Use of limited proteolysis to identify protein domains suitable for structural analysis

被引：16

作者：

Koth, CM

Orlicky, SM

Larson, SM

Edwards, AM

机构：

[1] Univ Toronto, Charles H Best Inst, Banting & Best Dept Med Res, Toronto, ON M5G 1L6, Canada

[2] Mt Sinai Hosp, Samuel Lunenfeld Res Inst, Program Mol Biol & Canc, Toronto, ON M5G 1X5, Canada

[3] Stanford Univ, Dept Biol Struct, Biophys Program, Stanford, CA 94305 USA

来源：

MACROMOLECULAR CRYSTALLOGRAPHY, PT C | 2003年 / 368卷

关键词：

D O I：

10.1016/S0076-6879(03)68005-5

中图分类号：

Q5 [生物化学];

学科分类号：

071010 ; 081704 ;

摘要：

[No abstract available]

引用

页码：77 / 84

页数：8

共 15 条

[11] ELECTROSPRAY MASS-SPECTROMETRY FOR PROTEIN CHARACTERIZATION [J].

MANN, M ;

WILM, M .

TRENDS IN BIOCHEMICAL SCIENCES, 1995, 20 (06) :219-224

[12] Yeast transcript elongation factor (TFIIS), structure and function - I: NMR structural analysis of the minimal transcriptionally active region [J].

Olmsted, VK ;

Awrey, DE ;

Koth, C ;

Shan, X ;

Morin, PE ;

Kazanis, S ;

Edwards, AM ;

Arrowsmith, CH .

JOURNAL OF BIOLOGICAL CHEMISTRY, 1998, 273 (35) :22589-22594

[13]

Pfuetzner RA, 1997, J BIOL CHEM, V272, P430

[14] 100,000 protein structures for the biologist [J].

Andrej Šali .

Nature Structural Biology, 1998, 5 (12) :1029-1032

[15] Assessing annotation transfer for genomics: Quantifying the relations between protein sequence, structure and function through traditional and probabilistic scores [J].

Wilson, CA ;

Kreychman, J ;

Gerstein, M .

JOURNAL OF MOLECULAR BIOLOGY, 2000, 297 (01) :233-249

← 1 2 →