메뉴 건너뛰기




Volumn 88, Issue 2, 2005, Pages 1300-1310

Unfolding studies on soybean agglutinin and Concanavalin A tetramers: A comparative account

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CONCANAVALIN A; GLYCOPROTEIN; LECTIN; SOYBEAN AGGLUTININ; AGGLUTININ; GUANIDINE; MULTIPROTEIN COMPLEX;

EID: 21244473965     PISSN: 00063495     EISSN: None     Source Type: Journal    
DOI: 10.1529/biophysj.104.051052     Document Type: Article
Times cited : (48)

References (41)
  • 1
    • 0028947236 scopus 로고
    • 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
    • 0014215017 scopus 로고
    • Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross- Linked dextran gels
    • Agrawal, B. B., and I. J. Goldstein. 1967. Protein-carbohydrate interaction. VI. Isolation of concanavalin A by specific adsorption on cross- linked dextran gels. Biochim. Biophys. Acta. 147:262-271.
    • (1967) Biochim. Biophys. Acta , vol.147 , pp. 262-271
    • Agrawal, B.B.1    Goldstein, I.J.2
  • 3
    • 0032564313 scopus 로고    scopus 로고
    • 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
  • 4
    • 0344073971 scopus 로고    scopus 로고
    • Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius
    • Backmann, J., G. Schafer, L. Wyns, and H. Bonisch. 1998. Thermodynamics and kinetics of unfolding of the thermostable trimeric adenylate kinase from the archaeon Sulfolobus acidocaldarius. J. Mol. Biol. 284:817-833.
    • (1998) J. Mol. Biol. , vol.284 , pp. 817-833
    • Backmann, J.1    Schafer, G.2    Wyns, L.3    Bonisch, H.4
  • 5
    • 0027254057 scopus 로고
    • 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
  • 6
    • 0017599085 scopus 로고
    • Lectin purification on affinity columns containing reductively aminated disaccharides
    • Baues, R. J., and G. R. Gray. 1977. Lectin purification on affinity columns containing reductively aminated disaccharides. J. Biol. Chem. 252:57-60.
    • (1977) J. Biol. Chem. , vol.252 , pp. 57-60
    • Baues, R.J.1    Gray, G.R.2
  • 7
    • 0024962376 scopus 로고
    • Equilibrium dissociation and unfolding of the Arc repressor dimer
    • Bowie, J. U., and R. T. Sauer. 1989. Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry. 28:7139-7143.
    • (1989) Biochemistry , vol.28 , pp. 7139-7143
    • Bowie, J.U.1    Sauer, R.T.2
  • 8
    • 0035667230 scopus 로고    scopus 로고
    • Structural similarity and functional diversity in proteins containing the legume lectin fold
    • Chandra, N. R., M. M. Prabu, K. Suguna, and M. Vijayan. 2001. Structural similarity and functional diversity in proteins containing the legume lectin fold. Protein Eng. 14:857-866.
    • (2001) Protein Eng. , vol.14 , pp. 857-866
    • Chandra, N.R.1    Prabu, M.M.2    Suguna, K.3    Vijayan, M.4
  • 9
    • 0030978479 scopus 로고    scopus 로고
    • Thermodynamic characterization of the reversible, two-state unfolding of maltose binding protein, a large two-domain protein
    • Ganesh, C., A. N. Shah, C. P. Swaminathan, A. Surolia, and R. Varadarajan. 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
  • 10
    • 0025334690 scopus 로고
    • 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
  • 11
    • 0032813944 scopus 로고    scopus 로고
    • The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli
    • Gualfetti, P. J., O. Bilsel, and C. R. Matthews. 1999. The progressive development of structure and stability during the equilibrium folding of the alpha subunit of tryptophan synthase from Escherichia coli. Protein Sci. 8:1623-1635.
    • (1999) Protein Sci. , vol.8 , pp. 1623-1635
    • Gualfetti, P.J.1    Bilsel, O.2    Matthews, C.R.3
  • 12
    • 0015516458 scopus 로고
    • Structure of Concanavalin A at 2.4-A resolution
    • Hardman, K. D., and C. F. Ainsworth. 1972. Structure of Concanavalin A at 2.4-A resolution. Biochemistry. 11:4910-4919.
    • (1972) Biochemistry , vol.11 , pp. 4910-4919
    • Hardman, K.D.1    Ainsworth, C.F.2
  • 14
    • 0032727842 scopus 로고    scopus 로고
    • Effect of N-linked glycosylation on glycopeptide and glycoprotein structure
    • Imperiali, B., and S. E. O'Connor. 1999. Effect of N-linked glycosylation on glycopeptide and glycoprotein structure. Curr. Opin. Chem. Biol. 3:643-649.
    • (1999) Curr. Opin. Chem. Biol. , vol.3 , pp. 643-649
    • Imperiali, B.1    O'Connor, S.E.2
  • 15
    • 0025906146 scopus 로고
    • Contribution to the thermodynamics of protein folding from the reduction in water accessible nonpolar surface area
    • Livingstone, J. R., R. S. Spolar, and M. T. Record, Jr. 1991. Contribution to the thermodynamics of protein folding from the reduction in water accessible nonpolar surface area. Biochemistry. 30:4237-4244.
    • (1991) Biochemistry , vol.30 , pp. 4237-4244
    • Livingstone, J.R.1    Spolar, R.S.2    Record Jr., M.T.3
  • 17
    • 0034613013 scopus 로고    scopus 로고
    • Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin
    • Manoj, N., V. R. Srinivas, A. Surolia, M. Vijayan, and K. Suguna. 2000. Carbohydrate specificity and salt-bridge mediated conformational change in acidic winged bean agglutinin. J. Mol. Biol. 302:1129-1137.
    • (2000) J. Mol. Biol. , vol.302 , pp. 1129-1137
    • Manoj, N.1    Srinivas, V.R.2    Surolia, A.3    Vijayan, M.4    Suguna, K.5
  • 18
    • 0035667291 scopus 로고    scopus 로고
    • Signature of quaternary structure in the sequences of legume lectins
    • Manoj, N., and K. Suguna. 2001. Signature of quaternary structure in the sequences of legume lectins. Protein Eng. 14:735-745.
    • (2001) Protein Eng. , vol.14 , pp. 735-745
    • Manoj, N.1    Suguna, K.2
  • 19
    • 0027313673 scopus 로고
    • 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
  • 20
    • 0028304962 scopus 로고
    • Satisfying hydrogen bonding potential in proteins
    • McDonald, I. K., and J. M. Thornton. 1994. Satisfying hydrogen bonding potential in proteins. J. Mol. Biol. 238:777-793.
    • (1994) J. Mol. Biol. , vol.238 , pp. 777-793
    • McDonald, I.K.1    Thornton, J.M.2
  • 21
    • 0142031495 scopus 로고    scopus 로고
    • 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
  • 22
    • 0037162419 scopus 로고    scopus 로고
    • 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
  • 23
    • 0029843132 scopus 로고    scopus 로고
    • Hydrogen bonding stabilizes globular proteins
    • Myers, J. K., and C. N. Pace. 1996. Hydrogen bonding stabilizes globular proteins. Biophys. J. 71:2033-2039.
    • (1996) Biophys. J. , vol.71 , pp. 2033-2039
    • Myers, J.K.1    Pace, C.N.2
  • 24
    • 0028606077 scopus 로고
    • Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation
    • Neet, K. E., and D. E. Timm. 1994. Conformational stability of dimeric proteins: quantitative studies by equilibrium denaturation. Protein Sci. 3:2167-2174.
    • (1994) Protein Sci , vol.3 , pp. 2167-2174
    • Neet, K.E.1    Timm, D.E.2
  • 25
    • 0029761976 scopus 로고    scopus 로고
    • 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
  • 26
    • 0030267033 scopus 로고    scopus 로고
    • Modulation of protein structure and function by asparagines linked glycosylation
    • O'Connor, S. E., and B. Imperiali. 1996. Modulation of protein structure and function by asparagines linked glycosylation. Chem. Biol. 3:803-812.
    • (1996) Chem. Biol. , vol.3 , pp. 803-812
    • O'Connor, S.E.1    Imperiali, B.2
  • 27
    • 0030720932 scopus 로고    scopus 로고
    • X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosachharides and soybean agglutinin
    • Olsen, L. R., A. Dessen, D. Gupta, S. Sabesan, J. C. Sacchettini, and C. F. Brewer. 1997. X-ray crystallographic studies of unique cross-linked lattices between four isomeric biantennary oligosachharides and soybean agglutinin. Biochemistry. 36:15073-15080.
    • (1997) Biochemistry , vol.36 , pp. 15073-15080
    • Olsen, L.R.1    Dessen, A.2    Gupta, D.3    Sabesan, S.4    Sacchettini, J.C.5    Brewer, C.F.6
  • 28
    • 0025019350 scopus 로고
    • 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
  • 29
    • 0029156116 scopus 로고
    • Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding
    • Pace, C. N. 1995. Evaluating contribution of hydrogen bonding and hydrophobic bonding to protein folding. Methods Enzymol. 259:538-554.
    • (1995) Methods Enzymol. , vol.259 , pp. 538-554
    • Pace, C.N.1
  • 30
    • 0035895356 scopus 로고    scopus 로고
    • Polar group burial contributes more to protein stability than nonpolar group burial
    • Pace, C. N. 2001. Polar group burial contributes more to protein stability than nonpolar group burial. Biochemistry. 40:310-313.
    • (2001) Biochemistry , vol.40 , pp. 310-313
    • Pace, C.N.1
  • 31
    • 0030059689 scopus 로고    scopus 로고
    • Forces contributing to the conformational stability of proteins
    • Pace, C. N., B. A. Shirley, M. McNutt, and K. Gajiwala. 1996. Forces contributing to the conformational stability of proteins. FASEB J. 10:75-83.
    • (1996) FASEB J. , vol.10 , pp. 75-83
    • Pace, C.N.1    Shirley, B.A.2    McNutt, M.3    Gajiwala, K.4
  • 32
    • 0035951080 scopus 로고    scopus 로고
    • Role of chain termini for the folding transition state of cold shock protein
    • Perl, D., G. Holtermann, and F. X. Schmid. 2001. Role of chain termini for the folding transition state of cold shock protein. Biochemistry. 40:15501-15511.
    • (2001) Biochemistry , vol.40 , pp. 15501-15511
    • Perl, D.1    Holtermann, G.2    Schmid, F.X.3
  • 33
    • 0033120809 scopus 로고    scopus 로고
    • Variability in quaternary association of proteins with the same tertiary fold: A case study and rationalization involving legume lectins
    • Prabu, M. M., K. Suguna, and M. Vijayan. 1999. Variability in quaternary association of proteins with the same tertiary fold: a case study and rationalization involving legume lectins. Proteins. 35:58-69.
    • (1999) Proteins , vol.35 , pp. 58-69
    • Prabu, M.M.1    Suguna, K.2    Vijayan, M.3
  • 34
    • 0030937062 scopus 로고    scopus 로고
    • Glycosylation: Heterogeneity and 3D structure of proteins
    • Rudd, P. M., and R. A. Dwek. 1997. Glycosylation: heterogeneity and 3D structure of proteins. Crit. Rev. Biochem. Mol. 32:1-100.
    • (1997) Crit. Rev. Biochem. Mol. , vol.32 , pp. 1-100
    • Rudd, P.M.1    Dwek, R.A.2
  • 35
    • 0025030410 scopus 로고
    • 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
  • 36
    • 0026584344 scopus 로고
    • Contribution of hydrogen bonding to the conformational stability of ribonuclease T1
    • Shirley, B. A., P. Stanssens, U. Hahn, and C. N. Pace. 1992. Contribution of hydrogen bonding to the conformational stability of ribonuclease T1. Biochemistry. 31:725-732.
    • (1992) Biochemistry , vol.31 , pp. 725-732
    • Shirley, B.A.1    Stanssens, P.2    Hahn, U.3    Pace, C.N.4
  • 38
    • 0026684671 scopus 로고
    • Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water
    • Spolar, R. S., J. R. Livingstone, arid M. T. Record, Jr. 1992. Use of liquid hydrocarbon and amide transfer data to estimate contributions to thermodynamic functions of protein folding from the removal of nonpolar and polar surface from water. Biochemistry. 31:3947-3955.
    • (1992) Biochemistry , vol.31 , pp. 3947-3955
    • Spolar, R.S.1    Livingstone, J.R.2    Record Jr., M.T.3
  • 39
    • 0141990950 scopus 로고    scopus 로고
    • Effect of gatekeepers on the early folding kinetics of a model β-barrel protein
    • Stoycheva, A. D., J. N. Onuchic, and C. L. Brooks. 2003. Effect of gatekeepers on the early folding kinetics of a model β-barrel protein. J. Chem. Phys. 119:5722-5729.
    • (2003) J. Chem. Phys. , vol.119 , pp. 5722-5729
    • Stoycheva, A.D.1    Onuchic, J.N.2    Brooks, C.L.3
  • 40
    • 0030067976 scopus 로고    scopus 로고
    • Importance of two buried salt-bridges in the stability and folding pathway of barnase
    • Tissot, A. C., S. Vuilleumier, and A. R. Fersht. 1996. Importance of two buried salt-bridges in the stability and folding pathway of barnase. Biochemistry. 35:6786-6794.
    • (1996) Biochemistry , vol.35 , pp. 6786-6794
    • Tissot, A.C.1    Vuilleumier, S.2    Fersht, A.R.3
  • 41
    • 0030220095 scopus 로고    scopus 로고
    • Structural role of sugars in glycoproteins
    • Wyss, D. F., and G. Wagner. 1996. Structural role of sugars in glycoproteins. Curr. Opin. Biotechnol. 7:409-416.
    • (1996) Curr. Opin. Biotechnol. , vol.7 , pp. 409-416
    • Wyss, D.F.1    Wagner, G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.