Do Protein Molecules Have a Native-Like Topology in the Pre-molten Globule State?

被引:0
|
作者
Inst for Biological Instrumentation, Russian Academy of Sciences, Pushchino, Moscow Region, 142292, Russia [1 ]
不详 [2 ]
机构
来源
Biochemistry Moscow | / 5卷 / 552-555期
关键词
D O I
暂无
中图分类号
学科分类号
摘要
引用
收藏
相关论文
共 50 条
  • [41] A guide to quantifying membrane protein dynamics in lipids and other native-like environments by solution-state NMR spectroscopy
    Bibow, Stefan
    Hiller, Sebastian
    FEBS JOURNAL, 2019, 286 (09) : 1610 - 1623
  • [42] Independent of Their Localization in Protein the Hydrophobic Amino Acid Residues Have No Effect on the Molten Globule State of Apomyoglobin and the Disulfide Bond on the Surface of Apomyoglobin Stabilizes This Intermediate State
    Melnik, Tatiana N.
    Majorina, Maria A.
    Larina, Daria S.
    Kashparov, Ivan A.
    Samatova, Ekaterina N.
    Glukhov, Anatoly S.
    Melnik, Bogdan S.
    PLOS ONE, 2014, 9 (06):
  • [43] Influence of Pre-/Postultrasound on Forming a Molten Globule-Like Conformation and Improving the Emulsifying Properties of Thermally Induced Soybean Protein Aggregates
    Huang, Zhaoxian
    Liu, Zelong
    An, Ran
    Guo, Zengwang
    Wang, Zhongjiang
    Jiang, Lianzhou
    ACS FOOD SCIENCE & TECHNOLOGY, 2021, 1 (09): : 1514 - 1522
  • [44] The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    Kragelund B.B.
    Osmark P.
    Neergaard T.B.
    Schiødt J.
    Kristiansen K.
    Knudsen J.
    Poulsen F.M.
    Nature Structural Biology, 1999, 6 (6) : 594 - 601
  • [45] Native-like beta-structure in a trifluoroethanol-induced partially folded state of the all-beta-sheet protein tendamistat
    Schonbrunner, N
    Wey, J
    Engels, J
    Georg, H
    Kiefhaber, T
    JOURNAL OF MOLECULAR BIOLOGY, 1996, 260 (03) : 432 - 445
  • [46] The formation of a native-like structure containing eight conserved hydrophobic residues is rate limiting in two-state protein folding of ACBP
    Kragelund, BB
    Osmark, P
    Neergaard, TB
    Schiodt, J
    Kristiansen, K
    Knudsen, J
    Poulsen, FM
    NATURE STRUCTURAL BIOLOGY, 1999, 6 (06): : 594 - 601
  • [47] Molten globule-like state of peanut lectin monomer retains its carbohydrate specificity - Implications in protein folding and legume lectin oligomerization
    Reddy, GB
    Srinivas, VR
    Ahmad, N
    Surolia, A
    JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (08) : 4500 - 4503
  • [48] THE STRUCTURE OF THE TRANSITION-STATE FOR THE ASSOCIATION OF 2 FRAGMENTS OF THE BARLEY CHYMOTRYPSIN INHIBITOR-2 TO GENERATE NATIVE-LIKE PROTEIN - IMPLICATIONS FOR MECHANISMS OF PROTEIN-FOLDING
    GAY, GD
    RUIZSANZ, J
    DAVIS, B
    FERSHT, AR
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1994, 91 (23) : 10943 - 10946
  • [49] Conformational folding and stability of the HET-C2 glycolipid transfer protein fold: Does a molten globule-like state regulate activity?
    Hormel Institute, University of Minnesota, Austin, MN 55912, United States
    不详
    不详
    不详
    不详
    Biochemistry, 23 (5163-5171):
  • [50] Conformational Folding and Stability of the HET-C2 Glycolipid Transfer Protein Fold: Does a Molten Globule-like State Regulate Activity?
    Kenoth, Roopa
    Kamlekar, Ravi Kanth
    Simanshu, Dhirendra K.
    Gao, Yongguang
    Malinina, Lucy
    Prendergast, Franklyn G.
    Molotkovsky, Julian G.
    Patel, Dinshaw J.
    Venyaminov, Sergei Y.
    Brown, Rhoderick E.
    BIOCHEMISTRY, 2011, 50 (23) : 5163 - 5171