Unusual Cold Denaturation of a Small Protein Domain

Biochemistry ◽  
2012 ◽  
Vol 51 (33) ◽  
pp. 6496-6498 ◽  
Author(s):  
Ginka S. Buchner ◽  
Natalie Shih ◽  
Amy E. Reece ◽  
Stephan Niebling ◽  
Jan Kubelka
Keyword(s):  
Protein Domain ◽  
Small Protein ◽  
Cold Denaturation

scholarly journals Cold Denaturation in a Small Protein Domain

2012 ◽  
Vol 102 (3) ◽  
pp. 454a
Author(s):  
Ginka Buchner ◽  
Natalie Shih ◽  
Jan Kubelka
Keyword(s):  
Protein Domain ◽  
Small Protein ◽  
Cold Denaturation

scholarly journals Phosphorylation Induced Global Structural Destabilization of a Small Protein Domain

2017 ◽  
Vol 112 (3) ◽  
pp. 58a-59a
Author(s):  
Ashleigh Bachman ◽  
Radwan Ebna Noor ◽  
Dimitra Keramisanou ◽  
Ioannis Gelis
Keyword(s):  
Protein Domain ◽  
Small Protein

Covariation of backbone motion throughout a small protein domain

2003 ◽  
Vol 10 (11) ◽  
pp. 962-965 ◽  
Author(s):  
Kristen L Mayer ◽  
Matthew R Earley ◽  
Sonia Gupta ◽  
Kumar Pichumani ◽  
Lynne Regan ◽  
...  
Keyword(s):  
Protein Domain ◽  
Small Protein

scholarly journals Identification of a small protein domain present in all plant lineages that confers high prephenate dehydratase activity

2016 ◽  
Vol 87 (2) ◽  
pp. 215-229 ◽  
Author(s):  
Jorge El-Azaz ◽  
Fernando de la Torre ◽  
Concepción Ávila ◽  
Francisco M. Cánovas
Keyword(s):  
Protein Domain ◽  
Small Protein ◽  
Prephenate Dehydratase ◽  
Dehydratase Activity

Self-Assembling Micelles Based on an Intrinsically Disordered Protein Domain

2018 ◽  
Author(s):  
Sarah Klass ◽  
Matthew J. Smith ◽  
Tahoe Fiala ◽  
Jessica Lee ◽  
Anthony Omole ◽  
...  
Keyword(s):  
Drug Delivery ◽  
Fusion Proteins ◽  
Organic Molecules ◽  
Intrinsically Disordered Protein ◽  
Protein Domain ◽  
Enzymatic Cleavage ◽  
Intrinsically Disordered ◽  
Disordered Protein ◽  
Self Assembling ◽  
Protein Tag

Herein, we describe a new series of fusion proteins that have been developed to self-assemble spontaneously into stable micelles that are 27 nm in diameter after enzymatic cleavage of a solubilizing protein tag. The sequences of the proteins are based on a human intrinsically disordered protein, which has been appended with a hydrophobic segment. The micelles were found to form across a broad range of pH, ionic strength, and temperature conditions, with critical micelle concentration (CMC) values below 1 µM being observed in some cases. The reported micelles were found to solubilize hydrophobic metal complexes and organic molecules, suggesting their potential suitability for catalysis and drug delivery applications.

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