Proline replacements and the simplification of the complex, parallel channel folding mechanism of the alpha subunit of Trp synthase, a TIM barrel protein

被引：0

作者：

Wu, Y ^{[1
]}

Matthews, CR ^{[1
]}

机构：

[1] Univ Massachusetts, Sch Med, Worcester, MA 01605 USA

来源：

BIOPHYSICAL JOURNAL | 2003年 / 84卷 / 02期

关键词：

D O I：

暂无

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

引用

页码：161A / 161A

页数：1

共 10 条

[1] Proline replacements and the simplification of the complex, parallel channel folding mechanism for the alpha subunit of Trp synthase, a TIM barrel protein
Wu, Y
Matthews, CR
JOURNAL OF MOLECULAR BIOLOGY, 2003, 330 (05) : 1131 - 1144
[2] Parallel channels and rate-limiting steps in complex protein folding reactions: Prolyl isomerization and the alpha subunit of Trp synthase, a TIM barrel protein
Wu, Y
Matthews, CR
JOURNAL OF MOLECULAR BIOLOGY, 2002, 323 (02) : 309 - 325
[3] A cis-prolyl peptide bond isomerization dominates the folding of the alpha subunit of trp synthase, a TIM barrel protein
Wu, Y
Matthews, CR
JOURNAL OF MOLECULAR BIOLOGY, 2002, 322 (01) : 7 - 13
[4] An obligatory intermediate controls the folding of the α-subunit of tryptophan synthase, a TIM barrel protein
Wintrode, PL
Rojsajjakul, T
Vadrevu, R
Matthews, CR
Smith, DL
JOURNAL OF MOLECULAR BIOLOGY, 2005, 347 (05) : 911 - 919
[5] Specific structure appears at the N terminus in the sub-millisecond folding intermediate of the alpha subunit of tryptophan synthase, a TIM barrel protein
Wu, Y
Vadrevu, R
Yang, XY
Matthews, CR
JOURNAL OF MOLECULAR BIOLOGY, 2005, 351 (03) : 445 - 452
[6] NMR analysis of partially folded states and persistent structure in the alpha subunit of tryptophan synthase: Implications for the equilibrium folding mechanism of a 29-kDa TIM barrel protein
Vadrevu, Ramakrishna
Wu, Ying
Matthews, C. Robert
JOURNAL OF MOLECULAR BIOLOGY, 2008, 377 (01) : 294 - 306
[7] Folding mechanism of the α-subunit of tryptophan synthase, an α/β barrel protein:: Global analysis highlights the interconversion of multiple native, intermediate, and unfolded forms through parallel channels
Bilsel, O
Zitzewitz, JA
Bowers, KE
Matthews, CR
BIOCHEMISTRY, 1999, 38 (03) : 1018 - 1029
[8] A tightly packed hydrophobic cluster directs the formation of an off-pathway sub-millisecond folding intermediate in the α subunit of tryptophan synthase, a TIM barrel protein
Wu, Ying
Vadrevu, Ramakrishna
Kathuria, Sagar
Yang, Xiaoyan
Matthews, C. Robert
JOURNAL OF MOLECULAR BIOLOGY, 2007, 366 (05) : 1624 - 1638
[9] Multi-state unfolding of the alpha subunit of tryptophan synthase, a TIM barrel protein: Insights into the secondary structure of the stable equilibrium intermediates by hydrogen exchange mass spectrometry
Rojsajjakul, T
Wintrode, PL
Vadrevu, R
Matthews, CR
Smith, DL
JOURNAL OF MOLECULAR BIOLOGY, 2004, 341 (01) : 241 - 253
[10] Topology and sequence in the folding of a TIM barrel protein:: Global analysis highlights partitioning between transient off-pathway and stable on-pathway folding intermediates in the complex folding mechanism of a (βα)8 barrel of unknown function from B-subtilis
Forsyth, William R.
Bilsel, Osman
Gu, Zhenyu
Matthews, C. Robert
JOURNAL OF MOLECULAR BIOLOGY, 2007, 372 (01) : 236 - 253

← 1 →