메뉴 건너뛰기




Volumn 37, Issue 1, 2007, Pages 1-10

Structural transition temperature of hemoglobins correlates with species' body temperature

Author keywords

Denaturation; Hemoglobin; Protein dynamics; Structural transition

Indexed keywords

HEMOGLOBIN;

EID: 36348967741     PISSN: 01757571     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00249-007-0144-4     Document Type: Article
Times cited : (17)

References (29)
  • 1
    • 0036141636 scopus 로고    scopus 로고
    • Static and dynamic light scattering approach to the hydration of hemoglobin and its supertetramers in the presence of osmolites
    • Arosio D, Kwansa HE, Gering H, Piszczek G, Bucci E (2002) Static and dynamic light scattering approach to the hydration of hemoglobin and its supertetramers in the presence of osmolites. Biopolymers 63:1-11
    • (2002) Biopolymers , vol.63 , pp. 1-11
    • Arosio, D.1    Kwansa, H.E.2    Gering, H.3    Piszczek, G.4    Bucci, E.5
  • 3
    • 0031795577 scopus 로고    scopus 로고
    • Temperature transitions of protein properties in human red blood cells
    • Artmann GM, Kelemen C, Porst D, Büldt G, Chien S (1998) Temperature transitions of protein properties in human red blood cells. Biophys J 75:3179-3183
    • (1998) Biophys J , vol.75 , pp. 3179-3183
    • Artmann, G.M.1    Kelemen, C.2    Porst, D.3    Büldt, G.4    Chien, S.5
  • 5
    • 0035118232 scopus 로고    scopus 로고
    • Protein flexibility from the dynamical transition: A force constant analysis
    • Biscout DJ, Zaccai G (2001) Protein flexibility from the dynamical transition: a force constant analysis. Biophys J 80:1115-1123
    • (2001) Biophys J , vol.80 , pp. 1115-1123
    • Biscout, D.J.1    Zaccai, G.2
  • 6
    • 0024203899 scopus 로고
    • Water of hydration in the intra- and extra-cellular environment of human erythrocytes
    • Cameron IL, Ord VA, Fullerton GD (1988) Water of hydration in the intra- and extra-cellular environment of human erythrocytes. Biochem Cell Biol 66:1186-1199
    • (1988) Biochem Cell Biol , vol.66 , pp. 1186-1199
    • Cameron, I.L.1    Ord, V.A.2    Fullerton, G.D.3
  • 7
    • 0031812904 scopus 로고    scopus 로고
    • The ProDom database of protein domain families
    • Corpet F, Gouzy J, Kahn D (1998) The ProDom database of protein domain families. Nucleic Acids Res 26:323-326
    • (1998) Nucleic Acids Res , vol.26 , pp. 323-326
    • Corpet, F.1    Gouzy, J.2    Kahn, D.3
  • 9
    • 0024976853 scopus 로고
    • Dynamical transition of myoglobin revealed by inelastic neutron scattering
    • Doster W, Cusack S, Petry W (1989) Dynamical transition of myoglobin revealed by inelastic neutron scattering. Nature 337:754-756
    • (1989) Nature , vol.337 , pp. 754-756
    • Doster, W.1    Cusack, S.2    Petry, W.3
  • 10
    • 11144256279 scopus 로고    scopus 로고
    • Shear-induced alignment of self-associated hemoglobin in human erythrocytes: Small angle neutron scattering studies
    • Garvey CJ, Knott RB, Drabarek E, Kuchel PW (2004) Shear-induced alignment of self-associated hemoglobin in human erythrocytes: small angle neutron scattering studies. Eur Biophys J 33:589-595
    • (2004) Eur Biophys J , vol.33 , pp. 589-595
    • Garvey, C.J.1    Knott, R.B.2    Drabarek, E.3    Kuchel, P.W.4
  • 13
    • 0030042763 scopus 로고    scopus 로고
    • Methods to estimate the confirmation of proteins and polypeptides from circular dichroism data
    • Greenfield NJ (1996) Methods to estimate the confirmation of proteins and polypeptides from circular dichroism data. Anal Biochem 235:1-10
    • (1996) Anal Biochem , vol.235 , pp. 1-10
    • Greenfield, N.J.1
  • 16
    • 0026605537 scopus 로고
    • Clustal V: Improved software for multiple sequence alignment
    • Higgins DG, Bleasby AJ, Fuchs R (1991) Clustal V: improved software for multiple sequence alignment. Comput Appl Biosci 8:189-191
    • (1991) Comput Appl Biosci , vol.8 , pp. 189-191
    • Higgins, D.G.1    Bleasby, A.J.2    Fuchs, R.3
  • 17
    • 0034995585 scopus 로고    scopus 로고
    • Temperature transition of human hemoglobin at body temperature: Effects of calcium
    • Kelemen C, Chien S, Artmann GM (2001) Temperature transition of human hemoglobin at body temperature: effects of calcium. Biophys J 80:2622-2630
    • (2001) Biophys J , vol.80 , pp. 2622-2630
    • Kelemen, C.1    Chien, S.2    Artmann, G.M.3
  • 18
    • 0025076502 scopus 로고
    • Small angle neutron scattering studies of HbA in concentrated solutions
    • Krueger S, Chen S-H, Hofrichter J, Nossal R (1990) Small angle neutron scattering studies of HbA in concentrated solutions. Biophys J 58:745-757
    • (1990) Biophys J , vol.58 , pp. 745-757
    • Krueger, S.1    Chen, S.-H.2    Hofrichter, J.3    Nossal, R.4
  • 19
    • 0023744299 scopus 로고
    • SANS studies of interacting hemoglobin in intact erythrocytes
    • Krueger S, Nossal R (1988) SANS studies of interacting hemoglobin in intact erythrocytes. Biophys J 53:97-105
    • (1988) Biophys J , vol.53 , pp. 97-105
    • Krueger, S.1    Nossal, R.2
  • 20
    • 0000569692 scopus 로고
    • Translational diffusion of hemoglobin in human erythrocytes and hemolysates
    • Kuchel PW, Chapman BE (1991) Translational diffusion of hemoglobin in human erythrocytes and hemolysates. J Magn Reson 95:574-580
    • (1991) J Magn Reson , vol.95 , pp. 574-580
    • Kuchel, P.W.1    Chapman, B.E.2
  • 21
    • 0042768031 scopus 로고    scopus 로고
    • Myoglobin in crowded solutions: Structure and diffusion
    • Longeville S, Doster W, Kali G (2003) Myoglobin in crowded solutions: structure and diffusion. Chem Phys 292:413-424
    • (2003) Chem Phys , vol.292 , pp. 413-424
    • Longeville, S.1    Doster, W.2    Kali, G.3
  • 22
    • 33745571654 scopus 로고    scopus 로고
    • 1.25 a resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms
    • Park SY, Yokoyama T, Shibayama N, Shiro Y, Tame JR (2006) 1.25 A resolution crystal structures of human haemoglobin in the oxy, deoxy and carbonmonoxy forms. J Mol Biol 360:690-701
    • (2006) J Mol Biol , vol.360 , pp. 690-701
    • Park, S.Y.1    Yokoyama, T.2    Shibayama, N.3    Shiro, Y.4    Tame, J.R.5
  • 26
    • 1542345526 scopus 로고    scopus 로고
    • Protein thermal aggregation involves distinct regions: Sequential events in the heat-induced unfolding and aggregation of hemoglobin
    • Yan Y-B, Wang Q, He H-W, Zhou H-M (2004) Protein thermal aggregation involves distinct regions: sequential events in the heat-induced unfolding and aggregation of hemoglobin. Biophys J 86:1682-1690
    • (2004) Biophys J , vol.86 , pp. 1682-1690
    • Yan, Y.-B.1    Wang, Q.2    He, H.-W.3    Zhou, H.-M.4
  • 27
    • 0042823410 scopus 로고    scopus 로고
    • Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin
    • Yan Y-B, Wang Q, He H-W, Hu X-Y, Zhang R-Q, Zou H-M (2003) Two-dimensional infrared correlation spectroscopy study of sequential events in the heat-induced unfolding and aggregation process of myoglobin. Biophys J 85:1959-1967
    • (2003) Biophys J , vol.85 , pp. 1959-1967
    • Yan, Y.-B.1    Wang, Q.2    He, H.-W.3    Hu, X.-Y.4    Zhang, R.-Q.5    Zou, H.-M.6
  • 28
    • 0036430012 scopus 로고    scopus 로고
    • Biphasic reductive unfolding of ribonuclease a is temperature dependent
    • Yan Y-B, Zhang R-Q, Zhou H-M (2002) Biphasic reductive unfolding of ribonuclease A is temperature dependent. Eur J Biochem 269:5314-5322
    • (2002) Eur J Biochem , vol.269 , pp. 5314-5322
    • Yan, Y.-B.1    Zhang, R.-Q.2    Zhou, H.-M.3
  • 29
    • 0021398902 scopus 로고
    • Multicomponent analysis of hemoglobin derivatives with a reversed-optics spectrophotometer
    • Zwart A, Buursma A, van Kampen EJ, Zijlstra WG (1984) Multicomponent analysis of hemoglobin derivatives with a reversed-optics spectrophotometer. Clin Chem 30:373-379
    • (1984) Clin Chem , vol.30 , pp. 373-379
    • Zwart, A.1    Buursma, A.2    Van Kampen, E.J.3    Zijlstra, W.G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.