Three-state thermal unfolding of onconase

被引：4
作者：
Casares-Atienza, Salvador [1 ]
Weininger, Ulrich [2 ]
Camara-Artigas, Ana [3 ]
Balbach, Jochen [2 ]
Garcia-Mira, Maria M. [1 ]
机构：
[1] Univ Granada, Fac Ciencias, Dept Quim Fis, E-18071 Granada, Spain
[2] Univ Halle Wittenberg, Inst Phys, D-06120 Halle, Saale, Germany
[3] Univ Almeria, Dept Quim Fis Bioquim & Quim Inorgan, Almeria 04120, Spain
来源：
BIOPHYSICAL CHEMISTRY | 2011年 / 159卷 / 2-3期
关键词：
Onconase; Protein folding; Thermal unfolding; Folding equilibrium intermediate; Differential scanning calorimetry; HEAT-CAPACITY; SELECTIVE DEGRADATION; MOLTEN GLOBULE; STABLE PROTEIN; RIBONUCLEASE-A; SH3; DOMAIN; INTERMEDIATE; STABILITY; PH; CELLS;
D O I：
10.1016/j.bpc.2011.07.005
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
Onconase is a member of the ribonuclease A superfamily currently in phase IIIb clinical trials as a treatment for malign mesothelioma due to its cytotoxic activity selective against tumor-cells. In this work, we have studied the equilibrium thermal unfolding of onconase using a combination of several structural and biophysical techniques. Our results indicate that at least one significantly populated intermediate, which implies the exposure of hydrophobic surface and significant changes in the environment around Trp3, occurs during the equilibrium unfolding process of this protein. The intermediate begins to populate at about 30 degrees below the global unfolding temperature, reaching a maximum population of nearly 60%, 10 degrees below the global unfolding temperature. (C) 2011 Elsevier B.V. All rights reserved.
引用
收藏
页码：267 / 274
页数：8
相关论文
共 50 条
  • [21] Three-state protein folding: Experimental determination of free-energy profile
    Baryshnikova, EN
    Melnik, BS
    Finkelstein, AV
    Semisotnov, GV
    Bychkova, VE
    [J]. PROTEIN SCIENCE, 2005, 14 (10) : 2658 - 2667
  • [22] A Spectroscopic Study on Secondary Structure and Thermal Unfolding of the Plant Toxin Gelonin Confirms Some Typical Structural Characteristics and Unravels the Sequence of Thermal Unfolding Events
    Scire, Andrea
    Tanfani, Fabio
    Ausili, Alessio
    [J]. TOXINS, 2019, 11 (09)
  • [23] Thermal unfolding of calreticulin. Structural and thermodynamic characterization of the transition
    Decca, Maria B.
    Borioli, Graciela A.
    Durand, Edith S.
    Moreschi, Alejandro
    Hallak, Marta E.
    Montich, Guillermo G.
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2019, 1867 (03): : 175 - 183
  • [24] The pH dependence of staphylococcal nuclease stability is incompatible with a three-state denaturation model
    Spencer, Daniel
    Garcia-Moreno E, Bertrand
    Stites, Wesley E.
    [J]. BIOPHYSICAL CHEMISTRY, 2013, 180 : 86 - 94
  • [25] Thermal unfolding of ribonuclease A in phosphate at neutral pH: Deviations from the two-state model
    Stelea, SD
    Pancoska, P
    Benight, AS
    Keiderling, TA
    [J]. PROTEIN SCIENCE, 2001, 10 (05) : 970 - 978
  • [26] Thermal unfolding mechanism of lipocalin-type prostaglandin D synthase
    Iida, Tsukimi
    Nishimura, Shigenori
    Mochizuki, Maki
    Uchiyama, Susumu
    Ohkubo, Tadayasu
    Urade, Yoshihiro
    Tanaka, Akiyoshi
    Inui, Takashi
    [J]. FEBS JOURNAL, 2008, 275 (02) : 233 - 241
  • [27] Three-state model for lysozyme folding: Triangular folding mechanism with an energetically trapped intermediate
    Wildegger, G
    Kiefhaber, T
    [J]. JOURNAL OF MOLECULAR BIOLOGY, 1997, 270 (02) : 294 - 304
  • [28] Three Weaknesses for Three Perturbations: Comparing Protein Unfolding Under Shear, Force, and Thermal Stresses
    Languin-Cattoen, Olivier
    Melchionna, Simone
    Derreumaux, Philippe
    Stirnemann, Guillaume
    Sterpone, Fabio
    [J]. JOURNAL OF PHYSICAL CHEMISTRY B, 2018, 122 (50) : 11922 - 11930
  • [29] Thermal unfolding of homodimers and heterodimers of different skeletal-muscle isoforms of tropomyosin
    Matyushenko, Alexander M.
    Kleymenov, Sergey Y.
    Susorov, Denis S.
    Levitsky, Dmitrii I.
    [J]. BIOPHYSICAL CHEMISTRY, 2018, 243 : 1 - 7
  • [30] Secondary structure length as a determinant of folding rate of proteins with two- and three-state kinetics
    Huang, Ji-Tao
    Cheng, Jin-Pei
    Chen, Hui
    [J]. PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2007, 67 (01) : 12 - 17
12345