Author

W. N. Zagotta

Listed by name: these papers carry no ORCID for this author, so different people with the same name may be mixed together.

Biology Disciplines

Click to filter author papers

Biophysics· 5 Biochemistry· 3

Signature Assays, Organisms & Methods

Click to filter · or open tag

Approach:experimental assay· 7 Research Focus:protein folding & dynamics· 6 Assay:fluorescence / live-cell microscopy· 3 Organism:human· 2 Assay:proteomics· 2 Approach:biophysical modeling· 1 Research Focus:cell signaling & trafficking· 1 Research Focus:cell type annotation· 1

Frequent Co-Authors

S. E. Gordon· 6 shared E. G. Evans· 3 shared J. Petersson· 3 shared R. A. Mehl· 3 shared S. Stoll· 3 shared C. M. Jones· 2 shared F. DiMaio· 2 shared G. Dai· 2 shared

Activity by Year

2018-2023 · peak 3/yr

Co-Author Collaboration Network

10 top collaborators · 22 mutual co-author links

Click any collaborator node to inspect or filter shared papers

Focal author (center)Selected co-authorORCID co-authorUnlinked name

Curved chords = mutual co-authorship

6 shared papersBiophysics

S. E. Gordon

Mutual co-authors in cluster

Author profile →

8 papers

Recent·Most cited

Long-distance tmFRET using bipyridyl- and phenanthroline-based ligands

S. E. Gordon, E. G. Evans, S. C. Otto, M. Tessmer, K. D. Shaffer, M. T. Gordon, J. Petersson, S. Stoll, W. N. Zagotta

This paper expands the working distance of tmFRET to 50 Å using new ligands, enabling precise measurement of conformational changes in maltose binding protein under physiological conditions.

bioRxiv · Oct 9, 2023Biophysics

Measuring conformational equilibria in allosteric proteins with time-resolved tmFRET

W. N. Zagotta, E. G. Evans, P. Eggan, M. Tessmer, K. D. Shaffer, J. Petersson, S. Stoll, S. E. Gordon

This paper develops a fluorescence method to measure protein conformational dynamics and energetics using time-resolved tmFRET and validates it with EPR spectroscopy.

bioRxiv · Oct 9, 2023Biophysics

Ultra-Fast Bioorthogonal Spin-Labeling and Distance Measurements in Mammalian Cells Using Small, Genetically Encoded Tetrazine Amino Acids

S. Jana, E. G. B. Evans, H. S. Jang, S. Zhang, H. Zhang, A. Rajca, S. E. Gordon, W. N. Zagotta, S. Stoll, R. A. Mehl

This paper introduces a fast bioorthogonal reaction system for in-cell spin-labeling and DEER spectroscopy, enabling structural studies of proteins in live mammalian cells.

bioRxiv · Jan 26, 2023 · PreprintBiochemistry

An improved fluorescent noncanonical amino acid for measuring conformational distributions using time-resolved transition metal ion FRET

W. N. Zagotta, B. S. Sim, A. K. Nhim, M. M. Raza, E. G. Evans, Y. Venkatesh, C. M. Jones, R. A. Mehl, J. Petersson, S. E. Gordon

This paper introduces an improved fluorescent noncanonical amino acid, Acd, for time-resolved tmFRET to measure conformational distributions in proteins.

bioRxiv · May 10, 2021Biophysics

Genetic Encoding of a Highly Photostable, Long Lifetime Fluorescent Amino Acid for Imaging in Mammalian Cells

C. M. Jones, D. M. Robkis, R. J. Blizzard, M. Munari, Y. Venkatesh, T. S. Mihaila, A. J. Eddins, R. A. Mehl, W. N. Zagotta, S. E. Gordon, E. J. Petersson

The paper introduces a genetically encodable fluorescent amino acid, Acd, with superior photostability and long fluorescence lifetime for use in FLIM and protein studies.

bioRxiv · Apr 5, 2021Biochemistry

NONCANONICAL ELECTROMECHANICAL COUPLING MECHANISM OF AN HCN CHANNEL

G. Dai, T. K. Aman, F. DiMaio, W. N. Zagotta

The paper investigates the structural rearrangements in spHCN channels during activation and inactivation, revealing a noncanonical electromechanical coupling mechanism involving the A helix and cAMP binding.

bioRxiv · Jan 6, 2021 · PreprintBiophysics

The HCN Channel Voltage Sensor Undergoes A Large Downward Motion During Hyperpolarization

G. Dai, T. K. Aman, F. DiMaio, W. N. Zagotta

This study measures the movement of the HCN channel's S4 helix during hyperpolarization using tmFRET and reveals a significant downward motion and tilting, providing insights into reverse gating mechanisms.

bioRxiv · Jan 16, 2019Biophysics

Visualizing conformational dynamics of proteins in solution and at the cell membrane

S. E. Gordon, M. Munari, W. N. Zagotta

This paper introduces ACCuRET, a method for measuring conformational dynamics in proteins with high precision, applicable to both soluble and membrane proteins.

bioRxiv · Apr 3, 2018Biochemistry