-
1
-
-
0025953443
-
Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis
-
Auld, D. S. & Pielak, G. J. (1991). Constraints on amino acid substitutions in the N-terminal helix of cytochrome c explored by random mutagenesis. Biochemistry, 30, 8684-8690.
-
(1991)
Biochemistry
, vol.30
, pp. 8684-8690
-
-
Auld, D.S.1
Pielak, G.J.2
-
2
-
-
0030347877
-
On-pathway versus off-pathway folding intermediates
-
Baldwin, R. L. (1996). On-pathway versus off-pathway folding intermediates. Fold. Des. 1, R1-R8.
-
(1996)
Fold. Des.
, vol.1
-
-
Baldwin, R.L.1
-
4
-
-
0023442217
-
Protein stability curves
-
Becktel, W. J. & Schellman, J. A. (1987). Protein stability curves. Biopolymers, 26, 1859-1877.
-
(1987)
Biopolymers
, vol.26
, pp. 1859-1877
-
-
Becktel, W.J.1
Schellman, J.A.2
-
5
-
-
0026608669
-
Oxidation state-dependent conformational changes in cytochrome c
-
Berghuis, A. M. & Brayer, G. D. (1992). Oxidation state-dependent conformational changes in cytochrome c. J. Mol. Biol. 223, 959-976.
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 959-976
-
-
Berghuis, A.M.1
Brayer, G.D.2
-
6
-
-
0027000943
-
Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state
-
Betz, S. F. & Pielak, G. J. (1992). Introduction of a disulfide bond into cytochrome c stabilizes a compact denatured state. Biochemistry, 31, 12337-12344.
-
(1992)
Biochemistry
, vol.31
, pp. 12337-12344
-
-
Betz, S.F.1
Pielak, G.J.2
-
7
-
-
0000837519
-
Structural studies of eukaryotic cytochromes c
-
(Scott, R. A. & Mauk, A. G., eds), University Science Books, Sausalito
-
Brayer, G. D. & Murphy, M. E. P. (1996). Structural studies of eukaryotic cytochromes c. In Cytochrome c: A Multidisciplinary Approach. (Scott, R. A. & Mauk, A. G., eds), pp. 103-166, University Science Books, Sausalito.
-
(1996)
Cytochrome C: A Multidisciplinary Approach
, pp. 103-166
-
-
Brayer, G.D.1
Murphy, M.E.P.2
-
8
-
-
0027935843
-
Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature
-
Cohen, D. S. & Pielak, G. J. (1994). Stability of yeast iso-1-ferricytochrome c as a function of pH and temperature. Protein Sci. 3, 1253-1260.
-
(1994)
Protein Sci.
, vol.3
, pp. 1253-1260
-
-
Cohen, D.S.1
Pielak, G.J.2
-
9
-
-
0028847055
-
Entropic stabilization of cytochrome c upon reduction
-
Cohen, D. S. & Pielak, G. J. (1995). Entropic stabilization of cytochrome c upon reduction. J. Am. Chem. Soc. 117, 1675-1677.
-
(1995)
J. Am. Chem. Soc.
, vol.117
, pp. 1675-1677
-
-
Cohen, D.S.1
Pielak, G.J.2
-
10
-
-
0030473296
-
Kinetic intermediates in the formation of the cytochrome c molten globule
-
Colón, W. & Roder, H. (1996). Kinetic intermediates in the formation of the cytochrome c molten globule. Nature Struct. Biol. 3, 1019-1025.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 1019-1025
-
-
Colón, W.1
Roder, H.2
-
11
-
-
0029967474
-
Side chain packing of the N- And C-terminal helices plays a critical role in the kinetics of cytochrome c folding
-
Colón, W., Elöve, G. A., Wakem, L. P., Sherman, F. & Roder, H. (1996). Side chain packing of the N- and C-terminal helices plays a critical role in the kinetics of cytochrome c folding. Biochemistry, 35, 5538-5549.
-
(1996)
Biochemistry
, vol.35
, pp. 5538-5549
-
-
Colón, W.1
Elöve, G.A.2
Wakem, L.P.3
Sherman, F.4
Roder, H.5
-
13
-
-
0023290578
-
Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: Improved stability of the mutant protein
-
Cutler, R. L., Pielak, G. J., Mauk, A. G. & Smith, M. (1987). Replacement of cysteine-107 of Saccharomyces cerevisiae iso-1-cytochrome c with threonine: improved stability of the mutant protein. Protein Eng. 1, 95-99.
-
(1987)
Protein Eng.
, vol.1
, pp. 95-99
-
-
Cutler, R.L.1
Pielak, G.J.2
Mauk, A.G.3
Smith, M.4
-
14
-
-
0023948010
-
High efficiency transformation of E. coli by high voltage electroporation
-
Dower, W. J., Miller, J. F. & Ragsdale, C. W. (1988). High efficiency transformation of E. coli by high voltage electroporation. Nucl. Acids Res. 16, 6127-6145.
-
(1988)
Nucl. Acids Res.
, vol.16
, pp. 6127-6145
-
-
Dower, W.J.1
Miller, J.F.2
Ragsdale, C.W.3
-
15
-
-
0017718187
-
Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes
-
Elwell, M. L. & Schellman, J. A. (1977). Stability of phage T4 lysozymes. I. Native properties and thermal stability of wild type and two mutant lysozymes. Biochim. Biophys. Acta, 494, 367-383.
-
(1977)
Biochim. Biophys. Acta
, vol.494
, pp. 367-383
-
-
Elwell, M.L.1
Schellman, J.A.2
-
16
-
-
0027995384
-
Classification of acid denaturation of proteins: Intermediates and unfolded states
-
Fink, A. L., Calciano, L. J., Goto, Y., Kurotsu, T. & Palleros, D. R. (1994). Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry, 33, 12504-12511.
-
(1994)
Biochemistry
, vol.33
, pp. 12504-12511
-
-
Fink, A.L.1
Calciano, L.J.2
Goto, Y.3
Kurotsu, T.4
Palleros, D.R.5
-
17
-
-
85030303365
-
-
Doctoral dissertation, The University of North Carolina at Chapel Hill, Chapel Hill, NC
-
Fredericks, Z. L. (1993). The effects of amino acid substitutions in the C-terminal helix on the functionality, structure and stability of iso-1-cytochrome c. Doctoral dissertation, The University of North Carolina at Chapel Hill, Chapel Hill, NC.
-
(1993)
The Effects of Amino Acid Substitutions in the C-terminal Helix on the Functionality, Structure and Stability of Iso-1-cytochrome c
-
-
Fredericks, Z.L.1
-
18
-
-
0027450286
-
Exploring the interface between the N- And C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix
-
Fredericks, Z. L. & Pielak, G. J. (1993). Exploring the interface between the N- and C-terminal helices of cytochrome c by random mutagenesis within the C-terminal helix. Biochemistry, 32, 929-936.
-
(1993)
Biochemistry
, vol.32
, pp. 929-936
-
-
Fredericks, Z.L.1
Pielak, G.J.2
-
19
-
-
0025727988
-
Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts
-
Gao, Y., Boyd, J., Pielak, G. J. & Williams, R. J. P. (1991). Comparison of reduced and oxidized yeast iso-1-cytochrome c using proton paramagnetic shifts. Biochemistry, 30, 1928-1934.
-
(1991)
Biochemistry
, vol.30
, pp. 1928-1934
-
-
Gao, Y.1
Boyd, J.2
Pielak, G.J.3
Williams, R.J.P.4
-
20
-
-
0028900809
-
Protein structure refinement based on paramagnetic NMR shifts: Application to wild-type and mutant forms of cytochrome c
-
Gochin, M. & Roder, H. (1995). Protein structure refinement based on paramagnetic NMR shifts: application to wild-type and mutant forms of cytochrome c. Protein Sci. 4, 296-305.
-
(1995)
Protein Sci.
, vol.4
, pp. 296-305
-
-
Gochin, M.1
Roder, H.2
-
21
-
-
0028143596
-
Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry
-
Hamada, D., Kidokoro, S.-I., Fukada, H., Takahashi, K. & Goto, G. (1994). Salt-induced formation of the molten globule state of cytochrome c studied by isothermal titration calorimetry. Proc. Natl Acad. Sci. USA, 91, 10325-10329.
-
(1994)
Proc. Natl Acad. Sci. USA
, vol.91
, pp. 10325-10329
-
-
Hamada, D.1
Kidokoro, S.-I.2
Fukada, H.3
Takahashi, K.4
Goto, G.5
-
22
-
-
0029863253
-
Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c
-
Hamada, D., Kuroda, Y., Kataoka, M., Aimoto, S., Yoshimura, T. & Goto, Y. (1996). Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c. J. Mol. Biol. 256, 172-186.
-
(1996)
J. Mol. Biol.
, vol.256
, pp. 172-186
-
-
Hamada, D.1
Kuroda, Y.2
Kataoka, M.3
Aimoto, S.4
Yoshimura, T.5
Goto, Y.6
-
23
-
-
0020959710
-
Studies of transformation of Escherichia coli with plasmids
-
Hanahan, D. (1983). Studies of transformation of Escherichia coli with plasmids. J. Mol. Biol. 166, 557-580.
-
(1983)
J. Mol. Biol.
, vol.166
, pp. 557-580
-
-
Hanahan, D.1
-
24
-
-
0025800137
-
The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector
-
Hilgen, S. E. & Pielak, G. J. (1991). The function of the Saccharomyces cerevisiae iso-1-cytochrome c gene is independent of the codon at invariant residue Phe82 when the gene is present on a low-copy-number vector. Protein Eng. 4, 575-578.
-
(1991)
Protein Eng.
, vol.4
, pp. 575-578
-
-
Hilgen, S.E.1
Pielak, G.J.2
-
25
-
-
85030300298
-
-
Doctoral dissertation, The University of North Carolina at Chapel Hill, Chapel Hill, NC
-
Hilgen-Willis, S. (1993). Spectroscopic, thermodynamic, and genetic studies of Saccharomyces cerevisiae iso-1-cytochrome c with substitutions at positions 6, 10, 20, 52, 82, 97, and 102. Doctoral dissertation, The University of North Carolina at Chapel Hill, Chapel Hill, NC.
-
(1993)
Spectroscopic, Thermodynamic, and Genetic Studies of Saccharomyces Cerevisiae Iso-1-Cytochrome c with Substitutions at Positions 6, 10, 20, 52, 82, 97, and 102
-
-
Hilgen-Willis, S.1
-
26
-
-
0027749370
-
Formation of a molten globule intermediate early in the kinetic folding pathway of apomyoglobin
-
Jennings, P. A. & 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
-
27
-
-
0027400842
-
Molten globule of cytochrome c studied by small angle X-ray scattering
-
Kataoka, M., Hagihara, Y., Mihara, K. & Goto, Y. (1993). Molten globule of cytochrome c studied by small angle X-ray scattering. J. Mol. Biol. 229, 591-596.
-
(1993)
J. Mol. Biol.
, vol.229
, pp. 591-596
-
-
Kataoka, M.1
Hagihara, Y.2
Mihara, K.3
Goto, Y.4
-
28
-
-
0029981924
-
Packing interactions in the apomyoglobin folding intermediate
-
Kay, M. S. & Baldwin, R. L. (1996). Packing interactions in the apomyoglobin folding intermediate. Nature Struct. Biol. 3, 439-445.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 439-445
-
-
Kay, M.S.1
Baldwin, R.L.2
-
29
-
-
0030057477
-
Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues
-
Khorasanizadeh, S., Peters, I. D. & Roder, H (1996). Evidence for a three-state model of protein folding from kinetic analysis of ubiquitin variants with altered core residues. Nature Struct. Biol. 3, 193-205.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 193-205
-
-
Khorasanizadeh, S.1
Peters, I.D.2
Roder, H.3
-
30
-
-
0026525049
-
Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process
-
Kuroda, Y., Kidokoro, S.-I. & Wada, A. (1992). Thermodynamic characterization of cytochrome c at low pH. Observation of the molten globule state and of the cold denaturation process. J. Mol. Biol. 223, 1139-1153.
-
(1992)
J. Mol. Biol.
, vol.223
, pp. 1139-1153
-
-
Kuroda, Y.1
Kidokoro, S.-I.2
Wada, A.3
-
32
-
-
0028926855
-
A native tertiary interaction stabilizes the A-state of cytochrome c
-
Marmorino, J. L. & Pielak, G. J. (1995). A native tertiary interaction stabilizes the A-state of cytochrome c. Biochemistry, 34, 3140-3143.
-
(1995)
Biochemistry
, vol.34
, pp. 3140-3143
-
-
Marmorino, J.L.1
Pielak, G.J.2
-
33
-
-
0021902977
-
The structure, function and evolution of cytochromes
-
Matthews, F. S. (1985). The structure, function and evolution of cytochromes. Prog. Biophys. Mol. Biol. 45, 1-56.
-
(1985)
Prog. Biophys. Mol. Biol.
, vol.45
, pp. 1-56
-
-
Matthews, F.S.1
-
36
-
-
0028568650
-
Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: Comparison with experimental scales
-
Muñoz, V. & Serrano, L. (1994). Intrinsic secondary structure propensities of the amino acids, using statistical φ-ψ matrices: comparison with experimental scales. Proteins: Struct. Funct. Genet. 20, 301-311.
-
(1994)
Proteins: Struct. Funct. Genet.
, vol.20
, pp. 301-311
-
-
Muñoz, V.1
Serrano, L.2
-
37
-
-
0028820703
-
Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding
-
Myers, J. K., Pace, C. N & 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
-
38
-
-
0030904568
-
A direct comparison of helix propensity in proteins and peptides
-
Myers, J. K., Pace, C. N. & Scholtz, J. M. (1997). A direct comparison of helix propensity in proteins and peptides. Proc. Natl Acad. Sci. USA. 94, 2833-2837.
-
(1997)
Proc. Natl Acad. Sci. USA
, vol.94
, pp. 2833-2837
-
-
Myers, J.K.1
Pace, C.N.2
Scholtz, J.M.3
-
39
-
-
0000181415
-
The influence of amino acid side chains on the free energy of helix-coil transitions
-
Némethy, G., Leach, S. J. & Scheraga, H. A. (1966). The influence of amino acid side chains on the free energy of helix-coil transitions. J. Phys. Chem. 70, 998-1004.
-
(1966)
J. Phys. Chem.
, vol.70
, pp. 998-1004
-
-
Némethy, G.1
Leach, S.J.2
Scheraga, H.A.3
-
40
-
-
0024002575
-
A rapid droplet method for Sanger dideoxy sequencing
-
Ner, S. S., Goodin, D. B., Pielak, G. J. & Smith, M. (1988). A rapid droplet method for Sanger dideoxy sequencing. Biotechniques, 6, 408-412.
-
(1988)
Biotechniques
, vol.6
, pp. 408-412
-
-
Ner, S.S.1
Goodin, D.B.2
Pielak, G.J.3
Smith, M.4
-
41
-
-
0028920911
-
Protein thermal denaturation, side-chain models, and evolution: Amino acid substitutions at a conserved helix-helix interface
-
Pielak, G. J., Auld, D. S., Beasley, J. R., Betz, S. F., Cohen, D. S., Doyle, D. F., Finger, S. A., Fredericks, Z. L., Hilgen-Willis, S., Saunders, A. J. & Trojak, S. K. (1995). Protein thermal denaturation, side-chain models, and evolution: amino acid substitutions at a conserved helix-helix interface. Biochemistry, 34, 3268-3276.
-
(1995)
Biochemistry
, vol.34
, pp. 3268-3276
-
-
Pielak, G.J.1
Auld, D.S.2
Beasley, J.R.3
Betz, S.F.4
Cohen, D.S.5
Doyle, D.F.6
Finger, S.A.7
Fredericks, Z.L.8
Hilgen-Willis, S.9
Saunders, A.J.10
Trojak, S.K.11
-
42
-
-
0013660457
-
Nuclear magnetic resonance studies of class I cytochromes c
-
(Scott, R. A. & Mauk, A. G., eds), University Science Books, Sausalito
-
Pielak, G. J., Auld, D. S., Betz, S. F., Hilgen-Willis, S. E. & Garcia, L. L. (1996). Nuclear magnetic resonance studies of class I cytochromes c. In Cytochrome c: A Multidisciplinary Approach (Scott, R. A. & Mauk, A. G., eds), pp. 203-284, University Science Books, Sausalito.
-
(1996)
Cytochrome C: A Multidisciplinary Approach
, pp. 203-284
-
-
Pielak, G.J.1
Auld, D.S.2
Betz, S.F.3
Hilgen-Willis, S.E.4
Garcia, L.L.5
-
43
-
-
0002940127
-
The molten globule state
-
(Creighton, T. E., ed.), Freeman, New York
-
Ptitsyn, O. B. (1992). The molten globule state. Protein Folding (Creighton, T. E., ed.), pp. 243-300, Freeman, New York.
-
(1992)
Protein Folding
, pp. 243-300
-
-
Ptitsyn, O.B.1
-
44
-
-
0029886627
-
How molten is the molten globule?
-
Ptitsyn, O. (1996). How molten is the molten globule? Nature Struct. Biol. 3, 488-490.
-
(1996)
Nature Struct. Biol.
, vol.3
, pp. 488-490
-
-
Ptitsyn, O.1
-
45
-
-
0030961780
-
The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions
-
Raschke, T. M. & Marqusee, S. (1997). The kinetic folding intermediate of ribonuclease H resembles the acid molten globule and partially unfolded molecules detected under native conditions. Nature Struct. Biol. 4, 298-304.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 298-304
-
-
Raschke, T.M.1
Marqusee, S.2
-
46
-
-
0031055942
-
Kinetic role of early intermediates in protein folding
-
Roder, H. & Colón, W. (1997). Kinetic role of early intermediates in protein folding. Curr. Opin. Struct. Biol. 7, 15-28.
-
(1997)
Curr. Opin. Struct. Biol.
, vol.7
, pp. 15-28
-
-
Roder, H.1
Colón, W.2
-
47
-
-
0023705432
-
Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR
-
Roder, H., El(ve, G. A. & Englander, S. W. (1988). Structural characterization of folding intermediates in cytochrome c by H-exchange labelling and proton NMR. Nature, 335, 700-704.
-
(1988)
Nature
, vol.335
, pp. 700-704
-
-
Roder, H.1
Elve, G.A.2
Englander, S.W.3
-
48
-
-
0030768045
-
A residue-specific view of the non-cooperative unfolding of a molten globule
-
Schulman, B. A., Kim, P. S., Dobson, C. M. & Redfield, C. (1997). A residue-specific view of the non-cooperative unfolding of a molten globule. Nature Struct. Biol. 4, 630-634.
-
(1997)
Nature Struct. Biol.
, vol.4
, pp. 630-634
-
-
Schulman, B.A.1
Kim, P.S.2
Dobson, C.M.3
Redfield, C.4
-
49
-
-
0014430126
-
The mutational alteration of the primary structure of yeast iso-1-cytochrome c
-
Sherman, F., Stewart, J. W., Parker, J. H., Inhaber, E., Shipman, N. A., Putterman, G. J., Gardisky, R. L. & Margoliash, E. (1968). The mutational alteration of the primary structure of yeast iso-1-cytochrome c. J. Biol. Chem. 243, 5446-5456.
-
(1968)
J. Biol. Chem.
, vol.243
, pp. 5446-5456
-
-
Sherman, F.1
Stewart, J.W.2
Parker, J.H.3
Inhaber, E.4
Shipman, N.A.5
Putterman, G.J.6
Gardisky, R.L.7
Margoliash, E.8
-
50
-
-
0028402689
-
The barriers in protein folding
-
Sosnick, T. R., Mayne, L., Hiller, R. & Englander, S. W. (1994). The barriers in protein folding. Nature Struct. Biol. 1, 149-156.
-
(1994)
Nature Struct. Biol.
, vol.1
, pp. 149-156
-
-
Sosnick, T.R.1
Mayne, L.2
Hiller, R.3
Englander, S.W.4
-
51
-
-
0028952169
-
Bipartite structure of the α-lactalbumin molten globule
-
Wu, L. C., Peng, Z.-y. & Kim, P. S. (1995). Bipartite structure of the α-lactalbumin molten globule. Nature Struct. Biol. 2, 281-286.
-
(1995)
Nature Struct. Biol.
, vol.2
, pp. 281-286
-
-
Wu, L.C.1
Peng, Z.-Y.2
Kim, P.S.3
-
52
-
-
0026595799
-
Levinthal's paradox
-
Zwanig, R., Szabo, A. & Bagchi, B. (1992). Levinthal's paradox. Proc. Natl Acad. Sci. USA, 89, 20-22.
-
(1992)
Proc. Natl Acad. Sci. USA
, vol.89
, pp. 20-22
-
-
Zwanig, R.1
Szabo, A.2
Bagchi, B.3
|