Warning: Undefined array key "mm" in /www/wwwroot/www.ai-bt.com/si.php on line 10 Deprecated: trim(): Passing null to parameter #1 ($string) of type string is deprecated in /www/wwwroot/www.ai-bt.com/si.php on line 10 Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin.

Literature DB >> 8599758

Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin.

C G Genzor, A Perales-Alcón, J Sancho, A Romero.

Abstract

Entities: Chemical

Mesh：

Substances：

Year: 1996 PMID： 8599758 DOI： 10.1038/nsb0496-329

Source DB: PubMed Journal: Nat Struct Biol ISSN： 1072-8368

Keyword Cloud
Cited

× No keyword cloud information.

23 in total

1. Energetics of aliphatic deletions in protein cores.

Authors: Marta Bueno; Luis A Campos; Jorge Estrada; Javier Sancho
Journal: Protein Sci Date: 2006-08 Impact factor: 6.725

2. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin.

Authors: Loren Stagg; Shao-Qing Zhang; Margaret S Cheung; Pernilla Wittung-Stafshede
Journal: Proc Natl Acad Sci U S A Date: 2007-11-16 Impact factor: 11.205

3. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.

Authors: Rakhi Agarwal; Jeffrey B Bonanno; Stephen K Burley; Subramanyam Swaminathan
Journal: Acta Crystallogr D Biol Crystallogr Date: 2006-03-18

4. Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin.

Authors: Dirar Homouz; Loren Stagg; Pernilla Wittung-Stafshede; Margaret S Cheung
Journal: Biophys J Date: 2009-01 Impact factor: 4.033

5. Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme.

Authors: Adam V Crain; Joan B Broderick
Journal: Biochim Biophys Acta Date: 2013-09-07

Closure of a tyrosine/tryptophan aromatic gate leads to a compact fold in apo flavodoxin.

1. Energetics of aliphatic deletions in protein cores.

2. Molecular crowding enhances native structure and stability of alpha/beta protein flavodoxin.

3. Structure determination of an FMN reductase from Pseudomonas aeruginosa PA01 using sulfur anomalous signal.

4. Macromolecular crowding modulates folding mechanism of alpha/beta protein apoflavodoxin.

5. Flavodoxin cofactor binding induces structural changes that are required for protein-protein interactions with NADP(+) oxidoreductase and pyruvate formate-lyase activating enzyme.

6. Cofactor-induced reversible folding of Flavodoxin-4 from Lactobacillus acidophilus.

7. Conformational stability of apoflavodoxin.

8. Structural insight into the high reduction potentials observed for Fusobacterium nucleatum flavodoxin.

9. Femtosecond dynamics of short-range protein electron transfer in flavodoxin.

10. The flavodoxin from Helicobacter pylori: structural determinants of thermostability and FMN cofactor binding.