STRUCTURE, STABILITY, AND FOLDING OF STAPHYLOCOCCAL NUCLEASE

被引:0
|
作者
ULRICH, EL [1 ]
ALEXANDRESCU, AT [1 ]
GRISSOM, CB [1 ]
MILLS, DA [1 ]
MARKLEY, JL [1 ]
机构
[1] UNIV WISCONSIN,MADISON,WI 53706
关键词
D O I
暂无
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
引用
收藏
页码:220 / 220
页数:1
相关论文
共 50 条
  • [41] Inhibitor Binding Increases the Mechanical Stability of Staphylococcal Nuclease
    Wang, Chien-Chung
    Tsong, Tian-Yow
    Hsu, Yau-Heiu
    Marszalek, Piotr E.
    BIOPHYSICAL JOURNAL, 2011, 100 (04) : 1094 - 1099
  • [42] Mechanism of induced folding: Both folding before binding and binding before folding can be realized in staphylococcal nuclease mutants
    Onitsuka, Masayoshi
    Kamikubo, Hironari
    Yamazaki, Yoichi
    Kataoka, Mikio
    PROTEINS-STRUCTURE FUNCTION AND BIOINFORMATICS, 2008, 72 (03) : 837 - 847
  • [43] Folding kinetics of staphylococcal nuclease studied by tryptophan engineering and rapid mixing methods
    Maki, Kosuke
    Cheng, Hong
    Dolgikh, Dimitry A.
    Roder, Heinrich
    JOURNAL OF MOLECULAR BIOLOGY, 2007, 368 (01) : 244 - 255
  • [44] Kinetic construction of a modular assembly model for staphylococcal nuclease (SNase) folding.
    Tsong, TY
    Su, ZD
    BIOPHYSICAL JOURNAL, 2000, 78 (01) : 165A - 165A
  • [45] Modular assembly revealed by tryptophan and other optical probes in Staphylococcal nuclease folding
    Su, ZD
    Wu, JM
    Tsong, TY
    Chen, HM
    JOURNAL OF THE CHINESE CHEMICAL SOCIETY, 2004, 51 (5B) : 1099 - 1106
  • [46] Multiple parallel-pathway folding of proline-free staphylococcal nuclease
    Kamagata, K
    Sawano, Y
    Tanokura, M
    Kuwajima, K
    JOURNAL OF MOLECULAR BIOLOGY, 2003, 332 (05) : 1143 - 1153
  • [47] Least activation path for protein folding: Investigation of staphylococcal nuclease folding by stopped-flow circular dichroism
    Su, ZD
    Arooz, MT
    Chen, HM
    Gross, CJ
    Tsong, TY
    PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1996, 93 (06) : 2539 - 2544
  • [48] PATTERNS OF NONADDITIVITY BETWEEN PAIRS OF STABILITY MUTATIONS IN STAPHYLOCOCCAL NUCLEASE
    GREEN, SM
    SHORTLE, D
    BIOCHEMISTRY, 1993, 32 (38) : 10131 - 10139
  • [49] Does proline isomerization shape the folding funnel of the wild type and mutant staphylococcal nuclease?
    Tsong, TY
    Su, ZD
    BIOLOGICAL PHYSICS, 1999, 487 : 37 - 53
  • [50] THE PRO117 TO GLYCINE MUTATION OF STAPHYLOCOCCAL NUCLEASE SIMPLIFIES THE UNFOLDING FOLDING KINETICS
    KUWAJIMA, K
    OKAYAMA, N
    YAMAMOTO, K
    ISHIHARA, T
    SUGAI, S
    FEBS LETTERS, 1991, 290 (1-2): : 135 - 138