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Volumn 2, Issue 5, 1997, Pages 281-290

Identification of a conserved Hydrophobie cluster in partially folded bovine β-lactoglobulin at pH 2

Author keywords

Bovine lactoglobulin; Folding; Hydrophobic cluster; NMR; Structural alignment

Indexed keywords

LACTOGLOBULIN;

EID: 0030635208     PISSN: 13590278     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1359-0278(97)00039-4     Document Type: Article
Times cited : (84)

References (24)
  • 1
    • 0029944773 scopus 로고    scopus 로고
    • Partially folded structure of monomeric bovine β-lactoglobulin
    • Molinari, H., et al., & Monaco H.L. (1996). Partially folded structure of monomeric bovine β-lactoglobulin. FEBS Lett. 381, 237-243.
    • (1996) FEBS Lett. , vol.381 , pp. 237-243
    • Molinari, H.1    Monaco, H.L.2
  • 2
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco, H.L., Zanotti, G., Spadon, P., Bolognesi, M., Sawyer, L. & Eliopoulos, E.E. (1987). Crystal structure of the trigonal form of bovine beta-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 197, 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, M.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 3
    • 0022931198 scopus 로고
    • The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein
    • Papiz, M.Z., et al., & Kraulis, P.J. (1986). The structure of β-lactoglobulin and its similarity to plasma retinol-binding protein. Nature 324, 383-385.
    • (1986) Nature , vol.324 , pp. 383-385
    • Papiz, M.Z.1    Kraulis, P.J.2
  • 4
    • 0025306809 scopus 로고
    • An intriguing member of the lipocalin protein family: α1-microglobulin
    • Aakerstroem, B. & Loegdberg, L (1990). An intriguing member of the lipocalin protein family: α1-microglobulin. Trends Biochem. Sci. 15, 240-243.
    • (1990) Trends Biochem. Sci. , vol.15 , pp. 240-243
    • Aakerstroem, B.1    Loegdberg, L.2
  • 5
    • 0029294696 scopus 로고    scopus 로고
    • Multiple molecular recognition properties of the lipocalin protein family
    • Flower, D.R. (1997). Multiple molecular recognition properties of the lipocalin protein family J. Mol. Recognit. 8, 185-195.
    • (1997) J. Mol. Recognit. , vol.8 , pp. 185-195
    • Flower, D.R.1
  • 6
    • 0004907667 scopus 로고    scopus 로고
    • Bovine β-lactoglobulin at 1.8 Å resolution - Still an enigmatic lipocalin
    • Brownlow, S., et al., & Sawyer L. (1997). Bovine β-lactoglobulin at 1.8 Å resolution - still an enigmatic lipocalin. Structure 5, 481-495.
    • (1997) Structure , vol.5 , pp. 481-495
    • Brownlow, S.1    Sawyer, L.2
  • 7
    • 0028168283 scopus 로고
    • Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure
    • Katakura, J., Totsuka, M., Ametani, A. & Kaminogawa, S. (1994). Tryptophan-19 of β-lactoglobulin, the only residue completely conserved in the lipocalin superfamily, is not essential for binding retinol, but relevant to stabilizing bound retinol and maintaining its structure. Biochim. Biophys. Acta 1207, 58-67.
    • (1994) Biochim. Biophys. Acta , vol.1207 , pp. 58-67
    • Katakura, J.1    Totsuka, M.2    Ametani, A.3    Kaminogawa, S.4
  • 8
    • 0027995384 scopus 로고
    • Classification of acid denaturation of proteins: Intermediates and unfolded states
    • Rnk, A.L., Calciano, L.J., Goto, Y., Kurotsu T. & Palleros, D. (1994). Classification of acid denaturation of proteins: intermediates and unfolded states. Biochemistry 33, 12504-12511.
    • (1994) Biochemistry , vol.33 , pp. 12504-12511
    • Rnk, A.L.1    Calciano, L.J.2    Goto, Y.3    Kurotsu, T.4    Palleros, D.5
  • 11
    • 0027506279 scopus 로고
    • Structure and sequence relationships in the lipocalins and related proteins
    • Flower, D.R., North, A.C.T. & Attwood, T. (1993). Structure and sequence relationships in the lipocalins and related proteins. Protein Sci. 2, 753-761.
    • (1993) Protein Sci. , vol.2 , pp. 753-761
    • Flower, D.R.1    North, A.C.T.2    Attwood, T.3
  • 12
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L. & Sander, C. (1993). Protein structure comparison by alignment of distance matrices. J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 13
    • 0027522088 scopus 로고
    • Probing the fatty acid binding site of beta-lactoglobulins
    • Frapin, D., Dufour, E. & Haertle, T. (1993). Probing the fatty acid binding site of beta-lactoglobulins. J. Protein Chem. 12, 443-449.
    • (1993) J. Protein Chem. , vol.12 , pp. 443-449
    • Frapin, D.1    Dufour, E.2    Haertle, T.3
  • 14
    • 0025609431 scopus 로고
    • β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites
    • Dufour, E., Marden, M.C. & Haertlé, T. (1990). β-Lactoglobulin binds retinol and protoporphyrin IX at two different binding sites. FEBS Lett. 277, 223-226.
    • (1990) FEBS Lett. , vol.277 , pp. 223-226
    • Dufour, E.1    Marden, M.C.2    Haertlé, T.3
  • 15
    • 0031035893 scopus 로고    scopus 로고
    • Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin
    • Narayan, M. & Berliner, L.J. (1997). Fatty acids and retinoids bind independently and simultaneously to beta-lactoglobulin. Biochemistry 36,1906-1991.
    • (1997) Biochemistry , vol.36 , pp. 1906-1991
    • Narayan, M.1    Berliner, L.J.2
  • 16
    • 0028232955 scopus 로고
    • Searching protein structure databases has come of age
    • Holm, L & Sander, C. (1994). Searching protein structure databases has come of age. Proteins 19,165-173.
    • (1994) Proteins , vol.19 , pp. 165-173
    • Holm, L.1    Sander, C.2
  • 17
    • 0019443447 scopus 로고
    • The anatomy and taxonomy of protein structure
    • Richardson, J.S. (1981). The anatomy and taxonomy of protein structure. Adv. Protein Chem. 34, 167-333.
    • (1981) Adv. Protein Chem. , vol.34 , pp. 167-333
    • Richardson, J.S.1
  • 18
    • 0030067976 scopus 로고    scopus 로고
    • Importance of two buried salt bridges in the stability and folding pathway of barnase
    • Tissot, A.C., Vuilleumier, S. & Fersht, A.R. (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
  • 19
    • 0026475945 scopus 로고
    • Pheromone binding pocket to two rodent urinary proteins revealed by X-ray crystallography
    • Bocskei, Z., et al., & North, A.C.T. (1992). Pheromone binding pocket to two rodent urinary proteins revealed by X-ray crystallography. Nature 360,186-189.
    • (1992) Nature , vol.360 , pp. 186-189
    • Bocskei, Z.1    North, A.C.T.2
  • 20
    • 0028246854 scopus 로고
    • Probing the retinol-binding site of bovine β-lactoglobulin
    • Cho, Y., Batt, C. & Sawyer, L. (1994). Probing the retinol-binding site of bovine β-lactoglobulin. J. Biol. Chem. 269,11102-11107.
    • (1994) J. Biol. Chem. , vol.269 , pp. 11102-11107
    • Cho, Y.1    Batt, C.2    Sawyer, L.3
  • 21
    • 0029882171 scopus 로고    scopus 로고
    • Structural and energetic responses to cavity-creating mutations in hydrophobic cores: Observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities
    • Buckle, A.M., Cramer, P. & Fersht, A.R. (1996). Structural and energetic responses to cavity-creating mutations in hydrophobic cores: observation of a buried water molecule and the hydrophilic nature of such hydrophobic cavities. Biochemistry 35, 4298-4305.
    • (1996) Biochemistry , vol.35 , pp. 4298-4305
    • Buckle, A.M.1    Cramer, P.2    Fersht, A.R.3
  • 22
    • 0030334664 scopus 로고    scopus 로고
    • High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy
    • Kuroda, Y., Hamada, D., Tanaka, T. & Goto, Y. (1996). High helicity of peptide fragments corresponding to β-strand regions of β-lactoglobulin observed by 2D-NMR spectroscopy. Fold. Des. 1, 255-263.
    • (1996) Fold. Des. , vol.1 , pp. 255-263
    • Kuroda, Y.1    Hamada, D.2    Tanaka, T.3    Goto, Y.4
  • 23
    • 0001151420 scopus 로고
    • β-Lactoglobulins A and B. I. Chromatographic separation and amino acid composition
    • Piez, K.A., Davie, E.W., Folk, J.E. & Gladner, J.A. (1961). β-Lactoglobulins A and B. I. Chromatographic separation and amino acid composition. J. Biol. Chem. 236, 2912-2916.
    • (1961) J. Biol. Chem. , vol.236 , pp. 2912-2916
    • Piez, K.A.1    Davie, E.W.2    Folk, J.E.3    Gladner, J.A.4
  • 24
    • 0026410969 scopus 로고
    • Relationship between nuclear magnetic resonance chemical shift and protein secondary structure
    • Wishart, D.S., Sykes, B.D. & Richards, F.M. (1991). Relationship between nuclear magnetic resonance chemical shift and protein secondary structure. J. Mol. Biol. 222, 311-333.
    • (1991) J. Mol. Biol. , vol.222 , pp. 311-333
    • Wishart, D.S.1    Sykes, B.D.2    Richards, F.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.