-
1
-
-
0029160445
-
How the molten globule became
-
Ptitsyn, O. B. (1995) How the molten globule became, Trends Biochem. Sci. 20, 376-379.
-
(1995)
Trends Biochem. Sci
, vol.20
, pp. 376-379
-
-
Ptitsyn, O.B.1
-
2
-
-
0015920746
-
Stages in the mechanism of self-organization of protein molecules
-
Ptitsyn, O. B. (1973) Stages in the mechanism of self-organization of protein molecules, Dokl. Akad. Nauk SSSR 210, 1213-1215.
-
(1973)
Dokl. Akad. Nauk SSSR
, vol.210
, pp. 1213-1215
-
-
Ptitsyn, O.B.1
-
3
-
-
0015766411
-
Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions
-
Wong, K. P., and Tanford, C. (1973) Denaturation of bovine carbonic anhydrase B by guanidine hydrochloride. A process involving separable sequential conformational transitions, J. Biol. Chem. 248, 8518-8523.
-
(1973)
J. Biol. Chem
, vol.248
, pp. 8518-8523
-
-
Wong, K.P.1
Tanford, C.2
-
4
-
-
0019890466
-
Alpha-Lactalbumin: Compact state with fluctuating tertiary structure?
-
Dolgikh, D. A., Gilmanshin, R. I., Brazhnikov, E. V., Bychkova, V. E., Semisotnov, G. V., Venyaminov, S., and Ptitsyn, O. B. (1981) Alpha-Lactalbumin: compact state with fluctuating tertiary structure? FEBS Lett. 136, 311-315.
-
(1981)
FEBS Lett
, vol.136
, pp. 311-315
-
-
Dolgikh, D.A.1
Gilmanshin, R.I.2
Brazhnikov, E.V.3
Bychkova, V.E.4
Semisotnov, G.V.5
Venyaminov, S.6
Ptitsyn, O.B.7
-
5
-
-
0016211812
-
Acid denaturation of bovine carbonic anhydrase B
-
Wong, K. P., and Hamlin, L. M. (1974) Acid denaturation of bovine carbonic anhydrase B, Biochemistry 13, 2678-2683.
-
(1974)
Biochemistry
, vol.13
, pp. 2678-2683
-
-
Wong, K.P.1
Hamlin, L.M.2
-
6
-
-
0026427243
-
Structures in colloidal physical chemistry
-
Prost, J., and Rondelez, F. (1991) Structures in colloidal physical chemistry, Nature 350, 11-23.
-
(1991)
Nature
, vol.350
, pp. 11-23
-
-
Prost, J.1
Rondelez, F.2
-
7
-
-
0021753299
-
Molten-globule' state accumulates in carbonic anhydrase folding
-
Dolgikh, D. A., Kolomiets, A. P., Bolotina, I. A., and Ptitsyn, O. B. (1984) 'Molten-globule' state accumulates in carbonic anhydrase folding, FEBS Lett. 165, 88-92.
-
(1984)
FEBS Lett
, vol.165
, pp. 88-92
-
-
Dolgikh, D.A.1
Kolomiets, A.P.2
Bolotina, I.A.3
Ptitsyn, O.B.4
-
8
-
-
0021114569
-
Molten-globule state': A compact form of globular proteins with mobile side-chains
-
Ohgushi, M., and Wada, A. (1983) 'Molten-globule state': a compact form of globular proteins with mobile side-chains, FEBS Lett. 164, 21-24.
-
(1983)
FEBS Lett
, vol.164
, pp. 21-24
-
-
Ohgushi, M.1
Wada, A.2
-
9
-
-
0028466243
-
Protein folding. Solid evidence for molten globules
-
Dobson, C. M. (1994) Protein folding. Solid evidence for molten globules, Curr. Biol. 4, 636-640.
-
(1994)
Curr. Biol
, vol.4
, pp. 636-640
-
-
Dobson, C.M.1
-
10
-
-
0029202647
-
What is the molten globule?
-
Ewbank, J. J., Creighton, T. E., Hayer-Hartl, M. K., and Ulrich, Hartl, F. (1995) What is the molten globule? Nat. Struct. Biol. 2, 10-11.
-
(1995)
Nat. Struct. Biol
, vol.2
, pp. 10-11
-
-
Ewbank, J.J.1
Creighton, T.E.2
Hayer-Hartl, M.K.3
-
11
-
-
0024417964
-
The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure
-
Kuwajima, K. (1989) The molten globule state as a clue for understanding the folding and cooperativity of globular-protein structure, Proteins 6, 87-103.
-
(1989)
Proteins
, vol.6
, pp. 87-103
-
-
Kuwajima, K.1
-
12
-
-
0032539684
-
Is the molten globule a third phase of proteins?
-
Pande, V. S., and Rokhsar, D. S. (1998) Is the molten globule a third phase of proteins? Proc. Natl. Acad. Sci. U.S.A. 95, 1490-1494.
-
(1998)
Proc. Natl. Acad. Sci. U.S.A
, vol.95
, pp. 1490-1494
-
-
Pande, V.S.1
Rokhsar, D.S.2
-
13
-
-
0030066904
-
Mapping the structure of a non-native state of staphylococcal nuclease
-
Ermacora, M. R., Ledman, D. W., and Fox, R. O. (1996) Mapping the structure of a non-native state of staphylococcal nuclease, Nat. Struct. Biol. 3, 59-66.
-
(1996)
Nat. Struct. Biol
, vol.3
, pp. 59-66
-
-
Ermacora, M.R.1
Ledman, D.W.2
Fox, R.O.3
-
14
-
-
0035919635
-
Persistence of native-like topology in a denatured protein in 8 M urea
-
Shortle, D., and Ackerman, M. S. (2001) Persistence of native-like topology in a denatured protein in 8 M urea, Science 293, 487-489.
-
(2001)
Science
, vol.293
, pp. 487-489
-
-
Shortle, D.1
Ackerman, M.S.2
-
16
-
-
0033970156
-
An in vitro peptide folding model suggests the presence of the molten globule state during nascent peptide folding
-
Zhou, B., Tian, K., and Jing, G. (2000) An in vitro peptide folding model suggests the presence of the molten globule state during nascent peptide folding, Protein Eng. 13, 35-39.
-
(2000)
Protein Eng
, vol.13
, pp. 35-39
-
-
Zhou, B.1
Tian, K.2
Jing, G.3
-
17
-
-
0028859841
-
Folding intermediates are involved in genetic diseases?
-
Bychkova, V. E., and Ptitsyn, O. B. (1995) Folding intermediates are involved in genetic diseases? FEBS Lett. 359, 6-8.
-
(1995)
FEBS Lett
, vol.359
, pp. 6-8
-
-
Bychkova, V.E.1
Ptitsyn, O.B.2
-
18
-
-
0026781952
-
Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
-
Denning, G. M., Anderson, M. P., Amara, J. F., Marshall, J., Smith, A. E., and Welsh, M. J. (1992) Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive, Nature 358, 761-764.
-
(1992)
Nature
, vol.358
, pp. 761-764
-
-
Denning, G.M.1
Anderson, M.P.2
Amara, J.F.3
Marshall, J.4
Smith, A.E.5
Welsh, M.J.6
-
19
-
-
0026649584
-
The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide
-
Thomas, P. J., Shenbagamurthi, P., Sondek, J., Hullihen, J. M., and Pedersen, P. L. (1992) The cystic fibrosis transmembrane conductance regulator. Effects of the most common cystic fibrosis-causing mutation on the secondary structure and stability of a synthetic peptide, J. Biol. Chem. 267, 5727-5730.
-
(1992)
J. Biol. Chem
, vol.267
, pp. 5727-5730
-
-
Thomas, P.J.1
Shenbagamurthi, P.2
Sondek, J.3
Hullihen, J.M.4
Pedersen, P.L.5
-
20
-
-
0027488993
-
The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
-
Yang, Y., Janich, S., Cohn, J. A., and Wilson, J. M. (1993) The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment, Proc. Natl. Acad. Sci. U.S.A. 90, 9480-9484.
-
(1993)
Proc. Natl. Acad. Sci. U.S.A
, vol.90
, pp. 9480-9484
-
-
Yang, Y.1
Janich, S.2
Cohn, J.A.3
Wilson, J.M.4
-
21
-
-
0026561138
-
Intracellular protein trafficking defects in human disease
-
Amara, J. F., Cheng, S. H., and Smith, A. E. (1992) Intracellular protein trafficking defects in human disease, Trends Cell Biol. 2, 145-149.
-
(1992)
Trends Cell Biol
, vol.2
, pp. 145-149
-
-
Amara, J.F.1
Cheng, S.H.2
Smith, A.E.3
-
22
-
-
0026755363
-
The mechanism of Z alpha 1-antitrypsin accumulation in the liver
-
Lomas, D. A., Evans, D. L., Finch, J. T., and Carrell, R. W. (1992) The mechanism of Z alpha 1-antitrypsin accumulation in the liver, Nature 357, 605-607.
-
(1992)
Nature
, vol.357
, pp. 605-607
-
-
Lomas, D.A.1
Evans, D.L.2
Finch, J.T.3
Carrell, R.W.4
-
23
-
-
0026625802
-
Protein transport. Z and the insoluble answer
-
Sifers, R. N. (1992) Protein transport. Z and the insoluble answer, Nature 357, 541-542.
-
(1992)
Nature
, vol.357
, pp. 541-542
-
-
Sifers, R.N.1
-
24
-
-
0029910017
-
Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin
-
Rajaraman, K., Raman, B., and Rao, C. M. (1996) Molten-globule state of carbonic anhydrase binds to the chaperone-like alpha-crystallin, J. Biol. Chem. 271, 27595-27600.
-
(1996)
J. Biol. Chem
, vol.271
, pp. 27595-27600
-
-
Rajaraman, K.1
Raman, B.2
Rao, C.M.3
-
25
-
-
0032540350
-
Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme
-
Rawat, U., and Rao, M. (1998) Interactions of chaperone alpha-crystallin with the molten globule state of xylose reductase. Implications for reconstitution of the active enzyme, J. Biol. Chem. 273, 9415-9423.
-
(1998)
J. Biol. Chem
, vol.273
, pp. 9415-9423
-
-
Rawat, U.1
Rao, M.2
-
26
-
-
0026416043
-
Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
-
Martin, J., Langer, T., Boteva, R., Schramel, A., Horwich, A. L., and Hartl, F. U. (1991) Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate, Nature 352, 36-42.
-
(1991)
Nature
, vol.352
, pp. 36-42
-
-
Martin, J.1
Langer, T.2
Boteva, R.3
Schramel, A.4
Horwich, A.L.5
Hartl, F.U.6
-
27
-
-
0028670568
-
Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry
-
Robinson, C. V., Gross, M., Eyles, S. J., Ewbank, J. J., Mayhew, M., Hartl, F. U., Dobson, C. M., and Radford, S. E. (1994) Conformation of GroEL-bound alpha-lactalbumin probed by mass spectrometry, Nature 372, 646-651.
-
(1994)
Nature
, vol.372
, pp. 646-651
-
-
Robinson, C.V.1
Gross, M.2
Eyles, S.J.3
Ewbank, J.J.4
Mayhew, M.5
Hartl, F.U.6
Dobson, C.M.7
Radford, S.E.8
-
28
-
-
0035874472
-
Molten-globule structure and membrane binding of the N-terminal protease-resistant domain (63-193) of the steroidogenic acute regulatory protein (StAR)
-
Song, M., Shao, H., Mujeeb, A., James, T. L., and Miller, W. L. (2001) Molten-globule structure and membrane binding of the N-terminal protease-resistant domain (63-193) of the steroidogenic acute regulatory protein (StAR), Biochem. J. 356, 151-158.
-
(2001)
Biochem. J
, vol.356
, pp. 151-158
-
-
Song, M.1
Shao, H.2
Mujeeb, A.3
James, T.L.4
Miller, W.L.5
-
29
-
-
0033532355
-
Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation
-
Ren, J., Kachel, K., Kim, H., Malenbaum, S. E., Collier, R. J., and London, E. (1999) Interaction of diphtheria toxin T domain with molten globule-like proteins and its implications for translocation, Science 284, 955-957.
-
(1999)
Science
, vol.284
, pp. 955-957
-
-
Ren, J.1
Kachel, K.2
Kim, H.3
Malenbaum, S.E.4
Collier, R.J.5
London, E.6
-
30
-
-
0025932041
-
A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A
-
van der Goot, F. G., Gonzalez-Manas, J. M., Lakey, J. H., and Pattus, F. (1991) A 'molten-globule' membrane-insertion intermediate of the pore-forming domain of colicin A, Nature 354, 408-410.
-
(1991)
Nature
, vol.354
, pp. 408-410
-
-
van der Goot, F.G.1
Gonzalez-Manas, J.M.2
Lakey, J.H.3
Pattus, F.4
-
31
-
-
0023710642
-
The 'molten globule' state is involved in the translocation of proteins across membranes?
-
Bychkova, V. E., Pain, R. H., and Ptitsyn, O. B. (1988) The 'molten globule' state is involved in the translocation of proteins across membranes? FEBS Lett. 238, 231-234.
-
(1988)
FEBS Lett
, vol.238
, pp. 231-234
-
-
Bychkova, V.E.1
Pain, R.H.2
Ptitsyn, O.B.3
-
32
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings, P. A., and Wright, P. E. (1993) Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin, Science 262, 892-896.
-
(1993)
Science
, vol.262
, pp. 892-896
-
-
Jennings, P.A.1
Wright, P.E.2
-
33
-
-
0025186451
-
Structural characterization of a partly folded apomyoglobin intermediate
-
Hughson, F. M., Wright, P. E., and Baldwin, R. L. (1990) Structural characterization of a partly folded apomyoglobin intermediate, Science 249, 1544-1548.
-
(1990)
Science
, vol.249
, pp. 1544-1548
-
-
Hughson, F.M.1
Wright, P.E.2
Baldwin, R.L.3
-
34
-
-
0025203243
-
Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR
-
Jeng, M. F., Englander, S. W., Elove, G. A., Wand, A. J., and Roder, H. (1990) Structural description of acid-denatured cytochrome c by hydrogen exchange and 2D NMR, Biochemistry 29, 10433-10437.
-
(1990)
Biochemistry
, vol.29
, pp. 10433-10437
-
-
Jeng, M.F.1
Englander, S.W.2
Elove, G.A.3
Wand, A.J.4
Roder, H.5
-
35
-
-
0034685617
-
Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin
-
Mizuguchi, M., Masaki, K., Demura, M., and Nitta, K. (2000) Local and long-range interactions in the molten globule state: A study of chimeric proteins of bovine and human alpha-lactalbumin, J. Mol. Biol. 298, 985-995.
-
(2000)
J. Mol. Biol
, vol.298
, pp. 985-995
-
-
Mizuguchi, M.1
Masaki, K.2
Demura, M.3
Nitta, K.4
-
36
-
-
0027787520
-
Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule
-
Ogasahara, K., Matsushita, E., and Yutani, K. (1993) Further examination of the intermediate state in the denaturation of the tryptophan synthase alpha subunit. Evidence that the equilibrium denaturation intermediate is a molten globule, J. Mol. Biol. 234, 1197-1206.
-
(1993)
J. Mol. Biol
, vol.234
, pp. 1197-1206
-
-
Ogasahara, K.1
Matsushita, E.2
Yutani, K.3
-
37
-
-
0031963564
-
Is the molten globule a third thermodynamic state of protein? The example of alpha-lactalbumin
-
Pfeil, W. (1998) Is the molten globule a third thermodynamic state of protein? The example of alpha-lactalbumin, Proteins 30, 43-48.
-
(1998)
Proteins
, vol.30
, pp. 43-48
-
-
Pfeil, W.1
-
38
-
-
0022445353
-
Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin
-
Pfeil, W., Bychkova, V. E., and Ptitsyn, O. B. (1986) Physical nature of the phase transition in globular proteins. Calorimetric study of human alpha-lactalbumin, FEBS Lett. 198, 287-291.
-
(1986)
FEBS Lett
, vol.198
, pp. 287-291
-
-
Pfeil, W.1
Bychkova, V.E.2
Ptitsyn, O.B.3
-
39
-
-
0026679847
-
Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry
-
Yutani, K., Ogasahara, K., and Kuwajima, K. (1992) Absence of the thermal transition in apo-alpha-lactalbumin in the molten globule state. A study by differential scanning microcalorimetry, J. Mol. Biol. 228, 347-350.
-
(1992)
J. Mol. Biol
, vol.228
, pp. 347-350
-
-
Yutani, K.1
Ogasahara, K.2
Kuwajima, K.3
-
40
-
-
0032536105
-
Native tertiary structure in an A-state
-
Marmorino, J. L., Lehti, M., and Pielak, G. J. (1998) Native tertiary structure in an A-state, J. Mol. Biol. 275, 379-388.
-
(1998)
J. Mol. Biol
, vol.275
, pp. 379-388
-
-
Marmorino, J.L.1
Lehti, M.2
Pielak, G.J.3
-
41
-
-
0032777726
-
Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's
-
Sheshadri, S., Lingaraju, G. M., and Varadarajan, R. (1999) Denaturant mediated unfolding of both native and molten globule states of maltose binding protein are accompanied by large deltaCp's, Protein Sci. 8, 1689-1695.
-
(1999)
Protein Sci
, vol.8
, pp. 1689-1695
-
-
Sheshadri, S.1
Lingaraju, G.M.2
Varadarajan, R.3
-
42
-
-
33846011885
-
Thermodynamic effects of proline introduction on protein stability
-
Prajapati, R. S., Das, M., Sreeramulu, S., Sirajuddin, M., Srinivasan, S., Krishnamurthy, V., Ranjani, R., Ramakrishnan, C., and Varadarajan, R. (2006) Thermodynamic effects of proline introduction on protein stability, Proteins 66, 480-491.
-
(2006)
Proteins
, vol.66
, pp. 480-491
-
-
Prajapati, R.S.1
Das, M.2
Sreeramulu, S.3
Sirajuddin, M.4
Srinivasan, S.5
Krishnamurthy, V.6
Ranjani, R.7
Ramakrishnan, C.8
Varadarajan, R.9
-
43
-
-
1542365360
-
X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity
-
Magnusson, U., Salopek-Sondi, B., Luck, L. A., and Mowbray, S. L. (2004) X-ray structures of the leucine-binding protein illustrate conformational changes and the basis of ligand specificity, J. Biol. Chem. 279, 8747-8752.
-
(2004)
J. Biol. Chem
, vol.279
, pp. 8747-8752
-
-
Magnusson, U.1
Salopek-Sondi, B.2
Luck, L.A.3
Mowbray, S.L.4
-
44
-
-
33845575030
-
Contribution of cation-pi interactions to protein stability
-
Prajapati, R. S., Sirajuddin, M., Durani, V., Sreeramulu, S., and Varadarajan, R. (2006) Contribution of cation-pi interactions to protein stability, Biochemistry 45, 15000-15010.
-
(2006)
Biochemistry
, vol.45
, pp. 15000-15010
-
-
Prajapati, R.S.1
Sirajuddin, M.2
Durani, V.3
Sreeramulu, S.4
Varadarajan, R.5
-
45
-
-
0030978479
-
Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein
-
Ganesh, C., Shah, A. N., Swaminathan, C. P., Surolia, A., and Varadarajan, R. (1997) Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein, Biochemistry 36, 5020-5028.
-
(1997)
Biochemistry
, vol.36
, pp. 5020-5028
-
-
Ganesh, C.1
Shah, A.N.2
Swaminathan, C.P.3
Surolia, A.4
Varadarajan, R.5
-
46
-
-
0028871804
-
How to measure and predict the molar absorption coefficient of a protein
-
Pace, C. N., Vajdos, F., Fee, L., Grimsley, G., and Gray, T. (1995) How to measure and predict the molar absorption coefficient of a protein, Protein Sci. 4, 2411-2423.
-
(1995)
Protein Sci
, vol.4
, pp. 2411-2423
-
-
Pace, C.N.1
Vajdos, F.2
Fee, L.3
Grimsley, G.4
Gray, T.5
-
47
-
-
33846582419
-
Energetics of peptide recognition by the second PDZ domain of human protein tyrosine phosphatase 1E
-
Milev, S., Bjelic, S., Georgiev, O., and Jelesarov, I. (2007) Energetics of peptide recognition by the second PDZ domain of human protein tyrosine phosphatase 1E, Biochemistry 46, 1064-1078.
-
(2007)
Biochemistry
, vol.46
, pp. 1064-1078
-
-
Milev, S.1
Bjelic, S.2
Georgiev, O.3
Jelesarov, I.4
-
48
-
-
0025293251
-
Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry
-
Connelly, P. R., Varadarajan, R., Sturtevant, J. M., and Richards, F. M. (1990) Thermodynamics of protein-peptide interactions in the ribonuclease S system studied by titration calorimetry, Biochemistry 29, 6108-6114.
-
(1990)
Biochemistry
, vol.29
, pp. 6108-6114
-
-
Connelly, P.R.1
Varadarajan, R.2
Sturtevant, J.M.3
Richards, F.M.4
-
49
-
-
0031571605
-
Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor
-
Quiocho, F. A., Spurlino, J. C., and Rodseth, L. E. (1997) Extensive features of tight oligosaccharide binding revealed in high-resolution structures of the maltodextrin transport/chemosensory receptor, Structure 5, 997-1015.
-
(1997)
Structure
, vol.5
, pp. 997-1015
-
-
Quiocho, F.A.1
Spurlino, J.C.2
Rodseth, L.E.3
-
50
-
-
0026493924
-
Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis
-
Sharff, A. J., Rodseth, L. E., Spurlino, J. C., and Quiocho, F. A. (1992) Crystallographic evidence of a large ligand-induced hinge-twist motion between the two domains of the maltodextrin binding protein involved in active transport and chemotaxis, Biochemistry 31, 10657-10663.
-
(1992)
Biochemistry
, vol.31
, pp. 10657-10663
-
-
Sharff, A.J.1
Rodseth, L.E.2
Spurlino, J.C.3
Quiocho, F.A.4
-
51
-
-
17844398488
-
Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: Trajectory and dynamics of the interdomain rotation and ligand specificity
-
Trakhanov, S., Vyas, N. K., Luecke, H., Kristensen, D. M., Ma, J., and Quiocho, F. A. (2005) Ligand-free and -bound structures of the binding protein (LivJ) of the Escherichia coli ABC leucine/isoleucine/valine transport system: trajectory and dynamics of the interdomain rotation and ligand specificity, Biochemistry 44, 6597-6608.
-
(2005)
Biochemistry
, vol.44
, pp. 6597-6608
-
-
Trakhanov, S.1
Vyas, N.K.2
Luecke, H.3
Kristensen, D.M.4
Ma, J.5
Quiocho, F.A.6
-
52
-
-
0028820703
-
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
-
Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4, 2138-2148.
-
(1995)
Protein Sci
, vol.4
, pp. 2138-2148
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
53
-
-
0004014257
-
-
Computer Program, Department of Biochemistry and Molecular Biology, University College, London, England
-
Hubbard, S. J., and Thronton, J. M. (1993) NACCESS, Computer Program, Department of Biochemistry and Molecular Biology, University College, London, England.
-
(1993)
NACCESS
-
-
Hubbard, S.J.1
Thronton, J.M.2
-
54
-
-
0021100265
-
Thermodynamics of the binding of L-arabinose and of D-galactose to the L-arabinose-binding protein of Escherichia coli
-
Fukada, H., Sturtevant, J. M., and Quiocho, F. A. (1983) Thermodynamics of the binding of L-arabinose and of D-galactose to the L-arabinose-binding protein of Escherichia coli, J. Biol. Chem. 258, 13193-13198.
-
(1983)
J. Biol. Chem
, vol.258
, pp. 13193-13198
-
-
Fukada, H.1
Sturtevant, J.M.2
Quiocho, F.A.3
-
55
-
-
2942740914
-
Thermodynamic characterization of monomelic and dimeric forms of CcdB (controller of cell division or death B protein)
-
Bajaj, K., Chakshusmathi, G., Bachhawat-Sikder, K., Surolia, A., and Varadarajan, R. (2004) Thermodynamic characterization of monomelic and dimeric forms of CcdB (controller of cell division or death B protein), Biochem. J. 380, 409-417.
-
(2004)
Biochem. J
, vol.380
, pp. 409-417
-
-
Bajaj, K.1
Chakshusmathi, G.2
Bachhawat-Sikder, K.3
Surolia, A.4
Varadarajan, R.5
-
56
-
-
0023150662
-
Electrophysiologic and clinical effects of intravenous and oral encainide in patients with Wolff-Parkinson-White syndrome and paroxysmal atrial fibrillation
-
Chimienti, M., Moizi, M., Salerno, J. A., Klersy, C., Guasti, L., Previtali, M., Marangoni, E., Montemartini, C., and Bobba, P. (1987) Electrophysiologic and clinical effects of intravenous and oral encainide in patients with Wolff-Parkinson-White syndrome and paroxysmal atrial fibrillation, Eur. Heart J. 8, 282-290.
-
(1987)
Eur. Heart J
, vol.8
, pp. 282-290
-
-
Chimienti, M.1
Moizi, M.2
Salerno, J.A.3
Klersy, C.4
Guasti, L.5
Previtali, M.6
Marangoni, E.7
Montemartini, C.8
Bobba, P.9
-
57
-
-
0022370492
-
-
Dolgikh, D. A., Abaturov, L. V., Bolotina, I. A., Brazhnikov, E. V., Bychkova, V. E., Gilmanshin, R. I., Lebedev, Yu, O., Semisotnov, G. V., Tiktopulo, E. I., Ptitsyn, O. B., et al. (1985) Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin, Eur. Biophys. J. 13, 109-121.
-
Dolgikh, D. A., Abaturov, L. V., Bolotina, I. A., Brazhnikov, E. V., Bychkova, V. E., Gilmanshin, R. I., Lebedev, Yu, O., Semisotnov, G. V., Tiktopulo, E. I., Ptitsyn, O. B., et al. (1985) Compact state of a protein molecule with pronounced small-scale mobility: bovine alpha-lactalbumin, Eur. Biophys. J. 13, 109-121.
-
-
-
-
58
-
-
0017399699
-
A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism
-
Kuwajima, K. (1977) A folding model of alpha-lactalbumin deduced from the three-state denaturation mechanism, J. Mol. Biol. 114, 241-258.
-
(1977)
J. Mol. Biol
, vol.114
, pp. 241-258
-
-
Kuwajima, K.1
-
59
-
-
0029124248
-
Molten globule and protein folding
-
Ptitsyn, O. B. (1995) Molten globule and protein folding, Adv. Protein Chem. 47, 83-229.
-
(1995)
Adv. Protein Chem
, vol.47
, pp. 83-229
-
-
Ptitsyn, O.B.1
-
60
-
-
0026096545
-
Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe
-
Semisotnov, G. V., Rodionova, N. A., Razgulyaev, O. I., Uversky, V. N., Gripas, A. F., and Gilmanshin, R. I. (1991) Study of the "molten globule" intermediate state in protein folding by a hydrophobic fluorescent probe, Biopolymers 31, 119-128.
-
(1991)
Biopolymers
, vol.31
, pp. 119-128
-
-
Semisotnov, G.V.1
Rodionova, N.A.2
Razgulyaev, O.I.3
Uversky, V.N.4
Gripas, A.F.5
Gilmanshin, R.I.6
-
61
-
-
0034646563
-
Energetic basis of structural stability in the molten globule state: Alpha-lactalbumin
-
Griko, Y. V. (2000) Energetic basis of structural stability in the molten globule state: alpha-lactalbumin, J. Mol. Biol. 297, 1259-1268.
-
(2000)
J. Mol. Biol
, vol.297
, pp. 1259-1268
-
-
Griko, Y.V.1
-
62
-
-
0026330844
-
Calorimetric determination of the energetics of the molten globule intermediate in protein folding: Apo-alpha-lactalbumin
-
Xie, D., Bhakuni, V., and Freire, E. (1991) Calorimetric determination of the energetics of the molten globule intermediate in protein folding: apo-alpha-lactalbumin, Biochemistry 30, 10673-10678.
-
(1991)
Biochemistry
, vol.30
, pp. 10673-10678
-
-
Xie, D.1
Bhakuni, V.2
Freire, E.3
-
63
-
-
0033060057
-
Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein
-
Koshiba, T., Hayashi, T., Miwako, I., Kumagai, I., Ikura, T., Kawano, K., Nitta, K., and Kuwajima, K. (1999) Expression of a synthetic gene encoding canine milk lysozyme in Escherichia coli and characterization of the expressed protein, Protein Eng. 12, 429-435.
-
(1999)
Protein Eng
, vol.12
, pp. 429-435
-
-
Koshiba, T.1
Hayashi, T.2
Miwako, I.3
Kumagai, I.4
Ikura, T.5
Kawano, K.6
Nitta, K.7
Kuwajima, K.8
-
64
-
-
0029157132
-
The unfolding thermodynamics of c-type lysozymes: A calorimetric study of the heat denaturation of equine lysozyme
-
Griko, Y. V., Freire, E., Privalov, G., van Dael, H., and Privalov, P. L. (1995) The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme, J. Mol. Biol. 252, 447-459.
-
(1995)
J. Mol. Biol
, vol.252
, pp. 447-459
-
-
Griko, Y.V.1
Freire, E.2
Privalov, G.3
van Dael, H.4
Privalov, P.L.5
-
65
-
-
0028206335
-
Thermodynamics of staphylococcal nuclease denaturation. II. The A-state
-
Carra, J. H., Anderson, E. A., and Privalov, P. L. (1994) Thermodynamics of staphylococcal nuclease denaturation. II. The A-state, Protein Sci. 3, 952-959.
-
(1994)
Protein Sci
, vol.3
, pp. 952-959
-
-
Carra, J.H.1
Anderson, E.A.2
Privalov, P.L.3
-
66
-
-
0037452560
-
Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants
-
Qureshi, S. H., Moza, B., Yadav, S., and Ahmad, F. (2003) Conformational and thermodynamic characterization of the molten globule state occurring during unfolding of cytochromes-c by weak salt denaturants, Biochemistry 42, 1684-1695.
-
(2003)
Biochemistry
, vol.42
, pp. 1684-1695
-
-
Qureshi, S.H.1
Moza, B.2
Yadav, S.3
Ahmad, F.4
-
67
-
-
0028346251
-
Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride
-
Hagihara, Y., Tan, Y., and Goto, Y. (1994) Comparison of the conformational stability of the molten globule and native states of horse cytochrome c. Effects of acetylation, heat, urea and guanidine-hydrochloride, J. Mol. Biol. 237, 336-348.
-
(1994)
J. Mol. Biol
, vol.237
, pp. 336-348
-
-
Hagihara, Y.1
Tan, Y.2
Goto, Y.3
-
68
-
-
0024199422
-
Stability of protein structure and hydrophobic interaction
-
Privalov, P. L., and Gill, S. J. (1988) Stability of protein structure and hydrophobic interaction, Adv. Protein Chem. 39, 191-234.
-
(1988)
Adv. Protein Chem
, vol.39
, pp. 191-234
-
-
Privalov, P.L.1
Gill, S.J.2
-
69
-
-
0026344361
-
Solid model compounds and the thermodynamics of protein unfolding
-
Murphy, K. P., and Gill, S. J. (1991) Solid model compounds and the thermodynamics of protein unfolding, J. Mol. Biol. 222, 699-709.
-
(1991)
J. Mol. Biol
, vol.222
, pp. 699-709
-
-
Murphy, K.P.1
Gill, S.J.2
-
70
-
-
0025287103
-
Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: Protein unfolding effects
-
Privalov, P. L., and Makhatadze, G. I. (1990) Heat capacity of proteins. II. Partial molar heat capacity of the unfolded polypeptide chain of proteins: protein unfolding effects, J. Mol. Biol. 213, 385-391.
-
(1990)
J. Mol. Biol
, vol.213
, pp. 385-391
-
-
Privalov, P.L.1
Makhatadze, G.I.2
-
71
-
-
0028143596
-
Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
-
Hamada, D., Kidokoro, S., Fukada, H., Takahashi, K., and Goto, Y. (1994) Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry, Proc. Natl. Acad. Sci. U.S.A. 91, 10325-10329.
-
(1994)
Proc. Natl. Acad. Sci. U.S.A
, vol.91
, pp. 10325-10329
-
-
Hamada, D.1
Kidokoro, S.2
Fukada, H.3
Takahashi, K.4
Goto, Y.5
-
72
-
-
11144277877
-
Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry
-
Nakamura, S., and Kidokoro, S. (2005) Direct observation of the enthalpy change accompanying the native to molten-globule transition of cytochrome c by using isothermal acid-titration calorimetry, Biophys. Chem. 113, 161-168.
-
(2005)
Biophys. Chem
, vol.113
, pp. 161-168
-
-
Nakamura, S.1
Kidokoro, S.2
-
73
-
-
0028329347
-
Thermodynamic puzzle of apomyoglobin unfolding
-
Griko, Y. V., and Privalov, P. L. (1994) Thermodynamic puzzle of apomyoglobin unfolding, J. Mol. Biol. 235, 1318-1325.
-
(1994)
J. Mol. Biol
, vol.235
, pp. 1318-1325
-
-
Griko, Y.V.1
Privalov, P.L.2
-
74
-
-
0032479440
-
A specific hydrophobic core in the alpha-lactalbumin molten globule
-
Wu, L. C., and Kim, P. S. (1998) A specific hydrophobic core in the alpha-lactalbumin molten globule, J. Mol. Biol. 280, 175-182.
-
(1998)
J. Mol. Biol
, vol.280
, pp. 175-182
-
-
Wu, L.C.1
Kim, P.S.2
-
75
-
-
0029653877
-
Does the molten globule have a native-like tertiary fold?
-
Peng, Z. Y., Wu, L. C., Schulman, B. A., and Kim, P. S. (1995) Does the molten globule have a native-like tertiary fold? Philos. Trans. R. Soc. London, Ser. B 348, 43-47.
-
(1995)
Philos. Trans. R. Soc. London, Ser. B
, vol.348
, pp. 43-47
-
-
Peng, Z.Y.1
Wu, L.C.2
Schulman, B.A.3
Kim, P.S.4
-
76
-
-
33645097323
-
Mapping the distribution of conformational information throughout a protein sequence
-
Gebhard, L. G., Risso, V. A., Santos, J., Ferreyra, R. G., Noguera, M. E., and Ermacora, M. R. (2006) Mapping the distribution of conformational information throughout a protein sequence, J. Mol. Biol. 358, 280-288.
-
(2006)
J. Mol. Biol
, vol.358
, pp. 280-288
-
-
Gebhard, L.G.1
Risso, V.A.2
Santos, J.3
Ferreyra, R.G.4
Noguera, M.E.5
Ermacora, M.R.6
-
77
-
-
0025754301
-
The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis
-
Spurlino, J. C., Lu, G. Y., and Quiocho, F. A. (1991) The 2.3-A resolution structure of the maltose- or maltodextrin-binding protein, a primary receptor of bacterial active transport and chemotaxis, J. Biol. Chem. 266, 5202-5219.
-
(1991)
J. Biol. Chem
, vol.266
, pp. 5202-5219
-
-
Spurlino, J.C.1
Lu, G.Y.2
Quiocho, F.A.3
-
78
-
-
0346494941
-
SCOP database in 2004: Refinements integrate structure and sequence family data
-
Andreeva, A., Howorth, D., Brenner, S. E., Hubbard, T. J., Chothia, C., and Murzin, A. G. (2004) SCOP database in 2004: refinements integrate structure and sequence family data, Nucleic Acids Res. 32, D226-D229.
-
(2004)
Nucleic Acids Res
, vol.32
-
-
Andreeva, A.1
Howorth, D.2
Brenner, S.E.3
Hubbard, T.J.4
Chothia, C.5
Murzin, A.G.6
-
79
-
-
0028961335
-
SCOP: A structural classification of proteins database for the investigation of sequences and structures
-
Murzin, A. G., Brenner, S. E., Hubbard, T., and Chothia, C. (1995) SCOP: a structural classification of proteins database for the investigation of sequences and structures, J. Mol. Biol. 247, 536-540.
-
(1995)
J. Mol. Biol
, vol.247
, pp. 536-540
-
-
Murzin, A.G.1
Brenner, S.E.2
Hubbard, T.3
Chothia, C.4
-
80
-
-
1642348275
-
Effect of signal peptide on the stability and folding kinetics of maltose binding protein
-
Beena, K., Udgaonkar, J. B., and Varadarajan, R. (2004) Effect of signal peptide on the stability and folding kinetics of maltose binding protein, Biochemistry 43, 3608-3619.
-
(2004)
Biochemistry
, vol.43
, pp. 3608-3619
-
-
Beena, K.1
Udgaonkar, J.B.2
Varadarajan, R.3
|