scholarly journals Engineering a de novo designed coiled-coil heterodimerization domain for the rapid detection, purification and characterization of recombinantly expressed peptides and proteins

1997 ◽  
Vol 10 (3) ◽  
pp. 299-299 ◽  
Author(s):  
B. Tripet ◽  
L. Yu ◽  
D. L. Bautista ◽  
W. Y. Wong ◽  
R. T. Irvin ◽  
...  
2005 ◽  
Vol 3 (7) ◽  
pp. 1189 ◽  
Author(s):  
Kevin Pagel ◽  
Karsten Seeger ◽  
Bettina Seiwert ◽  
Alessandra VillaCurrent address: J. W. Goethe ◽  
Alan E. Mark ◽  
...  

2001 ◽  
Vol 29 (4) ◽  
pp. 559-564 ◽  
Author(s):  
J. D. Lear ◽  
H. Gratkowski ◽  
W. F. DeGrado

Our current level of understanding of membrane-protein folding is primitive, but it is beginning to advance. Previously [Choma, Gratkowski, Lear and DeGrado (2000) Nat. Struct. Biol. 7, 161–166], we described studies of the association in detergent micelles of short, simple-sequence hydrophobic peptides modified from the sequence of the water-soluble, homodimeric coiled-coil GCN4-P1 peptide using the principle that the interiors of membrane proteins are similar to those of water-soluble proteins. Here, we discuss more quantitative aspects of the association equilibrium and compare the free energies of association of a number of mutant peptides designed to explore specific features responsible for the association.


2021 ◽  
Author(s):  
Jason Z Zhang ◽  
Hsien-Wei Yeh ◽  
Alexandra C Walls ◽  
Basile IM Wicky ◽  
Kaiti Sprouse ◽  
...  

With global vaccination efforts against SARS-CoV-2 underway, there is a need for rapid quantification methods for neutralizing antibodies elicited by vaccination and characterization of their strain dependence. Here, we describe a designed protein biosensor that enables sensitive and rapid detection of neutralizing antibodies against wild type and variant SARS-CoV-2 in serum samples. More generally, our thermodynamic coupling approach can better distinguish sample to sample differences in analyte binding affinity and abundance than traditional competition based assays.


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