- Home
- Search Results
- Page 1 of 1
Search for: All records
-
Total Resources2
- Resource Type
-
0000000002000000
- More
- Availability
-
11
- Author / Contributor
- Filter by Author / Creator
-
-
Ahmed, Wylie W (1)
-
Ahmed, Wylie W. (1)
-
Bobilev, Keren (1)
-
Dalal, Shibani (1)
-
Gomez, Mauricio (1)
-
Hayakawa, Daichi (1)
-
Ikonen, Eden (1)
-
Murphy, Ian (1)
-
Rogers, W Benjamin (1)
-
Rogers, W. Benjamin (1)
-
Ross, Jennifer L (1)
-
Ross, Jennifer L. (1)
-
Seyforth, Hunter (1)
-
Videbæk, Thomas E (1)
-
#Tyler Phillips, Kenneth E. (0)
-
#Willis, Ciara (0)
-
& Abreu-Ramos, E. D. (0)
-
& Abramson, C. I. (0)
-
& Abreu-Ramos, E. D. (0)
-
& Adams, S.G. (0)
-
- Filter by Editor
-
-
Signore, Giovanni (1)
-
& Spizer, S. M. (0)
-
& . Spizer, S. (0)
-
& Ahn, J. (0)
-
& Bateiha, S. (0)
-
& Bosch, N. (0)
-
& Brennan K. (0)
-
& Brennan, K. (0)
-
& Chen, B. (0)
-
& Chen, Bodong (0)
-
& Drown, S. (0)
-
& Ferretti, F. (0)
-
& Higgins, A. (0)
-
& J. Peters (0)
-
& Kali, Y. (0)
-
& Ruiz-Arias, P.M. (0)
-
& S. Spitzer (0)
-
& Sahin. I. (0)
-
& Spitzer, S. (0)
-
& Spitzer, S.M. (0)
-
-
Have feedback or suggestions for a way to improve these results?
!
Note: When clicking on a Digital Object Identifier (DOI) number, you will be taken to an external site maintained by the publisher.
Some full text articles may not yet be available without a charge during the embargo (administrative interval).
What is a DOI Number?
Some links on this page may take you to non-federal websites. Their policies may differ from this site.
-
Signore, Giovanni (Ed.)Attaching enzymes to nanostructures has proven useful to the study of enzyme functionality under controlled conditions and has led to new technologies. Often, the utility and interest of enzyme-tethered nanostructures lie in how the enzymatic activity is affected by how the enzymes are arranged in space. Therefore, being able to conjugate enzymes to nanostructures while preserving the enzymatic activity is essential. In this paper, we present a method to conjugate single-stranded DNA to the enzyme urease while maintaining enzymatic activity. We show evidence of successful conjugation and quantify the variables that affect the conjugation yield. We also show that the enzymatic activity is unchanged after conjugation compared to the enzyme in its native state. Finally, we demonstrate the tethering of urease to nanostructures made using DNA origami with high site-specificity. Decorating nanostructures with enzymatically-active urease may prove to be useful in studying, or even utilizing, the functionality of urease in disciplines ranging from biotechnology to soft-matter physics. The techniques we present in this paper will enable researchers across these fields to modify enzymes without disrupting their functionality, thus allowing for more insightful studies into their behavior and utility.more » « lessFree, publicly-accessible full text available April 21, 2026
-
Seyforth, Hunter; Gomez, Mauricio; Rogers, W. Benjamin; Ross, Jennifer L.; Ahmed, Wylie W. (, Physical Review Research)
An official website of the United States government
