-
1
-
-
0034737327
-
Two-state expansion and collapse of a polypeptide
-
Hagen S.J., Eaton W.A. Two-state expansion and collapse of a polypeptide. J. Mol. Biol. 297:2000;781-789.
-
(2000)
J. Mol. Biol.
, vol.297
, pp. 781-789
-
-
Hagen, S.J.1
Eaton, W.A.2
-
2
-
-
0028802181
-
Initial hydrophobic collapse in the folding of barstar
-
Agashe V.R., Shastry M.C., Udgaonkar J.B. Initial hydrophobic collapse in the folding of barstar. Nature. 377:1995;754-757.
-
(1995)
Nature
, vol.377
, pp. 754-757
-
-
Agashe, V.R.1
Shastry, M.C.2
Udgaonkar, J.B.3
-
3
-
-
0029973119
-
Direct observation of fast protein folding: The initial collapse of apomyoglobin
-
Ballew R.M., Sabelko J., Gruebele M. Direct observation of fast protein folding: the initial collapse of apomyoglobin. Proc. Natl Acad. Sci. USA. 93:1996;5759-5764.
-
(1996)
Proc. Natl Acad. Sci. USA
, vol.93
, pp. 5759-5764
-
-
Ballew, R.M.1
Sabelko, J.2
Gruebele, M.3
-
4
-
-
0035926229
-
Time resolved collapse of a folding protein observed with small angle X-ray scattering
-
Pollack L., Tate M., Finnefrock A., Kalidas C., Trotter S., Darnton N., et al. Time resolved collapse of a folding protein observed with small angle X-ray scattering. Phys. Rev. Letters. 86:2001;4962-4965.
-
(2001)
Phys. Rev. Letters
, vol.86
, pp. 4962-4965
-
-
Pollack, L.1
Tate, M.2
Finnefrock, A.3
Kalidas, C.4
Trotter, S.5
Darnton, N.6
-
5
-
-
0032512697
-
Kinetics of lysozyme refolding: Structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering
-
Chen L., Wildegger G., Kiefhaber T., Hodgson K.O., Doniach S. Kinetics of lysozyme refolding: structural characterization of a non-specifically collapsed state using time-resolved X-ray scattering. J. Mol. Biol. 276:1998;225-237.
-
(1998)
J. Mol. Biol.
, vol.276
, pp. 225-237
-
-
Chen, L.1
Wildegger, G.2
Kiefhaber, T.3
Hodgson, K.O.4
Doniach, S.5
-
6
-
-
0030871209
-
Acquisition of native beta-strand topology during the rapid collapse phase of protein folding
-
Parker M.J., Dempsey C.E., Lorch M., Clarke A.R. Acquisition of native beta-strand topology during the rapid collapse phase of protein folding. Biochemistry. 36:1997;13396-13405.
-
(1997)
Biochemistry
, vol.36
, pp. 13396-13405
-
-
Parker, M.J.1
Dempsey, C.E.2
Lorch, M.3
Clarke, A.R.4
-
7
-
-
0030740123
-
Folding of tryptophan mutants of barstar: Evidence for an initial hydrophobic collapse on the folding pathway
-
Nath U., Udgaonkar J.B. Folding of tryptophan mutants of barstar: evidence for an initial hydrophobic collapse on the folding pathway. Biochemistry. 36:1997;8602-8610.
-
(1997)
Biochemistry
, vol.36
, pp. 8602-8610
-
-
Nath, U.1
Udgaonkar, J.B.2
-
8
-
-
0037022327
-
Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle X-ray scattering
-
Akiyama S., Takahashi S., Kimura T., Ishimori K., Morishima I., Nishikawa Y., Fujisawa T. Conformational landscape of cytochrome c folding studied by microsecond-resolved small-angle X-ray scattering. Proc. Natl Acad. Sci. USA. 99:2002;1329-1334.
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 1329-1334
-
-
Akiyama, S.1
Takahashi, S.2
Kimura, T.3
Ishimori, K.4
Morishima, I.5
Nishikawa, Y.6
Fujisawa, T.7
-
9
-
-
0041321045
-
Single-molecule measurement of protein folding kinetics
-
Lipman E.A., Schuler B., Bakajin O., Eaton W.A. Single-molecule measurement of protein folding kinetics. Science. 301:2003;1233-1235.
-
(2003)
Science
, vol.301
, pp. 1233-1235
-
-
Lipman, E.A.1
Schuler, B.2
Bakajin, O.3
Eaton, W.A.4
-
10
-
-
0033576317
-
Transient dimer in the refolding kinetics of cytochrome c characterized by small-angle X-ray scattering
-
Segel D.J., Eliezer D., Uversky V., Fink A.L., Hodgson K.O., Doniach S. Transient dimer in the refolding kinetics of cytochrome c characterized by small-angle X-ray scattering. Biochemistry. 38:1999;15352-15359.
-
(1999)
Biochemistry
, vol.38
, pp. 15352-15359
-
-
Segel, D.J.1
Eliezer, D.2
Uversky, V.3
Fink, A.L.4
Hodgson, K.O.5
Doniach, S.6
-
11
-
-
0033532201
-
Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering
-
Segel D.J., Bachmann A., Hofrichter J., Hodgson K.O., Doniach S., Kiefhaber T. Characterization of transient intermediates in lysozyme folding with time-resolved small-angle X-ray scattering. J. Mol. Biol. 288:1999;489-499.
-
(1999)
J. Mol. Biol.
, vol.288
, pp. 489-499
-
-
Segel, D.J.1
Bachmann, A.2
Hofrichter, J.3
Hodgson, K.O.4
Doniach, S.5
Kiefhaber, T.6
-
12
-
-
0027301270
-
Evidence of an associative intermediate on the myoglobin refolding pathway
-
Eliezer D., Chiba K., Tsuruta H., Doniach S., Hodgson K.O., Kihara H. Evidence of an associative intermediate on the myoglobin refolding pathway. Biophys. J. 65:1993;912-917.
-
(1993)
Biophys. J.
, vol.65
, pp. 912-917
-
-
Eliezer, D.1
Chiba, K.2
Tsuruta, H.3
Doniach, S.4
Hodgson, K.O.5
Kihara, H.6
-
13
-
-
0029562577
-
Partially folded states of proteins: Characterization by X-ray scattering
-
Doniach S., Bascle J., Garel T., Orland H. Partially folded states of proteins: characterization by X-ray scattering. J. Mol. Biol. 254:1995;960-967.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 960-967
-
-
Doniach, S.1
Bascle, J.2
Garel, T.3
Orland, H.4
-
14
-
-
0030572626
-
A lysozyme folding intermediate revealed by solution X-ray scattering
-
Chen L., Hodgson K.O., Doniach S. A lysozyme folding intermediate revealed by solution X-ray scattering. J. Mol. Biol. 261:1996;658-671.
-
(1996)
J. Mol. Biol.
, vol.261
, pp. 658-671
-
-
Chen, L.1
Hodgson, K.O.2
Doniach, S.3
-
15
-
-
0032995379
-
Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering
-
Arai S., Hirai M. Reversibility and hierarchy of thermal transition of hen egg-white lysozyme studied by small-angle X-ray scattering. Biophys. J. 76:1999;2192-2197.
-
(1999)
Biophys. J.
, vol.76
, pp. 2192-2197
-
-
Arai, S.1
Hirai, M.2
-
16
-
-
0036349865
-
Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering
-
Arai M., Ito K., Inobe T., Nakao M., Maki K., Kamagata K., et al. Fast compaction of alpha-lactalbumin during folding studied by stopped-flow X-ray scattering. J. Mol. Biol. 321:2002;121-132.
-
(2002)
J. Mol. Biol.
, vol.321
, pp. 121-132
-
-
Arai, M.1
Ito, K.2
Inobe, T.3
Nakao, M.4
Maki, K.5
Kamagata, K.6
-
17
-
-
0036300690
-
Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques
-
Choy W.Y., Mulder F.A., Crowhurst K.A., Muhandiram D.R., Millett I.S., Doniach S., et al. Distribution of molecular size within an unfolded state ensemble using small-angle X-ray scattering and pulse field gradient NMR techniques. J. Mol. Biol. 316:2002;101-112.
-
(2002)
J. Mol. Biol.
, vol.316
, pp. 101-112
-
-
Choy, W.Y.1
Mulder, F.A.2
Crowhurst, K.A.3
Muhandiram, D.R.4
Millett, I.S.5
Doniach, S.6
-
19
-
-
0037126290
-
Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy
-
Schuler B., Lipman E.A., Eaton W.A. Probing the free-energy surface for protein folding with single-molecule fluorescence spectroscopy. Nature. 419:2002;743-747.
-
(2002)
Nature
, vol.419
, pp. 743-747
-
-
Schuler, B.1
Lipman, E.A.2
Eaton, W.A.3
-
20
-
-
0347284262
-
Rapid collapse precedes the fast two-state folding of the cold shock protein
-
Magg C., Schmid F.X. Rapid collapse precedes the fast two-state folding of the cold shock protein. J. Mol. Biol. 335:2004;1309-1323.
-
(2004)
J. Mol. Biol.
, vol.335
, pp. 1309-1323
-
-
Magg, C.1
Schmid, F.X.2
-
21
-
-
0041735179
-
Kinetics of intramolecular contact formation in a denatured protein
-
Buscaglia M., Schuler B., Lapidus L.J., Eaton W.A., Hofrichter J. Kinetics of intramolecular contact formation in a denatured protein. J. Mol. Biol. 332:2003;9-12.
-
(2003)
J. Mol. Biol.
, vol.332
, pp. 9-12
-
-
Buscaglia, M.1
Schuler, B.2
Lapidus, L.J.3
Eaton, W.A.4
Hofrichter, J.5
-
22
-
-
0036394906
-
Native-like mean structure in the unfolded ensemble of small proteins
-
Zagrovic B., Snow C.D., Khaliq S., Shirts M.R., Pande V.S. Native-like mean structure in the unfolded ensemble of small proteins. J. Mol. Biol. 323:2002;153-164.
-
(2002)
J. Mol. Biol.
, vol.323
, pp. 153-164
-
-
Zagrovic, B.1
Snow, C.D.2
Khaliq, S.3
Shirts, M.R.4
Pande, V.S.5
-
23
-
-
0037143694
-
The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation
-
Shimada J., Shakhnovich E.I. The ensemble folding kinetics of protein G from an all-atom Monte Carlo simulation. Proc. Natl Acad. Sci. USA. 99:2002;11175-11180.
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 11175-11180
-
-
Shimada, J.1
Shakhnovich, E.I.2
-
24
-
-
0032561237
-
Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution
-
Duan Y., Kollman P.A. Pathways to a protein folding intermediate observed in a 1-microsecond simulation in aqueous solution. Science. 282:1998;740-744.
-
(1998)
Science
, vol.282
, pp. 740-744
-
-
Duan, Y.1
Kollman, P.A.2
-
25
-
-
0036892356
-
All-atom fast protein folding simulations: The villin headpiece
-
Shen M.Y., Freed K.F. All-atom fast protein folding simulations: the villin headpiece. Proteins: Struct. Funct. Genet. 49:2002;439-445.
-
(2002)
Proteins: Struct. Funct. Genet.
, vol.49
, pp. 439-445
-
-
Shen, M.Y.1
Freed, K.F.2
-
26
-
-
0031965674
-
Molecular dynamics simulations of hydrophobic collapse of ubiquitin
-
Alonso D.O.V., Daggett V. Molecular dynamics simulations of hydrophobic collapse of ubiquitin. Protein Sci. 7:1998;860-874.
-
(1998)
Protein Sci.
, vol.7
, pp. 860-874
-
-
Alonso, D.O.V.1
Daggett, V.2
-
27
-
-
0036087885
-
The dual role of a loop with low loop contact distance in folding and domain swapping
-
Linhananta A., Zhou H.Y., Zhou Y.Q. The dual role of a loop with low loop contact distance in folding and domain swapping. Protein Sci. 11:2002;1695-1701.
-
(2002)
Protein Sci.
, vol.11
, pp. 1695-1701
-
-
Linhananta, A.1
Zhou, H.Y.2
Zhou, Y.Q.3
-
28
-
-
0037456298
-
The complete folding pathway of a protein from nanoseconds to microseconds
-
Mayor U., Guydosh N.R., Johnson C.M., Grossmann J.G., Sato S., Jas G.S., et al. The complete folding pathway of a protein from nanoseconds to microseconds. Nature. 421:2003;863-867.
-
(2003)
Nature
, vol.421
, pp. 863-867
-
-
Mayor, U.1
Guydosh, N.R.2
Johnson, C.M.3
Grossmann, J.G.4
Sato, S.5
Jas, G.S.6
-
29
-
-
0034691198
-
Measuring the rate of intramolecular contact formation in polypeptides
-
Lapidus L.J., Eaton W.A., Hofrichter J. Measuring the rate of intramolecular contact formation in polypeptides. Proc. Natl Acad. Sci. USA. 97:2000;7220-7225.
-
(2000)
Proc. Natl Acad. Sci. USA
, vol.97
, pp. 7220-7225
-
-
Lapidus, L.J.1
Eaton, W.A.2
Hofrichter, J.3
-
30
-
-
0043237588
-
Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding
-
Krieger F., Fierz B., Bieri O., Drewello M., Kiefhaber T. Dynamics of unfolded polypeptide chains as model for the earliest steps in protein folding. J. Mol. Biol. 332:2003;265-274.
-
(2003)
J. Mol. Biol.
, vol.332
, pp. 265-274
-
-
Krieger, F.1
Fierz, B.2
Bieri, O.3
Drewello, M.4
Kiefhaber, T.5
-
31
-
-
0037388138
-
Bioinorganic Chemistry Special Feature: The protein-folding speed limit: Intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c
-
Chang I.J., Lee J.C., Winkler J.R., Gray H.B. Bioinorganic Chemistry Special Feature: the protein-folding speed limit: intrachain diffusion times set by electron-transfer rates in denatured Ru(NH3)5(His-33)-Zn-cytochrome c. Proc. Natl Acad. Sci. USA. 100:2003;3838-3840.
-
(2003)
Proc. Natl Acad. Sci. USA
, vol.100
, pp. 3838-3840
-
-
Chang, I.J.1
Lee, J.C.2
Winkler, J.R.3
Gray, H.B.4
-
32
-
-
0037667601
-
Fast chain contraction during protein folding: "foldability" and collapse dynamics
-
Qiu L., Zachariah C., Hagen S.J. Fast chain contraction during protein folding: "foldability" and collapse dynamics. Phys. Rev. Letters. 90:2003;168103.
-
(2003)
Phys. Rev. Letters
, vol.90
, pp. 168103
-
-
Qiu, L.1
Zachariah, C.2
Hagen, S.J.3
-
34
-
-
0031815749
-
How do small single-domain proteins fold?
-
Jackson S.E. How do small single-domain proteins fold? Fold. Des. 3:1998;R81-R91.
-
(1998)
Fold. Des.
, vol.3
-
-
Jackson, S.E.1
-
35
-
-
0036440985
-
Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding
-
Krantz B.A., Mayne L., Rumbley J., Englander S.W., Sosnick T.R. Fast and slow intermediate accumulation and the initial barrier mechanism in protein folding. J. Mol. Biol. 324:2002;359-371.
-
(2002)
J. Mol. Biol.
, vol.324
, pp. 359-371
-
-
Krantz, B.A.1
Mayne, L.2
Rumbley, J.3
Englander, S.W.4
Sosnick, T.R.5
-
36
-
-
0026345750
-
Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition
-
Jackson S.E., Fersht A.R. Folding of chymotrypsin inhibitor 2.1. Evidence for a two-state transition. Biochemistry. 30:1991;10428-10435.
-
(1991)
Biochemistry
, vol.30
, pp. 10428-10435
-
-
Jackson, S.E.1
Fersht, A.R.2
-
37
-
-
0026781019
-
Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy
-
Elöve G.A., Chaffotte A.F., Roder H., Goldberg M.E. Early steps in cytochrome c folding probed by time-resolved circular dichroism and fluorescence spectroscopy. Biochemistry. 31:1992;6876-6883.
-
(1992)
Biochemistry
, vol.31
, pp. 6876-6883
-
-
Elöve, G.A.1
Chaffotte, A.F.2
Roder, H.3
Goldberg, M.E.4
-
38
-
-
0031055942
-
Kinetic role of early intermediates in protein folding
-
Roder H., Colon W. Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7:1997;15-28.
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 15-28
-
-
Roder, H.1
Colon, W.2
-
39
-
-
0031919973
-
Evidence for barrier-limited protein folding kinetics on the microsecond time scale
-
Shastry M.C., Roder H. Evidence for barrier-limited protein folding kinetics on the microsecond time scale. Nature Struct. Biol. 5:1998;385-392.
-
(1998)
Nature Struct. Biol.
, vol.5
, pp. 385-392
-
-
Shastry, M.C.1
Roder, H.2
-
40
-
-
0031047914
-
Submillisecond protein folding kinetics studied by ultrarapid mixing
-
Chan C.K., Hu Y., Takahashi S., Rousseau D.L., Eaton W.A., Hofrichter J. Submillisecond protein folding kinetics studied by ultrarapid mixing. Proc. Natl Acad. Sci. USA. 94:1997;1779-1784.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 1779-1784
-
-
Chan, C.K.1
Hu, Y.2
Takahashi, S.3
Rousseau, D.L.4
Eaton, W.A.5
Hofrichter, J.6
-
41
-
-
0030900533
-
Kinetics of folding of the IgG binding domain of peptostreptococcal protein L
-
Scalley M.L., Yi Q., Gu H., McCormack A., Yates J.R. 3rd, Baker D. Kinetics of folding of the IgG binding domain of peptostreptococcal protein L. Biochemistry. 36:1997;3373-3382.
-
(1997)
Biochemistry
, vol.36
, pp. 3373-3382
-
-
Scalley, M.L.1
Yi, Q.2
Gu, H.3
McCormack, A.4
Yates III, J.R.5
Baker, D.6
-
42
-
-
0034712675
-
PH jump studies of the folding of the multidomain ribosomal protein L9: The structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain
-
Sato S., Luisi D.L., Raleigh D.P. pH jump studies of the folding of the multidomain ribosomal protein L9: the structural organization of the N-terminal domain does not affect the anomalously slow folding of the C-terminal domain. Biochemistry. 39:2000;4955-4962.
-
(2000)
Biochemistry
, vol.39
, pp. 4955-4962
-
-
Sato, S.1
Luisi, D.L.2
Raleigh, D.P.3
-
43
-
-
0037137630
-
Formation of a compact structured ensemble without fluorescence signature early during ubiquitin folding
-
Qin Z., Ervin J., Larios E., Gruebele M., Kihara H. Formation of a compact structured ensemble without fluorescence signature early during ubiquitin folding. J. Phys. Chem. B. 106:2002;13040-13046.
-
(2002)
J. Phys. Chem. B
, vol.106
, pp. 13040-13046
-
-
Qin, Z.1
Ervin, J.2
Larios, E.3
Gruebele, M.4
Kihara, H.5
-
44
-
-
0031697733
-
The burst phase in ribonuclease a folding and solvent dependence of the unfolded state
-
Qi P.X., Sosnick T.R., Englander S.W. The burst phase in ribonuclease A folding and solvent dependence of the unfolded state. Nature Struct. Biol. 5:1998;882-884.
-
(1998)
Nature Struct. Biol.
, vol.5
, pp. 882-884
-
-
Qi, P.X.1
Sosnick, T.R.2
Englander, S.W.3
-
45
-
-
0029940033
-
Molecular collapse: The rate-limiting step in two-state cytochrome c folding
-
Sosnick T.R., Mayne L., Englander S.W. Molecular collapse: the rate-limiting step in two-state cytochrome c folding. Proteins: Struct. Funct. Genet. 24:1996;413-426.
-
(1996)
Proteins: Struct. Funct. Genet.
, vol.24
, pp. 413-426
-
-
Sosnick, T.R.1
Mayne, L.2
Englander, S.W.3
-
47
-
-
0242571958
-
Small-angle scattering studies of biological macromolecules in solution
-
Svergun D.I., Koch M.H.J. Small-angle scattering studies of biological macromolecules in solution. Rep. Prog. Phys. 66:2003;1735-1782.
-
(2003)
Rep. Prog. Phys.
, vol.66
, pp. 1735-1782
-
-
Svergun, D.I.1
Koch, M.H.J.2
-
48
-
-
0036401140
-
Toward a taxonomy of the denatured state: Small angle scattering studies of unfolded proteins
-
Millet I.S., Doniach S., Plaxco K.W. Toward a taxonomy of the denatured state: small angle scattering studies of unfolded proteins. Advan. Protein Chem. 62:2002;241-262.
-
(2002)
Advan. Protein Chem.
, vol.62
, pp. 241-262
-
-
Millet, I.S.1
Doniach, S.2
Plaxco, K.W.3
-
49
-
-
0037039440
-
Equilibrium collapse and the kinetic "foldability" of proteins
-
Millet I.S., Townsley L.E., Chiti F., Doniach S., Plaxco K.W. Equilibrium collapse and the kinetic "foldability" of proteins. Biochemistry. 41:2002;321-325.
-
(2002)
Biochemistry
, vol.41
, pp. 321-325
-
-
Millet, I.S.1
Townsley, L.E.2
Chiti, F.3
Doniach, S.4
Plaxco, K.W.5
-
50
-
-
0026733250
-
Denatured states of ribonuclease a have compact dimensions and residual secondary structure
-
Sosnick T.R., Trewhella J. Denatured states of ribonuclease A have compact dimensions and residual secondary structure. Biochemistry. 31:1992;8329-8335.
-
(1992)
Biochemistry
, vol.31
, pp. 8329-8335
-
-
Sosnick, T.R.1
Trewhella, J.2
-
52
-
-
0033621117
-
Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle X-ray scattering
-
Pollack L., Tate M.W., Darnton N.C., Knight J.B., Gruner S.M., Eaton W.A., Austin R.H. Compactness of the denatured state of a fast-folding protein measured by submillisecond small-angle X-ray scattering. Proc. Natl Acad. Sci. USA. 96:1999;10115-10117.
-
(1999)
Proc. Natl Acad. Sci. USA
, vol.96
, pp. 10115-10117
-
-
Pollack, L.1
Tate, M.W.2
Darnton, N.C.3
Knight, J.B.4
Gruner, S.M.5
Eaton, W.A.6
Austin, R.H.7
-
53
-
-
0030569018
-
Protein globularization during folding. A study by synchrotron small-angle X-ray scattering
-
Semisotnov G.V., Kihara H., Kotova N.V., Kimura K., Amemiya Y., Wakabayashi K., et al. Protein globularization during folding. A study by synchrotron small-angle X-ray scattering. J. Mol. Biol. 262:1996;559-574.
-
(1996)
J. Mol. Biol.
, vol.262
, pp. 559-574
-
-
Semisotnov, G.V.1
Kihara, H.2
Kotova, N.V.3
Kimura, K.4
Amemiya, Y.5
Wakabayashi, K.6
-
54
-
-
0032978994
-
Chain collapse can occur concomitantly with the rate-limiting step in protein folding
-
Plaxco K.W., Millett I.S., Segel D.J., Doniach S., Baker D. Chain collapse can occur concomitantly with the rate-limiting step in protein folding. Nature Struct. Biol. 6:1999;554-556.
-
(1999)
Nature Struct. Biol.
, vol.6
, pp. 554-556
-
-
Plaxco, K.W.1
Millett, I.S.2
Segel, D.J.3
Doniach, S.4
Baker, D.5
-
55
-
-
0034718524
-
Distinguishing between two-state and three-state models for ubiquitin folding
-
Krantz B.A., Sosnick T.R. Distinguishing between two-state and three-state models for ubiquitin folding. Biochemistry. 39:2000;11696-11701.
-
(2000)
Biochemistry
, vol.39
, pp. 11696-11701
-
-
Krantz, B.A.1
Sosnick, T.R.2
-
56
-
-
0033573838
-
Thermodynamics and kinetics of folding of common-type acylphosphatase: Comparison to the highly homologous muscle isoenzyme
-
Taddei N., Chiti F., Paoli P., Fiaschi T., Bucciantini M., Stefani M., et al. Thermodynamics and kinetics of folding of common-type acylphosphatase: comparison to the highly homologous muscle isoenzyme. Biochemistry. 38:1999;2135-2142.
-
(1999)
Biochemistry
, vol.38
, pp. 2135-2142
-
-
Taddei, N.1
Chiti, F.2
Paoli, P.3
Fiaschi, T.4
Bucciantini, M.5
Stefani, M.6
-
57
-
-
0036260620
-
Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects
-
Krantz B.A., Srivastava A.K., Nauli S., Baker D., Sauer R.T., Sosnick T.R. Understanding protein hydrogen bond formation with kinetic H/D amide isotope effects. Nature Struct. Biol. 9:2002;458-463.
-
(2002)
Nature Struct. Biol.
, vol.9
, pp. 458-463
-
-
Krantz, B.A.1
Srivastava, A.K.2
Nauli, S.3
Baker, D.4
Sauer, R.T.5
Sosnick, T.R.6
-
58
-
-
0023234618
-
Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin
-
Vijay-Kumar S., Bugg C.E., Wilkinson K.D., Vierstra R.D., Hatfield P.M., Cook W.J. Comparison of the three-dimensional structures of human, yeast, and oat ubiquitin. J. Biol. Chem. 262:1987;6396-6399.
-
(1987)
J. Biol. Chem.
, vol.262
, pp. 6396-6399
-
-
Vijay-Kumar, S.1
Bugg, C.E.2
Wilkinson, K.D.3
Vierstra, R.D.4
Hatfield, P.M.5
Cook, W.J.6
-
59
-
-
0031568309
-
Crystal structure of common type acylphosphatase from bovine testis
-
Thunnissen M.M., Taddei N., Liguri G., Ramponi G., Nordlund P. Crystal structure of common type acylphosphatase from bovine testis. Structure. 5:1997;69-79.
-
(1997)
Structure
, vol.5
, pp. 69-79
-
-
Thunnissen, M.M.1
Taddei, N.2
Liguri, G.3
Ramponi, G.4
Nordlund, P.5
-
60
-
-
0032478214
-
Protein hydration in solution: Experimental observation by X-ray and neutron scattering
-
Svergun D.I., Richard S., Koch M.H., Sayers Z., Kuprin S., Zaccai G. Protein hydration in solution: experimental observation by X-ray and neutron scattering. Proc. Natl Acad. Sci. USA. 95:1998;2267-2272.
-
(1998)
Proc. Natl Acad. Sci. USA
, vol.95
, pp. 2267-2272
-
-
Svergun, D.I.1
Richard, S.2
Koch, M.H.3
Sayers, Z.4
Kuprin, S.5
Zaccai, G.6
-
61
-
-
0037117502
-
Is the first hydration shell of lysozyme of higher density than bulk water?
-
Merzel F., Smith J.C. Is the first hydration shell of lysozyme of higher density than bulk water? Proc. Natl Acad. Sci. USA. 99:2002;5378-5383.
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 5378-5383
-
-
Merzel, F.1
Smith, J.C.2
-
62
-
-
0030057477
-
Evidence for a 3-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
-
Khorasanizadeh S., Peters I.D., Roder H. Evidence for a 3-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3:1996;193-205.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 193-205
-
-
Khorasanizadeh, S.1
Peters, I.D.2
Roder, H.3
-
63
-
-
0027305989
-
Folding and stability of a tryptophan-containing mutant of ubiquitin
-
Khorasanizadeh S., Peters I.D., Butt T.R., Roder H. Folding and stability of a tryptophan-containing mutant of ubiquitin. Biochemistry. 32:1993;7054-7063.
-
(1993)
Biochemistry
, vol.32
, pp. 7054-7063
-
-
Khorasanizadeh, S.1
Peters, I.D.2
Butt, T.R.3
Roder, H.4
-
64
-
-
0030322627
-
Structure of very early protein folding intermediates: New insights through a variant of hydrogen exchange labelling
-
Gladwin S.T., Evans P.A. Structure of very early protein folding intermediates: new insights through a variant of hydrogen exchange labelling. Fold. Des. 1:1996;407-417.
-
(1996)
Fold. Des.
, vol.1
, pp. 407-417
-
-
Gladwin, S.T.1
Evans, P.A.2
-
65
-
-
0037302324
-
Structural composition of betaI- and betaII-proteins
-
Sreerama N., Woody R.W. Structural composition of betaI- and betaII-proteins. Protein Sci. 12:2003;384-388.
-
(2003)
Protein Sci.
, vol.12
, pp. 384-388
-
-
Sreerama, N.1
Woody, R.W.2
-
66
-
-
0030828611
-
Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering
-
Hoshino M., Hagihara Y., Hamada D., Kataoka M., Goto Y. Trifluoroethanol-induced conformational transition of hen egg-white lysozyme studied by small-angle X-ray scattering. FEBS Letters. 416:1997;72-76.
-
(1997)
FEBS Letters
, vol.416
, pp. 72-76
-
-
Hoshino, M.1
Hagihara, Y.2
Hamada, D.3
Kataoka, M.4
Goto, Y.5
-
67
-
-
0031777173
-
Initial hydrophobic collapse is not necessary for folding RNase a
-
Noppert A., Gast K., Zirwer D., Damaschun G. Initial hydrophobic collapse is not necessary for folding RNase A. Fold. Des. 3:1998;213-221.
-
(1998)
Fold. Des.
, vol.3
, pp. 213-221
-
-
Noppert, A.1
Gast, K.2
Zirwer, D.3
Damaschun, G.4
-
68
-
-
0027495402
-
Mutations can cause large changes in the conformation of a denatured protein
-
Flanagan J.M., Kataoka M., Fujisawa T., Engelman D.M. Mutations can cause large changes in the conformation of a denatured protein. Biochemistry. 32:1993;10359-10370.
-
(1993)
Biochemistry
, vol.32
, pp. 10359-10370
-
-
Flanagan, J.M.1
Kataoka, M.2
Fujisawa, T.3
Engelman, D.M.4
-
69
-
-
0031890195
-
Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins
-
Perl D., Welker C., Schindler T., Schroder K., Marahiel M.A., Jaenicke R., Schmid F.X. Conservation of rapid two-state folding in mesophilic, thermophilic and hyperthermophilic cold shock proteins. Nature Struct. Biol. 5:1998;229-235.
-
(1998)
Nature Struct. Biol.
, vol.5
, pp. 229-235
-
-
Perl, D.1
Welker, C.2
Schindler, T.3
Schroder, K.4
Marahiel, M.A.5
Jaenicke, R.6
Schmid, F.X.7
-
70
-
-
0033986637
-
D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding
-
Krantz B.A., Moran L.B., Kentsis A., Sosnick T.R. D/H amide kinetic isotope effects reveal when hydrogen bonds form during protein folding. Nature Struct. Biol. 7:2000;62-71.
-
(2000)
Nature Struct. Biol.
, vol.7
, pp. 62-71
-
-
Krantz, B.A.1
Moran, L.B.2
Kentsis, A.3
Sosnick, T.R.4
-
72
-
-
0028929583
-
Free energy balance in protein folding
-
Honig B., Yang A.S. Free energy balance in protein folding. Advan. Protein Chem. 46:1995;27-58.
-
(1995)
Advan. Protein Chem.
, vol.46
, pp. 27-58
-
-
Honig, B.1
Yang, A.S.2
-
73
-
-
1842448706
-
-
Philadelphia, PA.
-
Sosnick, T. R., Mayne, L., Hiller, R. & Englander, S. W. (1995). Peptide and Protein Folding Workshop, Philadelphia, PA.
-
(1995)
Peptide and Protein Folding Workshop
-
-
Sosnick, T.R.1
Mayne, L.2
Hiller, R.3
Englandery, S.W.4
-
74
-
-
0542436309
-
What limits protein folding
-
O. Jardetzky, & J.F. Lefevre. New York: Plenum Press
-
Sosnick T.R., Englander S.W. What limits protein folding. Jardetzky O., Lefevre J.F. Dynamics and the Problem of Recognition in Biological Macromolecules. Dynamics and the Problem of Recognition in Biological Macromolecules. vol. 288:1996;65-71 Plenum Press, New York.
-
(1996)
Dynamics and the Problem of Recognition in Biological Macromolecules
, vol.288
, pp. 65-71
-
-
Sosnick, T.R.1
Englander, S.W.2
-
75
-
-
0032502839
-
Contact order, transition state placement and the refolding rates of single domain proteins
-
Plaxco K.W., Simons K.T., Baker D. Contact order, transition state placement and the refolding rates of single domain proteins. J. Mol. Biol. 277:1998;985-994.
-
(1998)
J. Mol. Biol.
, vol.277
, pp. 985-994
-
-
Plaxco, K.W.1
Simons, K.T.2
Baker, D.3
-
76
-
-
0034625167
-
Single-molecule protein folding: Diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2
-
Deniz A.A., Laurence T.A., Beligere G.S., Dahan M., Martin A.B., Chemla D.S., et al. Single-molecule protein folding: diffusion fluorescence resonance energy transfer studies of the denaturation of chymotrypsin inhibitor 2. Proc. Natl Acad. Sci. USA. 97:2000;5179-5184.
-
(2000)
Proc. Natl Acad. Sci. USA
, vol.97
, pp. 5179-5184
-
-
Deniz, A.A.1
Laurence, T.A.2
Beligere, G.S.3
Dahan, M.4
Martin, A.B.5
Chemla, D.S.6
-
77
-
-
0043009768
-
A four-way junction accelerates hairpin ribozyme folding via a discrete intermediate
-
Tan E., Wilson T.J., Nahas M.K., Clegg R.M., Lilley D.M., Ha T. A four-way junction accelerates hairpin ribozyme folding via a discrete intermediate. Proc. Natl Acad. Sci. USA. 100:2003;9308-9313.
-
(2003)
Proc. Natl Acad. Sci. USA
, vol.100
, pp. 9308-9313
-
-
Tan, E.1
Wilson, T.J.2
Nahas, M.K.3
Clegg, R.M.4
Lilley, D.M.5
Ha, T.6
-
78
-
-
0028783624
-
Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy
-
Zitzewitz J.A., Bilsel O., Luo J., Jones B.E., Matthews C.R. Probing the folding mechanism of a leucine zipper peptide by stopped-flow circular dichroism spectroscopy. Biochemistry. 34:1995;12812-12819.
-
(1995)
Biochemistry
, vol.34
, pp. 12812-12819
-
-
Zitzewitz, J.A.1
Bilsel, O.2
Luo, J.3
Jones, B.E.4
Matthews, C.R.5
-
79
-
-
0034718547
-
Absence of stable intermediates on the folding pathway of barnase
-
Takei J., Chu R.A., Bai Y. Absence of stable intermediates on the folding pathway of barnase. Proc. Natl Acad. Sci. USA. 97:2000;10796-10801.
-
(2000)
Proc. Natl Acad. Sci. USA
, vol.97
, pp. 10796-10801
-
-
Takei, J.1
Chu, R.A.2
Bai, Y.3
-
80
-
-
0025999787
-
Hydrogen exchange in thermally denatured ribonuclease a
-
Robertson A.D., Baldwin R.L. Hydrogen exchange in thermally denatured ribonuclease A. Biochemistry. 30:1991;9907-9914.
-
(1991)
Biochemistry
, vol.30
, pp. 9907-9914
-
-
Robertson, A.D.1
Baldwin, R.L.2
-
81
-
-
0029978353
-
Analysis of main chain torsion angles in proteins: Prediction of NMR coupling constants for native and random coil conformations
-
Smith L.J., Bolin K.A., Schwalbe H., MacArthur M.W., Thornton J.M., Dobson C.M. Analysis of main chain torsion angles in proteins: prediction of NMR coupling constants for native and random coil conformations. J. Mol. Biol. 255:1996;494-506.
-
(1996)
J. Mol. Biol.
, vol.255
, pp. 494-506
-
-
Smith, L.J.1
Bolin, K.A.2
Schwalbe, H.3
MacArthur, M.W.4
Thornton, J.M.5
Dobson, C.M.6
-
82
-
-
0028790273
-
Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation
-
Serrano L. Comparison between the phi distribution of the amino acids in the protein database and NMR data indicates that amino acids have various phi propensities in the random coil conformation. J. Mol. Biol. 254:1995;322-333.
-
(1995)
J. Mol. Biol.
, vol.254
, pp. 322-333
-
-
Serrano, L.1
-
83
-
-
0030726550
-
NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein
-
Penkett C.J., Redfield C., Dodd I., Hubbard J., McBay D.L., Mossakowska D.E., et al. NMR analysis of main-chain conformational preferences in an unfolded fibronectin-binding protein. J. Mol. Biol. 274:1997;152-159.
-
(1997)
J. Mol. Biol.
, vol.274
, pp. 152-159
-
-
Penkett, C.J.1
Redfield, C.2
Dodd, I.3
Hubbard, J.4
McBay, D.L.5
Mossakowska, D.E.6
-
84
-
-
0029147823
-
Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures
-
Swindells M.B., MacArthur M.W., Thornton J.M. Intrinsic phi, psi propensities of amino acids, derived from the coil regions of known structures. Nature Struct. Biol. 2:1995;596-603.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 596-603
-
-
Swindells, M.B.1
MacArthur, M.W.2
Thornton, J.M.3
-
85
-
-
0037610743
-
Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: Distributions of phi
-
Avbelj F., Baldwin R.L. Role of backbone solvation and electrostatics in generating preferred peptide backbone conformations: distributions of phi. Proc. Natl Acad. Sci. USA. 100:2003;5742-5747.
-
(2003)
Proc. Natl Acad. Sci. USA
, vol.100
, pp. 5742-5747
-
-
Avbelj, F.1
Baldwin, R.L.2
-
86
-
-
0037047134
-
Polyproline II structure in a sequence of seven alanine residues
-
Shi Z., Olson C.A., Rose G.D., Baldwin R.L., Kallenbach N.R. Polyproline II structure in a sequence of seven alanine residues. Proc. Natl Acad. Sci. USA. 99:2002;9190-9195.
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 9190-9195
-
-
Shi, Z.1
Olson, C.A.2
Rose, G.D.3
Baldwin, R.L.4
Kallenbach, N.R.5
-
87
-
-
0036400325
-
Is polyproline II a major backbone conformation in unfolded proteins?
-
Shi Z., Woody R.W., Kallenbach N.R. Is polyproline II a major backbone conformation in unfolded proteins? Advan. Protein Chem. 62:2002;163-240.
-
(2002)
Advan. Protein Chem.
, vol.62
, pp. 163-240
-
-
Shi, Z.1
Woody, R.W.2
Kallenbach, N.R.3
-
88
-
-
0038344087
-
Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy
-
Eker F., Griebenow K., Schweitzer-Stenner R. Stable conformations of tripeptides in aqueous solution studied by UV circular dichroism spectroscopy. J. Am. Chem. Soc. 125:2003;8178-8185.
-
(2003)
J. Am. Chem. Soc.
, vol.125
, pp. 8178-8185
-
-
Eker, F.1
Griebenow, K.2
Schweitzer-Stenner, R.3
-
89
-
-
0036784642
-
A simple model for polyproline II structure in unfolded states of alanine-based peptides
-
Pappu R.V., Rose G.D. A simple model for polyproline II structure in unfolded states of alanine-based peptides. Protein Sci. 10:2002;2437-2455.
-
(2002)
Protein Sci.
, vol.10
, pp. 2437-2455
-
-
Pappu, R.V.1
Rose, G.D.2
-
90
-
-
0036402323
-
Determinants of the polyproline II helix from modeling studies
-
Creamer T.P., Campbell M.N. Determinants of the polyproline II helix from modeling studies. Advan. Protein Chem. 62:2002;263-282.
-
(2002)
Advan. Protein Chem.
, vol.62
, pp. 263-282
-
-
Creamer, T.P.1
Campbell, M.N.2
-
91
-
-
0026355426
-
Reassessment of the random coil conformation: Vibrational CD study of proline oligopeptides and related polypeptides
-
Dukor R.K., Keiderling T.A. Reassessment of the random coil conformation: vibrational CD study of proline oligopeptides and related polypeptides. Biopolymers. 31:1991;1747-1761.
-
(1991)
Biopolymers
, vol.31
, pp. 1747-1761
-
-
Dukor, R.K.1
Keiderling, T.A.2
-
92
-
-
84987322752
-
The circular dichroism spectrum and structure of unordered polypeptides and proteins
-
Krimm S., Tiffany M.L. The circular dichroism spectrum and structure of unordered polypeptides and proteins. Isr. J. Chem. 12:1974;189-200.
-
(1974)
Isr. J. Chem.
, vol.12
, pp. 189-200
-
-
Krimm, S.1
Tiffany, M.L.2
-
93
-
-
0029842116
-
Residual structure in unfolded proteins revealed by Raman optical activity
-
Wilson G., Hecht L., Barron L.D. Residual structure in unfolded proteins revealed by Raman optical activity. Biochemistry. 35:1996;12518-12525.
-
(1996)
Biochemistry
, vol.35
, pp. 12518-12525
-
-
Wilson, G.1
Hecht, L.2
Barron, L.D.3
-
94
-
-
0036400324
-
Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra
-
Keiderling T.A., Xu Q. Unfolded peptides and proteins studied with infrared absorption and vibrational circular dichroism spectra. Advan. Protein Chem. 62:2002;111-161.
-
(2002)
Advan. Protein Chem.
, vol.62
, pp. 111-161
-
-
Keiderling, T.A.1
Xu, Q.2
-
95
-
-
0028577684
-
Conservation of polyproline II helices in homologous proteins: Implications for structure prediction by model building
-
Adzhubei A.A., Sternberg M.J. Conservation of polyproline II helices in homologous proteins: implications for structure prediction by model building. Protein Sci. 3:1994;2395-2410.
-
(1994)
Protein Sci.
, vol.3
, pp. 2395-2410
-
-
Adzhubei, A.A.1
Sternberg, M.J.2
-
96
-
-
0031692650
-
Left-handed polyproline II helix formation is (very) locally driven
-
Creamer T.P. Left-handed polyproline II helix formation is (very) locally driven. Proteins: Struct. Funct. Genet. 33:1998;218-226.
-
(1998)
Proteins: Struct. Funct. Genet.
, vol.33
, pp. 218-226
-
-
Creamer, T.P.1
-
99
-
-
0345862082
-
Characterization of non-alpha helical conformations in Ala peptides
-
Garcia A.E. Characterization of non-alpha helical conformations in Ala peptides. Polymers. 45:2004;669-676.
-
(2004)
Polymers
, vol.45
, pp. 669-676
-
-
Garcia, A.E.1
-
100
-
-
18744388560
-
Circular dichroism spectra of short, fixed-nucleus alanine helices
-
Chin D.H., Woody R.W., Rohl C.A., Baldwin R.L. Circular dichroism spectra of short, fixed-nucleus alanine helices. Proc. Natl Acad. Sci. USA. 99:2002;15416-15421.
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 15416-15421
-
-
Chin, D.H.1
Woody, R.W.2
Rohl, C.A.3
Baldwin, R.L.4
-
101
-
-
0031936293
-
The methanol-induced transition and the expanded helical conformation in hen lysozyme
-
Kamatari Y.O., Konno T., Kataoka M., Akasaka K. The methanol-induced transition and the expanded helical conformation in hen lysozyme. Protein Sci. 7:1998;681-688.
-
(1998)
Protein Sci.
, vol.7
, pp. 681-688
-
-
Kamatari, Y.O.1
Konno, T.2
Kataoka, M.3
Akasaka, K.4
-
102
-
-
0029893286
-
The methanol-induced globular and expanded denatured states of cytochrome c: A study by CD fluorescence, NMR and small-angle X-ray scattering
-
Kamatari Y.O., Konno T., Kataoka M., Akasaka K. The methanol-induced globular and expanded denatured states of cytochrome c: a study by CD fluorescence, NMR and small-angle X-ray scattering. J. Mol. Biol. 259:1996;512-523.
-
(1996)
J. Mol. Biol.
, vol.259
, pp. 512-523
-
-
Kamatari, Y.O.1
Konno, T.2
Kataoka, M.3
Akasaka, K.4
-
104
-
-
0023517017
-
Effects of point mutations on the folding of globular proteins
-
Matthews C.R. Effects of point mutations on the folding of globular proteins. Methods Enzymol. 154:1987;498-511.
-
(1987)
Methods Enzymol.
, vol.154
, pp. 498-511
-
-
Matthews, C.R.1
|