-
1
-
-
0031052147
-
A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding
-
Rank J.A., and Baker D. A desolvation barrier to hydrophobic cluster formation may contribute to the rate-limiting step in protein folding. Protein Sci. 6 (1997) 347-354
-
(1997)
Protein Sci.
, vol.6
, pp. 347-354
-
-
Rank, J.A.1
Baker, D.2
-
2
-
-
0037154268
-
Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after structural collapse
-
Cheung S.M., Garcia A.E., and Onuchic J.N. Protein folding mediated by solvation: water expulsion and formation of the hydrophobic core occur after structural collapse. Proc. Natl Acad. Sci. USA 99 (2002) 685-690
-
(2002)
Proc. Natl Acad. Sci. USA
, vol.99
, pp. 685-690
-
-
Cheung, S.M.1
Garcia, A.E.2
Onuchic, J.N.3
-
3
-
-
19444384541
-
Desolvation is a likely origin of robust enthalpic barriers to protein folding
-
Liu Z., and Chan H.S. Desolvation is a likely origin of robust enthalpic barriers to protein folding. J. Mol. Biol. 349 (2005) 872-889
-
(2005)
J. Mol. Biol.
, vol.349
, pp. 872-889
-
-
Liu, Z.1
Chan, H.S.2
-
4
-
-
27744500841
-
Solvation and desolvation effects in protein folding: native flexibility, kinetic cooperativity ad enthalpic barriers under isostability conditions
-
Liu Z., and Chan H.S. Solvation and desolvation effects in protein folding: native flexibility, kinetic cooperativity ad enthalpic barriers under isostability conditions. Phys. Biol. 2 (2005) S75-S85
-
(2005)
Phys. Biol.
, vol.2
-
-
Liu, Z.1
Chan, H.S.2
-
5
-
-
11844285690
-
Temperature dependence of three-body hydrophobic interactions: potential of mean force, enthalpy, entropy, heat capacity, and nonadditivity
-
Moghaddam M.S., Shimizu S., and Chan H.S. Temperature dependence of three-body hydrophobic interactions: potential of mean force, enthalpy, entropy, heat capacity, and nonadditivity. J. Am. Chem. Soc. 127 (2005) 303-316
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 303-316
-
-
Moghaddam, M.S.1
Shimizu, S.2
Chan, H.S.3
-
7
-
-
33748442685
-
Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates
-
Rodríguez-Larrea D., Ibarra-Molero B., and Sanchez-Ruiz J.M. Energetic and structural consequences of desolvation/solvation barriers to protein folding/unfolding assessed from experimental unfolding rates. Biophys. J. 91 (2006) L48-L50
-
(2006)
Biophys. J.
, vol.91
-
-
Rodríguez-Larrea, D.1
Ibarra-Molero, B.2
Sanchez-Ruiz, J.M.3
-
8
-
-
34547516861
-
Hydrophobic association of α-helices, steric dewetting, and enthalpic barriers to protein folding
-
MacCallum J.L., Moghaddam M.S., Chan H.S., and Tieleman D.P. Hydrophobic association of α-helices, steric dewetting, and enthalpic barriers to protein folding. Proc. Natl Acad. Sci. USA 104 (2007) 6206-6210
-
(2007)
Proc. Natl Acad. Sci. USA
, vol.104
, pp. 6206-6210
-
-
MacCallum, J.L.1
Moghaddam, M.S.2
Chan, H.S.3
Tieleman, D.P.4
-
9
-
-
33749365298
-
A molecular mechanism for osmolyte-induced protein stability
-
Street T.O., Bolen D.W., and Rose G.D. A molecular mechanism for osmolyte-induced protein stability. Proc. Natl Acad. Sci. USA 103 (2006) 13997-14002
-
(2006)
Proc. Natl Acad. Sci. USA
, vol.103
, pp. 13997-14002
-
-
Street, T.O.1
Bolen, D.W.2
Rose, G.D.3
-
10
-
-
42149084432
-
Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model
-
Gong H., and Rose G.D. Assessing the solvent-dependent surface area of unfolded proteins using an ensemble model. Proc. Natl Acad. Sci. USA 105 (2008) 3321-3326
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 3321-3326
-
-
Gong, H.1
Rose, G.D.2
-
11
-
-
0001002352
-
Conformation changes in proteins
-
Lumry R., and Eyring E. Conformation changes in proteins. J. Phys. Chem. 58 (1954) 110-120
-
(1954)
J. Phys. Chem.
, vol.58
, pp. 110-120
-
-
Lumry, R.1
Eyring, E.2
-
12
-
-
0026586591
-
Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry
-
Sanchez-Ruiz J.M. Theoretical analysis of Lumry-Eyring models in differential scanning calorimetry. Biophys. J. 61 (1992) 921-935
-
(1992)
Biophys. J.
, vol.61
, pp. 921-935
-
-
Sanchez-Ruiz, J.M.1
-
13
-
-
0034237295
-
Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases
-
Plaza del Pino I.M., Ibarra-Molero B., and Sanchez-Ruiz J.M. Lower kinetic limit to protein thermal stability: a proposal regarding protein stability in vivo and its relation with misfolding diseases. Proteins Struct. Funct. Genet. 40 (2000) 58-70
-
(2000)
Proteins Struct. Funct. Genet.
, vol.40
, pp. 58-70
-
-
Plaza del Pino, I.M.1
Ibarra-Molero, B.2
Sanchez-Ruiz, J.M.3
-
14
-
-
0031149622
-
A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions
-
Schnyrov V.I., Zhadan G.G., Cobaleda C., Muñoz-Barroso I., and Villar E. A differential scanning calorimetric study of Newcastle disease virus: identification of proteins involved in thermal transitions. Arch. Biochem. Biophys. 341 (1997) 89-97
-
(1997)
Arch. Biochem. Biophys.
, vol.341
, pp. 89-97
-
-
Schnyrov, V.I.1
Zhadan, G.G.2
Cobaleda, C.3
Muñoz-Barroso, I.4
Villar, E.5
-
15
-
-
0032558779
-
Unfolded conformation of alpha-lytic protease are more stable than its native state
-
Sohl J.L., Jaswal S.S., and Agard D.A. Unfolded conformation of alpha-lytic protease are more stable than its native state. Nature 395 (1998) 817-819
-
(1998)
Nature
, vol.395
, pp. 817-819
-
-
Sohl, J.L.1
Jaswal, S.S.2
Agard, D.A.3
-
16
-
-
0033200063
-
Protein misfolding, evolution and disease
-
Dobson C.M. Protein misfolding, evolution and disease. Trends Biochem. Sci. 24 (1998) 329-332
-
(1998)
Trends Biochem. Sci.
, vol.24
, pp. 329-332
-
-
Dobson, C.M.1
-
17
-
-
0037122769
-
Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability
-
Jaswal S.S., Sohl J.L., Dans J.H., and Agard D.A. Energetic landscape of alpha-lytic protease optimizes longevity through kinetic stability. Nature 415 (2002) 343-346
-
(2002)
Nature
, vol.415
, pp. 343-346
-
-
Jaswal, S.S.1
Sohl, J.L.2
Dans, J.H.3
Agard, D.A.4
-
20
-
-
4444330121
-
Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure
-
Manning M., and Colon W. Structural basis of protein kinetic stability: resistance to sodium dodecyl sulfate suggests a central role for rigidity and a bias toward beta-sheet structure. Biochemistry 43 (2004) 11248-11254
-
(2004)
Biochemistry
, vol.43
, pp. 11248-11254
-
-
Manning, M.1
Colon, W.2
-
21
-
-
11144256229
-
Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS
-
Lynch S.M., Boswell S.A., and Colon W. Kinetic stability of Cu/Zn superoxide dismutase is dependent on its metal ligands: implications for ALS. Biochemistry 43 (2004) 16525-16531
-
(2004)
Biochemistry
, vol.43
, pp. 16525-16531
-
-
Lynch, S.M.1
Boswell, S.A.2
Colon, W.3
-
22
-
-
7044264514
-
Kinetic stability and crystal structure of the viral capside protein SHP
-
Forrer P., Chang C., Ott D., Wlodawer A., and Plückthun A. Kinetic stability and crystal structure of the viral capside protein SHP. J. Mol. Biol. 344 (2004) 179-193
-
(2004)
J. Mol. Biol.
, vol.344
, pp. 179-193
-
-
Forrer, P.1
Chang, C.2
Ott, D.3
Wlodawer, A.4
Plückthun, A.5
-
23
-
-
14844357602
-
Structural basis for thermal stability of human low-density lipoprotein
-
Jaramayan S., Gantz D., and Gursky O. Structural basis for thermal stability of human low-density lipoprotein. Biochemistry 44 (2005) 3965-3971
-
(2005)
Biochemistry
, vol.44
, pp. 3965-3971
-
-
Jaramayan, S.1
Gantz, D.2
Gursky, O.3
-
24
-
-
23944522022
-
Downhill protein folding: evolution meets physics
-
Gruebele M. Downhill protein folding: evolution meets physics. C. R. Biol. 328 (2005) 701-712
-
(2005)
C. R. Biol.
, vol.328
, pp. 701-712
-
-
Gruebele, M.1
-
25
-
-
14644412777
-
Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases
-
Jaswal S.S., Truhlar S.M., Dill K.A., and Agard D.A. Comprehensive analysis of protein folding activation thermodynamics reveals a universal behaviour violated by kinetically stable proteases. J. Mol. Biol. 347 (2005) 355-366
-
(2005)
J. Mol. Biol.
, vol.347
, pp. 355-366
-
-
Jaswal, S.S.1
Truhlar, S.M.2
Dill, K.A.3
Agard, D.A.4
-
26
-
-
33748454832
-
Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments
-
Godoy-Ruiz R., Ariza F., Rodríguez-Larrea D., Perez-Jimenez R., Ibarra-Molero B., and Sanchez-Ruiz J.M. Natural selection for kinetic stability is a likely origin of correlations between mutational effects on protein energetics and frequencies of amino acid occurrences in sequence alignments. J. Mol. Biol. 362 (2006) 966-978
-
(2006)
J. Mol. Biol.
, vol.362
, pp. 966-978
-
-
Godoy-Ruiz, R.1
Ariza, F.2
Rodríguez-Larrea, D.3
Perez-Jimenez, R.4
Ibarra-Molero, B.5
Sanchez-Ruiz, J.M.6
-
27
-
-
33645654042
-
Effects of salt on the thermal stability of human plasma high-density lipoprotein
-
Jaramayan S., Gantz D.L., and Gursky O. Effects of salt on the thermal stability of human plasma high-density lipoprotein. Biochemistry 45 (2006) 4620-4628
-
(2006)
Biochemistry
, vol.45
, pp. 4620-4628
-
-
Jaramayan, S.1
Gantz, D.L.2
Gursky, O.3
-
28
-
-
33750078696
-
Glutamine deamidation destabilizes human γd-crystallin and lowers the kinetic barrier to unfolding
-
Flaugh S.L., Mills I.A., and King J. Glutamine deamidation destabilizes human γd-crystallin and lowers the kinetic barrier to unfolding. J. Biol. Chem. 281 (2006) 30782-30793
-
(2006)
J. Biol. Chem.
, vol.281
, pp. 30782-30793
-
-
Flaugh, S.L.1
Mills, I.A.2
King, J.3
-
29
-
-
34247239927
-
Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability
-
Young T.A., Skordakales E., and Marqusee S. Comparison of proteolytic susceptibility in phosphoglycerate kinases from yeast and E. coli: modulation of conformational ensembles without altering structure or stability. J. Mol. Biol. 368 (2007) 1438-1447
-
(2007)
J. Mol. Biol.
, vol.368
, pp. 1438-1447
-
-
Young, T.A.1
Skordakales, E.2
Marqusee, S.3
-
30
-
-
34247180735
-
Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis
-
Park C., Zhou S., Gilmore J., and Marqusee S. Energetics-based protein profiling on a proteomic scale: identification of proteins resistant to proteolysis. J. Mol. Biol. 368 (2007) 1426-1437
-
(2007)
J. Mol. Biol.
, vol.368
, pp. 1426-1437
-
-
Park, C.1
Zhou, S.2
Gilmore, J.3
Marqusee, S.4
-
31
-
-
36849036714
-
Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE
-
Xia K., Manning M., Hesham H., Bystroff C., and Colon W. Identifying the subproteome of kinetically stable proteins via diagonal 2D SDS/PAGE. Proc. Natl Acad. Sci. USA 104 (2007) 17329-17334
-
(2007)
Proc. Natl Acad. Sci. USA
, vol.104
, pp. 17329-17334
-
-
Xia, K.1
Manning, M.2
Hesham, H.3
Bystroff, C.4
Colon, W.5
-
32
-
-
34249092307
-
Thermal transitions in human very-low-density lipoprotein: fusion, rupture, and dissociation of HDL-like particles
-
Guha M., England C., Herscovitz H., and Gursky O. Thermal transitions in human very-low-density lipoprotein: fusion, rupture, and dissociation of HDL-like particles. Biochemistry 46 (2007) 6043-6049
-
(2007)
Biochemistry
, vol.46
, pp. 6043-6049
-
-
Guha, M.1
England, C.2
Herscovitz, H.3
Gursky, O.4
-
33
-
-
34047133713
-
Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophile behaviour
-
Kelch B.A., Eagen K.P., Pinar Erciyas P., Humphris E.L., Thomason A.R., Mitsuiki S., and Agard D.A. Structural and mechanistic exploration of acid resistance: kinetic stability facilitates evolution of extremophile behaviour. J. Mol. Biol. 368 (2007) 870-883
-
(2007)
J. Mol. Biol.
, vol.368
, pp. 870-883
-
-
Kelch, B.A.1
Eagen, K.P.2
Pinar Erciyas, P.3
Humphris, E.L.4
Thomason, A.R.5
Mitsuiki, S.6
Agard, D.A.7
-
34
-
-
34249933886
-
Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability
-
Kelch B.A., and Agard D.A. Mesophile versus thermophile: insights into the structural mechanisms of kinetic stability. J. Mol. Biol. 370 (2007) 784-795
-
(2007)
J. Mol. Biol.
, vol.370
, pp. 784-795
-
-
Kelch, B.A.1
Agard, D.A.2
-
35
-
-
0037473750
-
Prevention of transthyretin amyloid disease by changing protein misfolding energetics
-
Hammarström P., Wiseman R.L., Powers E.T., and Kelly J.W. Prevention of transthyretin amyloid disease by changing protein misfolding energetics. Science 299 (2003) 713-716
-
(2003)
Science
, vol.299
, pp. 713-716
-
-
Hammarström, P.1
Wiseman, R.L.2
Powers, E.T.3
Kelly, J.W.4
-
36
-
-
18644384035
-
Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state
-
Petrassi M.M., Johnson S.M., Purkey H.E., Chiang K.P., Walkup T., Jinag X., et al. Potent and selective structure-based dibenzofuran inhibitors of transthyretin amyloidogenesis: kinetic stabilization of the native state. J. Am. Chem. Soc. 127 (2005) 5540-5541
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 5540-5541
-
-
Petrassi, M.M.1
Johnson, S.M.2
Purkey, H.E.3
Chiang, K.P.4
Walkup, T.5
Jinag, X.6
-
37
-
-
14944376972
-
Kinetic stabilization of an oligomeric protein by a single ligand binding event
-
Wiseman R.L., Jonson S.M., Keller M.S., Foss T., Wilson I.A., and Kelly J.W. Kinetic stabilization of an oligomeric protein by a single ligand binding event. J. Am. Chem. Soc. 127 (2005) 5540-5541
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 5540-5541
-
-
Wiseman, R.L.1
Jonson, S.M.2
Keller, M.S.3
Foss, T.4
Wilson, I.A.5
Kelly, J.W.6
-
38
-
-
26844546899
-
Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis
-
Green N.S., Foss T.R., and Kelly J.W. Genistein, a natural product from soy, is a potent inhibitor of transthyretin amyloidosis. Proc. Natl Acad. Sci. USA 102 (2005) 14545-14550
-
(2005)
Proc. Natl Acad. Sci. USA
, vol.102
, pp. 14545-14550
-
-
Green, N.S.1
Foss, T.R.2
Kelly, J.W.3
-
39
-
-
33751082387
-
Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis
-
Sekijima Y., Dendle M.A., and Kelly J.W. Orally administered diflunisal stabilizes transthyretin against dissociation required for amyloidogenesis. Amyloid 13 (2006) 236-249
-
(2006)
Amyloid
, vol.13
, pp. 236-249
-
-
Sekijima, Y.1
Dendle, M.A.2
Kelly, J.W.3
-
40
-
-
0025882523
-
The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three complexes
-
Noble M.E., Wierenga R.K., Lambeir A.M., Opperdoes F.R., Thunnissen A.M., Kalk K.H., et al. The adaptability of the active site of trypanosomal triosephosphate isomerase as observed in the crystal structures of three complexes. Proteins Struct. Funct. Genet. 10 (1991) 50-69
-
(1991)
Proteins Struct. Funct. Genet.
, vol.10
, pp. 50-69
-
-
Noble, M.E.1
Wierenga, R.K.2
Lambeir, A.M.3
Opperdoes, F.R.4
Thunnissen, A.M.5
Kalk, K.H.6
-
41
-
-
0029557025
-
Using evolutionary changes to achieve species-specific inhibition of enzyme action studies with triosephosphate isomerase
-
Gómez-Puyou A., Saavedra-Lira E., Becker I., Zubillaga R.A., Rojo-Domínguez A., and Pérez-Monfort R. Using evolutionary changes to achieve species-specific inhibition of enzyme action studies with triosephosphate isomerase. Chem. Biol. 2 (1995) 847-855
-
(1995)
Chem. Biol.
, vol.2
, pp. 847-855
-
-
Gómez-Puyou, A.1
Saavedra-Lira, E.2
Becker, I.3
Zubillaga, R.A.4
Rojo-Domínguez, A.5
Pérez-Monfort, R.6
-
42
-
-
0031570683
-
Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design
-
Velanker S.S., Ray S.S., Gokhale R.S., Balaram H., Balaram P., and Murphy M.R.N. Triosephosphate isomerase from Plasmodium falciparum: the crystal structure provides insights into antimalarial drug design. Structure 5 (1997) 751-761
-
(1997)
Structure
, vol.5
, pp. 751-761
-
-
Velanker, S.S.1
Ray, S.S.2
Gokhale, R.S.3
Balaram, H.4
Balaram, P.5
Murphy, M.R.N.6
-
43
-
-
4143068388
-
Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface
-
Téllez-Valencia A., Olivares-Illana V., Hernández-Santoyo A., Pérez-Monfort R., Costas M., Rodríguez-Romero A., et al. Inactivation of triosephosphate isomerase from Trypanosoma cruzi by an agent that perturbs its dimer interface. J. Mol. Biol. 341 (2004) 1355-1365
-
(2004)
J. Mol. Biol.
, vol.341
, pp. 1355-1365
-
-
Téllez-Valencia, A.1
Olivares-Illana, V.2
Hernández-Santoyo, A.3
Pérez-Monfort, R.4
Costas, M.5
Rodríguez-Romero, A.6
-
44
-
-
33644535470
-
Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor
-
Olivares-Illana V., Pérez-Monfort R., López-Calahorra F., Costas M., Rodríguez-Romero A., Tuena de Gómez-Puyou M., et al. Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor. Biochemistry 45 (2006) 2556-2560
-
(2006)
Biochemistry
, vol.45
, pp. 2556-2560
-
-
Olivares-Illana, V.1
Pérez-Monfort, R.2
López-Calahorra, F.3
Costas, M.4
Rodríguez-Romero, A.5
Tuena de Gómez-Puyou, M.6
-
45
-
-
47749092414
-
Perturbation of the dimer interface of triosephosphate isomerase and its effect on Trypanosoma cruzi
-
10.1371/journal.pndt.0000001
-
Olivares-Illana V., Rodríguez-Romero A., Becker I., Berzunza M., García J., Pérez-Monfort R., et al. Perturbation of the dimer interface of triosephosphate isomerase and its effect on Trypanosoma cruzi. PLoS Negl. Trop. Dis. 1 1 (2007) e01 10.1371/journal.pndt.0000001
-
(2007)
PLoS Negl. Trop. Dis.
, vol.1
, Issue.1
-
-
Olivares-Illana, V.1
Rodríguez-Romero, A.2
Becker, I.3
Berzunza, M.4
García, J.5
Pérez-Monfort, R.6
-
46
-
-
43449098518
-
Kemp elimination catalysts by computational enzyme design
-
Röthlisberger D., Khersonsky O., Wollacott A.M., Jiang L., DeChancie J., Betker J., et al. Kemp elimination catalysts by computational enzyme design. Nature 453 (2008) 164-166
-
(2008)
Nature
, vol.453
, pp. 164-166
-
-
Röthlisberger, D.1
Khersonsky, O.2
Wollacott, A.M.3
Jiang, L.4
DeChancie, J.5
Betker, J.6
-
47
-
-
0033579862
-
Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels
-
Bilsel O., Zitzewitz J.A., Bowers K.E., and Matthews C.R. Folding mechanism of the alpha-subunit of tryptophan synthase, an alpha/beta barrel protein: global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels. Biochemistry 38 (1999) 1018-1029
-
(1999)
Biochemistry
, vol.38
, pp. 1018-1029
-
-
Bilsel, O.1
Zitzewitz, J.A.2
Bowers, K.E.3
Matthews, C.R.4
-
48
-
-
39649117122
-
NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein
-
Vadrevu R., Wu Y., and Matthews C.R. NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein. J. Mol. Biol. 377 (2008) 294-305
-
(2008)
J. Mol. Biol.
, vol.377
, pp. 294-305
-
-
Vadrevu, R.1
Wu, Y.2
Matthews, C.R.3
-
49
-
-
0028820703
-
Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein folding
-
Myers J.K., Pace C.N., and Scholtz J.M. Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein folding. Protein Sci. 4 (1995) 2138-2148
-
(1995)
Protein Sci.
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
50
-
-
0028271856
-
Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase
-
Chen X., and Matthews C.R. Thermodynamic properties of the transition state for the rate-limiting step in the folding of the alpha subunit of tryptophan synthase. Biochemistry 33 (1994) 6356-6362
-
(1994)
Biochemistry
, vol.33
, pp. 6356-6362
-
-
Chen, X.1
Matthews, C.R.2
-
51
-
-
0037444807
-
Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reason for the oligomeric nature of the enzyme
-
Najera H., Costas M., and Fernández-Velasco D.A. Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reason for the oligomeric nature of the enzyme. Biochem. J. 370 (2003) 785-792
-
(2003)
Biochem. J.
, vol.370
, pp. 785-792
-
-
Najera, H.1
Costas, M.2
Fernández-Velasco, D.A.3
-
52
-
-
23844433968
-
Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates
-
Chánez-Cárdenas M.E., Pérez-Hernández G., Shánchez-Rebollar B.G., Costas M., and Vázquez-Contreras E. Reversible equilibrium unfolding of triosephosphate isomerase from Trypanosoma cruzi in guanidinium hydrochloride involves stable dimeric and monomeric intermediates. Biochemistry 44 (2005) 10883-10892
-
(2005)
Biochemistry
, vol.44
, pp. 10883-10892
-
-
Chánez-Cárdenas, M.E.1
Pérez-Hernández, G.2
Shánchez-Rebollar, B.G.3
Costas, M.4
Vázquez-Contreras, E.5
-
53
-
-
0000159569
-
Protein structure and the energetics of protein stability
-
Robertson A.D., and Murphy K.P. Protein structure and the energetics of protein stability. Chem. Rev. 97 (1997) 1251-1268
-
(1997)
Chem. Rev.
, vol.97
, pp. 1251-1268
-
-
Robertson, A.D.1
Murphy, K.P.2
-
54
-
-
0029957505
-
The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations
-
Hilser V.J., Gómez J., and Freire E. The enthalpy change in protein folding and binding: refinement of parameters for structure-based calculations. Proteins Struct. Funct. Genet. 26 (1996) 123-133
-
(1996)
Proteins Struct. Funct. Genet.
, vol.26
, pp. 123-133
-
-
Hilser, V.J.1
Gómez, J.2
Freire, E.3
-
56
-
-
44949236102
-
Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data
-
Godoy-Ruiz R., Henry E.R., Kubelka J., Hofrichter J., Muñoz V., Sanchez-Ruiz J.M., and Eaton W.A. Estimating free-energy barrier heights for an ultrafast folding protein from calorimetric and kinetic data. J. Phys. Chem. B 112 (2008) 5938-5949
-
(2008)
J. Phys. Chem. B
, vol.112
, pp. 5938-5949
-
-
Godoy-Ruiz, R.1
Henry, E.R.2
Kubelka, J.3
Hofrichter, J.4
Muñoz, V.5
Sanchez-Ruiz, J.M.6
Eaton, W.A.7
-
57
-
-
44949091517
-
Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha-beta topology that folds downhill
-
Fung A., Li P., Godoy-Ruiz R., Sanchez-Ruiz J.M., and Muñoz V. Expanding the realm of ultrafast protein folding: gpW, a midsize natural single-domain with alpha-beta topology that folds downhill. J. Am. Chem. Soc. 130 (2008) 7489-7495
-
(2008)
J. Am. Chem. Soc.
, vol.130
, pp. 7489-7495
-
-
Fung, A.1
Li, P.2
Godoy-Ruiz, R.3
Sanchez-Ruiz, J.M.4
Muñoz, V.5
-
58
-
-
0014722597
-
Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water
-
Lumry R., and Rajender S. Enthalpy-entropy compensation phenomena in water solutions of proteins and small molecules: a ubiquitous property of water. Biopolymers 9 (1970) 1125-1227
-
(1970)
Biopolymers
, vol.9
, pp. 1125-1227
-
-
Lumry, R.1
Rajender, S.2
-
59
-
-
0035965868
-
Heat does not come in different colours: entropy-enthalpy compensation, free-energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions
-
Cooper A., Johnson C.M., Lakey J.H., and Nöllmann M. Heat does not come in different colours: entropy-enthalpy compensation, free-energy windows, quantum confinement, pressure perturbation calorimetry, solvation and the multiple causes of heat capacity effects in biomolecular interactions. Biophys. Chem. 93 (2001) 215-230
-
(2001)
Biophys. Chem.
, vol.93
, pp. 215-230
-
-
Cooper, A.1
Johnson, C.M.2
Lakey, J.H.3
Nöllmann, M.4
-
60
-
-
0035107447
-
Entropy-enthalpy compensation: fact or artifact
-
Sharp K. Entropy-enthalpy compensation: fact or artifact. Protein Sci. 10 (2001) 661-667
-
(2001)
Protein Sci.
, vol.10
, pp. 661-667
-
-
Sharp, K.1
-
61
-
-
0027991081
-
Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation
-
Lee K.H., Xie D., Freire E., and Amzel L.M. Estimation of changes in side chain configurational entropy in binding and folding: general methods and application to helix formation. Proteins Struct. Funct. Genet. 20 (1994) 68-84
-
(1994)
Proteins Struct. Funct. Genet.
, vol.20
, pp. 68-84
-
-
Lee, K.H.1
Xie, D.2
Freire, E.3
Amzel, L.M.4
-
62
-
-
12944309313
-
Scaling of folding times with protein size
-
Naganathan A.N., and Muñoz V. Scaling of folding times with protein size. J. Am. Chem. Soc. 127 (2005) 480-481
-
(2005)
J. Am. Chem. Soc.
, vol.127
, pp. 480-481
-
-
Naganathan, A.N.1
Muñoz, V.2
-
63
-
-
0032502839
-
Contact order, transition state placement and the refolding rates of single-domain proteins
-
Plaxco K.W., Simons K.T., and 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
-
64
-
-
47249146415
-
Large-scale modulation of thremodynamic protein folding barriers linked to electrostatics
-
Halskau Ø., Perez-Jimenez R., Ibarra-Molero B., Underhaug J., Muñoz V., Martinez A., and Sanchez-Ruiz J.M. Large-scale modulation of thremodynamic protein folding barriers linked to electrostatics. Proc. Natl Acad. Sci. USA 105 (2008) 8625-8630
-
(2008)
Proc. Natl Acad. Sci. USA
, vol.105
, pp. 8625-8630
-
-
Halskau, Ø.1
Perez-Jimenez, R.2
Ibarra-Molero, B.3
Underhaug, J.4
Muñoz, V.5
Martinez, A.6
Sanchez-Ruiz, J.M.7
-
65
-
-
0030997077
-
Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi
-
Ostoa-Saloma P., Garza-Ramos G., Ramírez J., Becker I., Berzunza M., Landa A., et al. Cloning, expression, purification and characterization of triosephosphate isomerase from Trypanosoma cruzi. Eur. J. Biochem. 244 (1997) 700-705
-
(1997)
Eur. J. Biochem.
, vol.244
, pp. 700-705
-
-
Ostoa-Saloma, P.1
Garza-Ramos, G.2
Ramírez, J.3
Becker, I.4
Berzunza, M.5
Landa, A.6
-
66
-
-
0027401730
-
Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterization a dimer-interface mutant
-
Borchert T.V., Pratt K., Zeelen J.P., Callens M., Noble M.E., Opperdoes F.R., et al. Overexpression of trypanosomal triosephosphate isomerase in Escherichia coli and characterization a dimer-interface mutant. Eur. J. Biochem. 211 (1993) 703-710
-
(1993)
Eur. J. Biochem.
, vol.211
, pp. 703-710
-
-
Borchert, T.V.1
Pratt, K.2
Zeelen, J.P.3
Callens, M.4
Noble, M.E.5
Opperdoes, F.R.6
-
67
-
-
0028268915
-
Triosephosphate isomerase of Leishmania mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein
-
Kohl I., Callens M., Wierenga R.K., Opperdoes F.R., and Michles P.A. Triosephosphate isomerase of Leishmania mexicana. Cloning and characterization of the gene, overexpression in Escherichia coli and analysis of the protein. Eur. J. Biochem. 220 (1994) 331-338
-
(1994)
Eur. J. Biochem.
, vol.220
, pp. 331-338
-
-
Kohl, I.1
Callens, M.2
Wierenga, R.K.3
Opperdoes, F.R.4
Michles, P.A.5
|