메뉴 건너뛰기




Volumn 27, Issue 2, 1998, Pages 173-176

A reduction of protein specific motions in co-ligated myoglobin embedded in a trehalose glass

Author keywords

[No Author keywords available]

Indexed keywords

CARBOXYMYOGLOBIN; GLASS; HEMOGLOBIN; MYOGLOBIN; PROTEIN; TREHALOSE;

EID: 0031889847     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002490050123     Document Type: Review
Times cited : (85)

References (17)
  • 1
    • 0001566390 scopus 로고
    • Novel carbohydrate metabolism in the resurrection plant. Craterostigma Plantagineum
    • Bianchi G, Gamba A, Murellie C, Salamini F, Bartels D (1991) Novel carbohydrate metabolism in the resurrection plant. Craterostigma Plantagineum. Plant J 1:355-359
    • (1991) Plant J , vol.1 , pp. 355-359
    • Bianchi, G.1    Gamba, A.2    Murellie, C.3    Salamini, F.4    Bartels, D.5
  • 2
    • 0348053809 scopus 로고
    • Preservation of membranes in anhydrobiotic organisms: The role of trehalose
    • Crowe JH, Crowe LM, Chapman D (1984) Preservation of membranes in anhydrobiotic organisms: the role of trehalose. Science 223:701-703
    • (1984) Science , vol.223 , pp. 701-703
    • Crowe, J.H.1    Crowe, L.M.2    Chapman, D.3
  • 3
    • 0029820371 scopus 로고    scopus 로고
    • Is trehalose special for preserving dry biomaterials?
    • Crowe LM, David SR, Crowe JH (1996) Is trehalose special for preserving dry biomaterials? Biophys J 71:2087-2093
    • (1996) Biophys J , vol.71 , pp. 2087-2093
    • Crowe, L.M.1    David, S.R.2    Crowe, J.H.3
  • 4
    • 0028922168 scopus 로고
    • Low temperature optical spectroscopy as a tool to study structure-dynamics-function relationships in heme proteins
    • Cupane A, Leone M, Vitrano E, Cordone L (1995) Low temperature optical spectroscopy as a tool to study structure-dynamics-function relationships in heme proteins. Eur Biophys J 23: 385-398
    • (1995) Eur Biophys J , vol.23 , pp. 385-398
    • Cupane, A.1    Leone, M.2    Vitrano, E.3    Cordone, L.4
  • 5
    • 0026700192 scopus 로고
    • Vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape
    • Di Pace A, Cupane A, Leone M, Vitrano E, Cordone L (1992) Vibrational coupling, spectral broadening mechanisms and anharmonicity effects in carbonmonoxy heme proteins studied by the temperature dependence of the Soret band lineshape. Biophys J 63:475-484
    • (1992) Biophys J , vol.63 , pp. 475-484
    • Di Pace, A.1    Cupane, A.2    Leone, M.3    Vitrano, E.4    Cordone, L.5
  • 8
    • 0029647450 scopus 로고
    • Protein reaction kinetics in a room temperature glass
    • Hagen SJ, Hofrichter J, Eaton WA (1995) Protein reaction kinetics in a room temperature glass. Science 269: 959-962
    • (1995) Science , vol.269 , pp. 959-962
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 9
    • 0030197743 scopus 로고    scopus 로고
    • Geminate Rebinding and Conformational Dynamics of Myoglobin Embedded in a Glass at Room Temperature
    • Hagen SJ, Hofrichter J, Eaton WA (1996) Geminate Rebinding and Conformational Dynamics of Myoglobin Embedded in a Glass at Room Temperature. J Phys Chem 100: 12008-12021
    • (1996) J Phys Chem , vol.100 , pp. 12008-12021
    • Hagen, S.J.1    Hofrichter, J.2    Eaton, W.A.3
  • 10
    • 0028575357 scopus 로고
    • Thermal broadening of Soret band in heme complexes and in heme-proteins: Role of the iron dynamics
    • Leone M, Cupane A, Militello V, Cordone L (1994) Thermal broadening of Soret band in heme complexes and in heme-proteins: Role of the iron dynamics. Eur Biophys J 23: 349-352
    • (1994) Eur Biophys J , vol.23 , pp. 349-352
    • Leone, M.1    Cupane, A.2    Militello, V.3    Cordone, L.4
  • 11
    • 84908597142 scopus 로고
    • Anhydrobiosis in nematodes: Carbohydrate and lipid metabolism during dehydration
    • Madin KA, Crowe SH (1975) Anhydrobiosis in nematodes: carbohydrate and lipid metabolism during dehydration. J Exp Zool 193: 335-142
    • (1975) J Exp Zool , vol.193 , pp. 335-1142
    • Madin, K.A.1    Crowe, S.H.2
  • 12
    • 0030004479 scopus 로고
    • Structural fluctuations of myoglobin derived from Normal Mode Analysis: Comparison with Mössbauer, Resonance Raman, and Absorption Spectroscopy
    • Melchers B, Knapp EW, Parak F, Cordone L, Cupane A, Leone M (1995) Structural fluctuations of myoglobin derived from Normal Mode Analysis: Comparison with Mössbauer, Resonance Raman, and Absorption Spectroscopy. Biophys J 70: 2092-2099
    • (1995) Biophys J , vol.70 , pp. 2092-2099
    • Melchers, B.1    Knapp, E.W.2    Parak, F.3    Cordone, L.4    Cupane, A.5    Leone, M.6
  • 13
    • 0029242120 scopus 로고
    • Trehalose metabolism - New horizons in technological applications
    • Panek AD (1995) Trehalose metabolism - new horizons in technological applications. Brazilian J Med Biol Res 28: 169-181
    • (1995) Brazilian J Med Biol Res , vol.28 , pp. 169-181
    • Panek, A.D.1
  • 14
    • 0020333863 scopus 로고
    • Protein dynamics, Mössbauer spectroscopy on deoxymyoglobin crystals
    • Parak F, Knapp EW, Kucheida D (1982) Protein dynamics, Mössbauer spectroscopy on deoxymyoglobin crystals. J Mol Biol 161: 177-194
    • (1982) J Mol Biol , vol.161 , pp. 177-194
    • Parak, F.1    Knapp, E.W.2    Kucheida, D.3
  • 15
    • 0022555897 scopus 로고
    • Mössbauer effect in the study of structure dynamics
    • Parak F, Reinisch L (1986) Mössbauer effect in the study of structure dynamics. Methods in Enzymology 131:568-607
    • (1986) Methods in Enzymology , vol.131 , pp. 568-607
    • Parak, F.1    Reinisch, L.2
  • 17
    • 0030921074 scopus 로고    scopus 로고
    • Trehalose prevents myoglobin collapse and preserves its internal mobility
    • Sastry GM, Agmon N (1997) Trehalose prevents myoglobin collapse and preserves its internal mobility. Biochemistry 36:7097-7108
    • (1997) Biochemistry , vol.36 , pp. 7097-7108
    • Sastry, G.M.1    Agmon, N.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.