-
1
-
-
0028947236
-
Thermodynamics of denaturation of barstar: Evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride
-
Agashe, V. R., and J. B. Udgaonkar. 1995. Thermodynamics of denaturation of barstar: evidence for cold denaturation and evaluation of the interaction with guanidine hydrochloride. Biochemistry. 34:3286-3299.
-
(1995)
Biochemistry
, vol.34
, pp. 3286-3299
-
-
Agashe, V.R.1
Udgaonkar, J.B.2
-
2
-
-
0032564313
-
Thermodynamic characterization of the conformational stability of the homodimeric protein, pea lectin
-
Ahmad, N., V. R. Srinivas, G. B. Reddy, and A. Surolia. 1998. Thermodynamic characterization of the conformational stability of the homodimeric protein, pea lectin. Biochemistry. 37:16765-16772.
-
(1998)
Biochemistry
, vol.37
, pp. 16765-16772
-
-
Ahmad, N.1
Srinivas, V.R.2
Reddy, G.B.3
Surolia, A.4
-
3
-
-
0042035633
-
Folding of phage P22 coat protein monomers: Kinetic and thermodynamic properties
-
Anderson, E., and C. M. Teschke. 2003. Folding of phage P22 coat protein monomers: kinetic and thermodynamic properties. Virology. 313:184-197.
-
(2003)
Virology
, vol.313
, pp. 184-197
-
-
Anderson, E.1
Teschke, C.M.2
-
4
-
-
0035912854
-
The reversible two-state unfolding of a monocot mannose-binding lectin from garlic bulbs reveals the dominant role of the dimeric interface in its stabilization
-
Bachhawat, K., M. Kapoor, T. K. Dam, and A. Surolia. 2001. The reversible two-state unfolding of a monocot mannose-binding lectin from garlic bulbs reveals the dominant role of the dimeric interface in its stabilization. Biochemistry. 40:7291-7300.
-
(2001)
Biochemistry
, vol.40
, pp. 7291-7300
-
-
Bachhawat, K.1
Kapoor, M.2
Dam, T.K.3
Surolia, A.4
-
5
-
-
2942740914
-
Thermodynamic characterization of monomeric and dimeric forms of CcdB (controller of cell division or death B protein)
-
Bajaj, K., G. Chakshusmathi, K. Bachhawat-Sikder, A. Surolia, and R. Varadarajan. 2004. Thermodynamic characterization of monomeric 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
-
6
-
-
0027254057
-
Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding
-
Barrick, D., and R. L. Baldwin. 1993. Stein and Moore Award address. The molten globule intermediate of apomyoglobin and the process of protein folding. Protein Sci. 2:869-876.
-
(1993)
Protein Sci.
, vol.2
, pp. 869-876
-
-
Barrick, D.1
Baldwin, R.L.2
-
7
-
-
0017599085
-
Lectin purification on affinity columns containing reductively animated disaccharides
-
Baues, R. J., and G. R. Gray. 1977. Lectin purification on affinity columns containing reductively animated disaccharides. J. Biol. Chem. 252: 57-60.
-
(1977)
J. Biol. Chem.
, vol.252
, pp. 57-60
-
-
Baues, R.J.1
Gray, G.R.2
-
8
-
-
11144221992
-
pH effects on the stability and dimerization of procaspase-3
-
Bose, K., and A. C. Clark. 2005. pH effects on the stability and dimerization of procaspase-3. Protein Sci. 14:24-36.
-
(2005)
Protein Sci.
, vol.14
, pp. 24-36
-
-
Bose, K.1
Clark, A.C.2
-
9
-
-
0036303451
-
The ATPase domain of SecA can form a tetramer in solution
-
Dempsey, B. R., A. Economou, S. D. Dunn, and B. H. Shilton. 2002. The ATPase domain of SecA can form a tetramer in solution. J. Mol. Biol. 315:831-843.
-
(2002)
J. Mol. Biol.
, vol.315
, pp. 831-843
-
-
Dempsey, B.R.1
Economou, A.2
Dunn, S.D.3
Shilton, B.H.4
-
10
-
-
0028921961
-
X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen
-
Dessen, A., D. Gupta, S. Sabesan, C. F. Brewer, and J. C. Sacchettini. 1995. X-ray crystal structure of the soybean agglutinin cross-linked with a biantennary analog of the blood group I carbohydrate antigen. Biochemistry. 34:4933-4942.
-
(1995)
Biochemistry
, vol.34
, pp. 4933-4942
-
-
Dessen, A.1
Gupta, D.2
Sabesan, S.3
Brewer, C.F.4
Sacchettini, J.C.5
-
11
-
-
7044247460
-
Folding mechanism of the CH2 antibody domain
-
Feige, M. J., W. Stefan, and J. Buchner. 2004. Folding mechanism of the CH2 antibody domain. J. Mol. Biol. 344:107-118.
-
(2004)
J. Mol. Biol.
, vol.344
, pp. 107-118
-
-
Feige, M.J.1
Stefan, W.2
Buchner, J.3
-
12
-
-
0025334690
-
Folding and stability of Trp aporepressor from Escherichia coli
-
Gittelman, M. S., and C. R. Matthews. 1990. Folding and stability of Trp aporepressor from Escherichia coli. Biochemistry. 29:7011-7020.
-
(1990)
Biochemistry
, vol.29
, pp. 7011-7020
-
-
Gittelman, M.S.1
Matthews, C.R.2
-
13
-
-
0004180464
-
-
Department of Biomolecular Sciences, UMIST, Manchester, UK
-
Hubbard, S. J. 1996. NACCESS, Ver. 2.1.1 Computer Program, Department of Biomolecular Sciences, UMIST, Manchester, UK.
-
(1996)
NACCESS, Ver. 2.1.1 Computer Program
-
-
Hubbard, S.J.1
-
14
-
-
0015976317
-
Subunit structure of soybean agglutinin
-
Lotan, R., H. W. Siegelman, H. Lis, and N. Sharon. 1974. Subunit structure of soybean agglutinin. J. Biol. Chem. 249:1219-1224.
-
(1974)
J. Biol. Chem.
, vol.249
, pp. 1219-1224
-
-
Lotan, R.1
Siegelman, H.W.2
Lis, H.3
Sharon, N.4
-
15
-
-
0027313673
-
Pathways of protein folding
-
Matthews, C. R. 1993. Pathways of protein folding. Annu. Rev. Biochem. 62:653-658.
-
(1993)
Annu. Rev. Biochem.
, vol.62
, pp. 653-658
-
-
Matthews, C.R.1
-
16
-
-
0142031495
-
Role of N-linked glycan in the unfolding pathway of Erythrina corallodendron lectin
-
Mitra, N., N. Sharon, and A. Surolia. 2003. Role of N-linked glycan in the unfolding pathway of Erythrina corallodendron lectin. Biochemistry. 42:12208-12216.
-
(2003)
Biochemistry
, vol.42
, pp. 12208-12216
-
-
Mitra, N.1
Sharon, N.2
Surolia, A.3
-
17
-
-
0037162419
-
Conformational stability of legume lectins reflect their different modes of quaternary association: Solvent denaturation studies on Concanavalin A and winged bean acidic agglutinin
-
Mitra, N., V. R. Srinivas, T. N. Ramya, N. Ahmad, G. B. Reddy, and A. Surolia. 2002. Conformational stability of legume lectins reflect their different modes of quaternary association: solvent denaturation studies on Concanavalin A and winged bean acidic agglutinin. Biochemistry. 41:9256-9263.
-
(2002)
Biochemistry
, vol.41
, pp. 9256-9263
-
-
Mitra, N.1
Srinivas, V.R.2
Ramya, T.N.3
Ahmad, N.4
Reddy, G.B.5
Surolia, A.6
-
18
-
-
0029761976
-
Conformational stability of the Escherichia coli HPr protein: Test of the linear extrapolation method and a thermodynamic characterization of cold denaturation
-
Nicholson, E. M., and J. M. Scholtz. 1996. Conformational stability of the Escherichia coli HPr protein: test of the linear extrapolation method and a thermodynamic characterization of cold denaturation. Biochemistry. 35:11369-11378.
-
(1996)
Biochemistry
, vol.35
, pp. 11369-11378
-
-
Nicholson, E.M.1
Scholtz, J.M.2
-
19
-
-
0025019350
-
Conformational stability of globular proteins
-
Pace, C. N. 1990. Conformational stability of globular proteins. Trends Biochem. Sci. 15:14-17.
-
(1990)
Trends Biochem. Sci.
, vol.15
, pp. 14-17
-
-
Pace, C.N.1
-
20
-
-
1242283878
-
Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: Equilibrium studies at neutral pH
-
Parisi, M., A. Mazzini, R. T. Sorbi, R. Ramoni, S. Grolli, and R. Favilla. 2003. Unfolding and refolding of porcine odorant binding protein in guanidinium hydrochloride: equilibrium studies at neutral pH. Biochim. Biophys. Acta. 1652:115-125.
-
(2003)
Biochim. Biophys. Acta
, vol.1652
, pp. 115-125
-
-
Parisi, M.1
Mazzini, A.2
Sorbi, R.T.3
Ramoni, R.4
Grolli, S.5
Favilla, R.6
-
21
-
-
0024199422
-
Stability of protein structure and hydrophobic interaction
-
Privalov, P. L., and S. J. Gill. 1988. Stability of protein structure and hydrophobic interaction. Adv. Protein Chem. 39:191-235.
-
(1988)
Adv. Protein Chem.
, vol.39
, pp. 191-235
-
-
Privalov, P.L.1
Gill, S.J.2
-
22
-
-
0033582454
-
Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization
-
Reddy, G. B., V. R. Srinivas, N. Ahmad, and A. Surolia. 1999. Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity. Implications in protein folding and legume lectin oligomerization. J. Biol. Chem. 274:4500-4503.
-
(1999)
J. Biol. Chem.
, vol.274
, pp. 4500-4503
-
-
Reddy, G.B.1
Srinivas, V.R.2
Ahmad, N.3
Surolia, A.4
-
23
-
-
0025030410
-
Selective binding and solvent denaturation
-
Schellman, J. A. 1990. Selective binding and solvent denaturation. Biophys. Chem. 37:121-140.
-
(1990)
Biophys. Chem.
, vol.37
, pp. 121-140
-
-
Schellman, J.A.1
-
24
-
-
21244473965
-
Unfolding studies on soybean agglutinin and Concanavalin-A tetramers: A comparative account
-
Sinha, S., N. Mitra, G. Kumar, K. Bajaj, and A. Surolia. 2005. Unfolding studies on soybean agglutinin and Concanavalin-A tetramers: a comparative account. Biophys. J. 88:1300-1310.
-
(2005)
Biophys. J.
, vol.88
, pp. 1300-1310
-
-
Sinha, S.1
Mitra, N.2
Kumar, G.3
Bajaj, K.4
Surolia, A.5
-
25
-
-
0035882421
-
Legume lectin family, the "natural mutants of the quaternary state", provide insights into the relationship between protein stability and oligomerization
-
Srinivas, V. R., G. B. Reddy, N. Ahmad, C. P. Swaminathan, N. Mitra, and A. Surolia. 2001. Legume lectin family, the "natural mutants of the quaternary state", provide insights into the relationship between protein stability and oligomerization. Biochim. Biophys. Acta. 1527:102-111.
-
(2001)
Biochim. Biophys. Acta
, vol.1527
, pp. 102-111
-
-
Srinivas, V.R.1
Reddy, G.B.2
Ahmad, N.3
Swaminathan, C.P.4
Mitra, N.5
Surolia, A.6
-
26
-
-
12344274329
-
Monitoring of unfolding and refolding in fungal phytase (phyA) by dynamic light scattering
-
Ullah, A. H. J., K. Sethumadhavan, and E. J. Mullaney. 2005. Monitoring of unfolding and refolding in fungal phytase (phyA) by dynamic light scattering. Biochem. Biophys. Res. Com. 327:993-998.
-
(2005)
Biochem. Biophys. Res. Com.
, vol.327
, pp. 993-998
-
-
Ullah, A.H.J.1
Sethumadhavan, K.2
Mullaney, E.J.3
-
27
-
-
0036295816
-
Hemoglobin equilibrium analysis by the multiangle laser light-scattering method
-
Yamaguchi, T., and K. Adachi. 2002. Hemoglobin equilibrium analysis by the multiangle laser light-scattering method. Biochem. Biophys. Res. Com. 290:1382-1387.
-
(2002)
Biochem. Biophys. Res. Com.
, vol.290
, pp. 1382-1387
-
-
Yamaguchi, T.1
Adachi, K.2
|