: Partially folded, molten globule and molten coil states of bovine pancreatic trypsin inhibitor. Nature Struct Biol 1995, 2:211-217. A one-disulphide and a no-disulphide analogue of BPTI are characterized. The one-disulphide intermediate is denatured at pH 2.5 and forms an acid state with molten globule characteristics at pH 1.5. The no-disulphide analogue has no significant secondary or tertiary structure as measured by CD, yet is able to bind ANS, suggesting the presence of hydrophobic surface.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 211-217
-
-
Ferrer, M.1
Barany, G.2
Woodward, C.3
-
46
-
-
0028367331
-
Structural characterization of a highly ordered molten globule at low pH
-
Redfield C, Smith RAG, Dobson CM: Structural characterization of a highly ordered molten globule at low pH. Nature Struct Biol 1994, 1:23-29.
-
(1994)
Nature Struct Biol
, vol.1
, pp. 23-29
-
-
Redfield, C.1
Smith, R.A.G.2
Dobson, C.M.3
-
47
-
-
0029011017
-
Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH
-
Chalikian TV, Gindikin VS, Breslauer KJ: Volumetric characterizations of the native, molten globule and unfolded states of cytochrome c at acidic pH. J Mol Biol 1995, 250:291-306. Volume and compressibility of native, unfolded and acid states of cytochrome care determined using ultrasonic and densimetric techniques. This approach has been used to study the size and dynamical properties of the solvent-excluded core in the acid state relative to the native and the unfolded state.
-
(1995)
J Mol Biol
, vol.250
, pp. 291-306
-
-
Chalikian, T.V.1
Gindikin, V.S.2
Breslauer, K.J.3
-
48
-
-
0028334906
-
A protein dissection study of a molten globule
-
Peng ZY, Kim PS: A protein dissection study of a molten globule. Biochemistry 1994, 33:2136-2141.
-
(1994)
Biochemistry
, vol.33
, pp. 2136-2141
-
-
Peng, Z.Y.1
Kim, P.S.2
-
49
-
-
0028952169
-
Bipartite structure of the α-lactalbumin molten globule
-
Wu LC, Peng ZY, Kim PS: Bipartite structure of the α-lactalbumin molten globule. Nature Struct Biol 1995, 2:281-286. Two site-directed mutants of α-lactalbumin are designed such that two of the four disulphides are retained in either one or the other of the two subdomains of this protein. Both mutants demonstrate molten-globule characteristics in common with the native protein under acid conditions. Disulphide rearrangement studies indicate native-like disulphide formation in only one of the subdomains.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 281-286
-
-
Wu, L.C.1
Peng, Z.Y.2
Kim, P.S.3
-
50
-
-
0027280472
-
Structure and stability of the molten globule state of guinea-pig α-lactalbumin: A hydrogen exchange study
-
Chyan CL, Wormald C, Dobson CM, Evans PA, Baum J: Structure and stability of the molten globule state of guinea-pig α-lactalbumin: a hydrogen exchange study. Biochemistry 1993, 32:5681-5691.
-
(1993)
Biochemistry
, vol.32
, pp. 5681-5691
-
-
Chyan, C.L.1
Wormald, C.2
Dobson, C.M.3
Evans, P.A.4
Baum, J.5
-
51
-
-
0029145759
-
Dynamic structure of a highly ordered β-sheet molten globule: Multiple conformations with a stable core
-
Barbar E, Barany G, Woodward C: Dynamic structure of a highly ordered β-sheet molten globule: multiple conformations with a stable core. Biochemistry 1995, 34:11423-11434. NMR analysis of the molten-globule state of a one-disulphide derivative of BPTI reveals two exchange peaks for many residues. Residues representing a two-stranded β sheet in the native protein do not give exchange peaks. This is taken as an indication of multiple conformations which share a common structural core.
-
(1995)
Biochemistry
, vol.34
, pp. 11423-11434
-
-
Barbar, E.1
Barany, G.2
Woodward, C.3
-
52
-
-
0028926855
-
A native tertiary interaction stabilizes the A state of cytochrome c
-
Marmorino JL, Pielak GJ: A native tertiary interaction stabilizes the A state of cytochrome c. Biochemistry 1995, 34:3140-3143. The thermodynamic properties of unfolding cytochrome c from its native state are compared to those of unfolding from its acid denatured state. Mutations directed at the N- and C-terminal helical interface yield similar perturbations to the two transitions. This is interpreted as showing that this helix-helix interaction equivalently stabilizes the native and acid states of this protein.
-
(1995)
Biochemistry
, vol.34
, pp. 3140-3143
-
-
Marmorino, J.L.1
Pielak, G.J.2
-
53
-
-
0029099221
-
Structural basis of the stability of a lysozyme molten globule
-
Morozova LA, Haynie DT, Arico-Muendel C, Dael HV, Dobson CM: Structural basis of the stability of a lysozyme molten globule. Nature Struct Biol 1995, 2:871-875. The pattern of hydrogen-exchange protection of the acid-induced molten globule of equine lysozyme is compared to that of the native protein. The correlation of the most highly protected residues of this molten globule with the compact core of the native protein is taken as an indication of significant native-like interactions within the hydrophobic core.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 871-875
-
-
Morozova, L.A.1
Haynie, D.T.2
Arico-Muendel, C.3
Dael, H.V.4
Dobson, C.M.5
-
54
-
-
0028917484
-
Nature of the early folding intermediate of ribonuclease A
-
Udgaonkar JB, Baldwin RL: Nature of the early folding intermediate of ribonuclease A. Biochemistry 1995, 34:4088-4096. Inhibitor binding and hydrogen-exchange protection are reported as consistent with the presence of well developed tertiary structure in an early intermediate of ribonuclease A.
-
(1995)
Biochemistry
, vol.34
, pp. 4088-4096
-
-
Udgaonkar, J.B.1
Baldwin, R.L.2
-
55
-
-
0027443871
-
Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones
-
Flynn GC, Beckers CJM, Baase WA, Dahlquist FW: Individual subunits of bacterial luciferase are molten globules and interact with molecular chaperones. Proc Natl Acad Sci USA 1993, 90:10826-10830.
-
(1993)
Proc Natl Acad Sci USA
, vol.90
, pp. 10826-10830
-
-
Flynn, G.C.1
Beckers, C.J.M.2
Baase, W.A.3
Dahlquist, F.W.4
-
56
-
-
0028929556
-
Principles of protein folding: A perspective from simple exact models
-
Dill KA, Bromberg S, Yue KZ, Fiebig KM, Yee DP, Thomas PD, Chan HS: Principles of protein folding: a perspective from simple exact models. Protein Sci 1995, 4:561-602. A review of results from lattice models of folding and their correlation with experimental data, particularly with respect to bipolar coding of the overall native architecture of proteins.
-
(1995)
Protein Sci
, vol.4
, pp. 561-602
-
-
Dill, K.A.1
Bromberg, S.2
Yue, K.Z.3
Fiebig, K.M.4
Yee, D.P.5
Thomas, P.D.6
Chan, H.S.7
-
57
-
-
23444436172
-
Protein design by binary patterning of polar and nonpolar amino acids
-
Kamtekar S, Schiffer JM, Xiong HY, Babik JM, Hecht MH: Protein design by binary patterning of polar and nonpolar amino acids. Science 1993, 262:1680-1685.
-
(1993)
Science
, vol.262
, pp. 1680-1685
-
-
Kamtekar, S.1
Schiffer, J.M.2
Xiong, H.Y.3
Babik, J.M.4
Hecht, M.H.5
-
58
-
-
0029653924
-
Protein folds: Towards understanding folding from inspection of native structures
-
Thornton JM, Jones DT, Macarthur MW, Orengo CM, Swindells MB: Protein folds: towards understanding folding from inspection of native structures. Philos Trans R Soc Lond Biol 1995, 348:71-79. A review of studies deriving secondary structure propensity information from coil regions of proteins with known three-dimensional structure. A parallel discussion of the current status of domain families is also presented.
-
(1995)
Philos Trans R Soc Lond Biol
, vol.348
, pp. 71-79
-
-
Thornton, J.M.1
Jones, D.T.2
Macarthur, M.W.3
Orengo, C.M.4
Swindells, M.B.5
-
59
-
-
0029064713
-
Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides
-
Xiong HY, Buckwalter BL, Shieh HM, Hecht MH: Periodicity of polar and nonpolar amino acids is the major determinant of secondary structure in self-assembling oligomeric peptides. Proc Natl Acad Sci USA 1995, 92:6349-6353. Two sets of synthetic peptides were synthesized containing residues whose intrinsic propensities are helix and non-helix forming. In each of these sets, the peptides could be subdivided into two groups containing either helix or sheet hydrophobic/hydrophilic periodicities. CD spectra of these peptides suggest that periodicity is a stronger determinant of secondary structure than is intrinsic propensity.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 6349-6353
-
-
Xiong, H.Y.1
Buckwalter, B.L.2
Shieh, H.M.3
Hecht, M.H.4
-
60
-
-
0029120253
-
Cooperatively folded proteins in random sequence libraries
-
Davidson AR, Lumb KJ, Sauer RT: Cooperatively folded proteins in random sequence libraries. Nature Struct Biol 1995, 2:856-863. Helix-containing proteins were recovered from a random library of 80-mer peptides. These polypeptides demonstrate native-like thermal and denaturant transitions, but lack significant hydrogen-exchange protection.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 856-863
-
-
Davidson, A.R.1
Lumb, K.J.2
Sauer, R.T.3
-
61
-
-
0026731991
-
Hydrogen exchange in native and denatured states of hen egg white lysozyme
-
Radford SE, Buck M, Topping KD, Dobson CM, Evans PA: Hydrogen exchange in native and denatured states of hen egg white lysozyme. Proteins 1992, 14:237-248.
-
(1992)
Proteins
, vol.14
, pp. 237-248
-
-
Radford, S.E.1
Buck, M.2
Topping, K.D.3
Dobson, C.M.4
Evans, P.A.5
-
62
-
-
0029154811
-
Native-like and structurally characterized designed α-helical bundles
-
Betz SF, Bryson JW, Degrado WF: Native-like and structurally characterized designed α-helical bundles. Curr Opin Struct Biol 1995, 5:457-463. A review discussing structural aspects of designed proteins which relate to both molten-globule and native states of real proteins.
-
(1995)
Curr Opin Struct Biol
, vol.5
, pp. 457-463
-
-
Betz, S.F.1
Bryson, J.W.2
Degrado, W.F.3
-
63
-
-
0029004982
-
A phage display system for studying the sequence determinants of protein folding
-
Gu HD, Yi QA, Bray ST, Riddle DS, Shiau AK, Baker D: A phage display system for studying the sequence determinants of protein folding. Protein Sci 1995, 4:1108-1117. Random mutagenesis techniques were applied to the IgG-binding domain of protein L, which was expressed as a component of filamentous phage coat proteins. Mutated protein L, which retained a native-like conformation, could be isolated on the basis of binding activity to IgG and then amplified using the simultaneously isolated virus.
-
(1995)
Protein Sci
, vol.4
, pp. 1108-1117
-
-
Gu, H.D.1
Yi, Q.A.2
Bray, S.T.3
Riddle, D.S.4
Shiau, A.K.5
Baker, D.6
-
64
-
-
0029090502
-
Ultrafast thermally induced unfolding of RNase A
-
Phillips CM, Mizutani Y, Hochstrasser RM: Ultrafast thermally induced unfolding of RNase A. Proc Natl Acad Sci USA 1995, 92:7292-7296. Unfolding kinetics of ribonuclease A were monitored after a laser-induced temperature jump using picosecond transient infrared spectroscopy. Although time-resolved spectra could be reconstructed using unfolded and native spectra, a lag phase of 1 ns was observed in the unfolding kinetics.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 7292-7296
-
-
Phillips, C.M.1
Mizutani, Y.2
Hochstrasser, R.M.3
-
65
-
-
0029564595
-
Are buried salt bridges important for protein stability and conformational specificity?
-
Waldburger CD, Schildbach JF, Sauer RT: Are buried salt bridges important for protein stability and conformational specificity? Nature Struct Biol 1995, 2:122-128. Using combinatorial mutagenesis, a buried salt bridge formed from two arginines and one glutamic acid was replaced with hydrophobic residues. In several cases, the stability of the protein is increased and, in one of these, the crystal structure shows that the wild-type fold is largely maintained.
-
(1995)
Nature Struct Biol
, vol.2
, pp. 122-128
-
-
Waldburger, C.D.1
Schildbach, J.F.2
Sauer, R.T.3
-
66
-
-
0028593509
-
Protein superfamilies and domain superfolds
-
Orengo CA, Jones DT, Thornton JM: Protein superfamilies and domain superfolds. Nature 1994, 372:631-634.
-
(1994)
Nature
, vol.372
, pp. 631-634
-
-
Orengo, C.A.1
Jones, D.T.2
Thornton, J.M.3
-
67
-
-
0028814936
-
Probing the molten globule state of α-lactalbumin by limited proteolysis
-
Polverino de Laureto P, De Filippis V, Di Bello M, Zambonin M, Fontana A: Probing the molten globule state of α-lactalbumin by limited proteolysis. Biochemistry 1995, 34:12596-12604. Native, acid and trifluoroethanol states of a-lactalbumin were treated with the relatively non-specific proteases thermolysin and pepsin. Although these non-native states have previously been shown to be dynamic and unstructured relative to the native protein, this work suggests that they retain considerable resistance to proteolysis.
-
(1995)
Biochemistry
, vol.34
, pp. 12596-12604
-
-
De Polverino Laureto, P.1
De Filippis, V.2
Di Bello, M.3
Zambonin, M.4
Fontana, A.5
-
68
-
-
0027756896
-
A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants
-
Harbury PB, Zhang T, Kim PS, Alber T: A switch between two-, three-, and four-stranded coiled coils in GCN4 leucine zipper mutants. Science 1993, 262:1401-1407.
-
(1993)
Science
, vol.262
, pp. 1401-1407
-
-
Harbury, P.B.1
Zhang, T.2
Kim, P.S.3
Alber, T.4
-
69
-
-
0000454088
-
Recurring structural motifs in proteins with different functions
-
Orengo CA, Flores TP, Jones DT, Taylor WR, Thornton JM: Recurring structural motifs in proteins with different functions. Curr Biol 1993, 3:131-139.
-
(1993)
Curr Biol
, vol.3
, pp. 131-139
-
-
Orengo, C.A.1
Flores, T.P.2
Jones, D.T.3
Taylor, W.R.4
Thornton, J.M.5
-
70
-
-
0028856292
-
Defective protein folding as a basis of human disease
-
Thomas PJ, Qu B-H, Pederson PL: Defective protein folding as a basis of human disease. Trends Biochem Sci 1995, 20:456-459. A review covering the relationship between protein folding and the occurrence of certain diseases.
-
(1995)
Trends Biochem Sci
, vol.20
, pp. 456-459
-
-
Thomas, P.J.1
Qu, B.-H.2
Pederson, P.L.3
-
71
-
-
0028963362
-
Toward an outline of the topography of a realistic protein folding funnel
-
Onuchic JN, Wolynes PG, Luthey-Schulten Z, Socci ND: Toward an outline of the topography of a realistic protein folding funnel. Proc Natl Acad Sci USA 1995, 92:3626-3630. Experimental data in conjuction with helix-coil transition theory are used to characterize the properties of a protein folding funnel. A law of corresponding slates permits comparisons to be made between experimental results and data obtained from simplified lattice models of protein folding.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 3626-3630
-
-
Onuchic, J.N.1
Wolynes, P.G.2
Luthey-Schulten, Z.3
Socci, N.D.4
-
72
-
-
0028247281
-
Side chain entropy and packing in proteins
-
Bromberg S, Dill KA: Side chain entropy and packing in proteins. Protein Sci 1994, 3:997-1009.
-
(1994)
Protein Sci
, vol.3
, pp. 997-1009
-
-
Bromberg, S.1
Dill, K.A.2
-
73
-
-
0029653906
-
Models of cooperativity in protein folding
-
Chan HS, Bromberg S, Dill KA: Models of cooperativity in protein folding. Philos Trans R Soc Lond Biol 1995, 348:61 -70. An overview of the cooperative basis of protein folding. Data derived from lattice models of proteins are discussed in the context of experimental observables.
-
(1995)
Philos Trans R Soc Lond Biol
, vol.348
, pp. 61-70
-
-
Chan, H.S.1
Bromberg, S.2
Dill, K.A.3
-
74
-
-
0028327236
-
Protein folding dynamics: The diffusion-collision model and experimental data
-
Karplus M, Weaver DL: Protein folding dynamics: the diffusion-collision model and experimental data. Protein Sci 1994, 3:650-668.
-
(1994)
Protein Sci
, vol.3
, pp. 650-668
-
-
Karplus, M.1
Weaver, D.L.2
-
75
-
-
0028124611
-
Does compactness induce secondary structure in proteins: A study of polyalanine chains computed by distance geometry
-
Yee DP, Chan HS, Havel TF, Dill KA: Does compactness induce secondary structure in proteins: a study of polyalanine chains computed by distance geometry. J Mol Biol 1994, 241:557-573.
-
(1994)
J Mol Biol
, vol.241
, pp. 557-573
-
-
Yee, D.P.1
Chan, H.S.2
Havel, T.F.3
Dill, K.A.4
-
77
-
-
0028957666
-
Evolution-like selection of fast folding model proteins
-
Gutin AM, Abkevich VI, Shakhnovich El: Evolution-like selection of fast folding model proteins. Proc Natl Acad Sci USA 1995, 92:1282-1286. The sequence of a lattice model protein is optimized for fast folding. The results are sequences which not only fold 100 times faster than random sequences but also have native-state stabilities significantly higher than the starting random sequences.
-
(1995)
Proc Natl Acad Sci USA
, vol.92
, pp. 1282-1286
-
-
Gutin, A.M.1
Abkevich, V.I.2
Shakhnovich, El.3
-
78
-
-
0028024928
-
Specific nucleus as the transition state for protein folding: Evidence from the lattice model
-
Abkevich VI, Gutin AM, Shakhnovich El: Specific nucleus as the transition state for protein folding: evidence from the lattice model. Biochemistry 1994, 33:10026-10036.
-
(1994)
Biochemistry
, vol.33
, pp. 10026-10036
-
-
Abkevich, V.I.1
Gutin, A.M.2
Shakhnovich, El.3
-
79
-
-
0029000377
-
Domains in folding of model proteins
-
Abkevich VI, Gutin AM, Shakhnovich El: Domains in folding of model proteins. Protein Sci 1995, 4:1167-1177. The refolding of self-avoiding chains on a lattice were examined as a function of chain length. Two-state refolding was shown by 36-mer chains, whereas nine out of twelve 48-mer sequences showed three-state refolding attributed to subdomains of the native-state model.
-
(1995)
Protein Sci
, vol.4
, pp. 1167-1177
-
-
Abkevich, V.I.1
Gutin, A.M.2
Shakhnovich, El.3
-
80
-
-
0028835443
-
Nucleation mechanism for protein folding and theoretical predictions for hydrogen exchange labeling experiments
-
Thirumalai D, Guo ZY: Nucleation mechanism for protein folding and theoretical predictions for hydrogen exchange labeling experiments. Biopolymers 1995, 35:137-140. Model simulations of the refolding of 46 beads on a string yield parallel path-ways in which a proportion of the molecules fold via a nucleation mechanism to the native state, whereas the remainder fold via a collapsed intermediate.
-
(1995)
Biopolymers
, vol.35
, pp. 137-140
-
-
Thirumalai, D.1
Guo, Z.Y.2
|