Evolution of fold switching in a metamorphic protein

Autor: Brian F. Volkman, Kenneth E. Prehoda, Acacia F. Dishman, Andrew B. Kleist, M. Madan Babu, Francis C. Peterson, Robert C. Tyler, Jamie C. Fox

Publikováno v: Science (New York, N.Y.). 371(6524)

One sequence encoding two structures Most proteins have stable, folded structures, but there are rare examples of metamorphic proteins that can switch between two different folds that may each have a different function. Dishman et al. investigated th

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::316c63615f078fe65c38d859da30f43a
https://pubmed.ncbi.nlm.nih.gov/33752957

Solution NMR spectroscopy of GPCRs: Residue-specific labeling strategies with a focus on

Autor: Andrew B, Kleist, Francis, Peterson, Robert C, Tyler, Martin, Gustavsson, Tracy M, Handel, Brian F, Volkman

Publikováno v: Methods in cell biology. 149

The past decade has witnessed remarkable progress in the determination of G protein-coupled receptor (GPCR) structures, profoundly expanding our understanding of how GPCRs recognize ligands, undergo activation, and interact with intracellular signali

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=pmid________::c39dfbadfdcdf59e56e7fc0114a14ff7
https://pubmed.ncbi.nlm.nih.gov/30616824

A Requirement for Metamorphic Interconversion in the Antimicrobial Activity of Chemokine XCL1

Autor: Jazma L. Tapia, Akshay Subramanian, Amanda M. Nevins, Robert C. Tyler, Davin R. Jensen, David P. Delgado, Brian F. Volkman, Andre J. Ouellette

Publikováno v: Biochemistry. 55:3784-3793

Chemokines make up a superfamily of ∼50 small secreted proteins (8-12 kDa) involved in a host of physiological processes and disease states, with several previously shown to have direct antimicrobial activity comparable to that of defensins in effi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ad897e79ea70b87e494f99f9a22ef6a2
https://doi.org/10.1021/acs.biochem.6b00353

Electron capture dissociation and drift tube ion mobility-mass spectrometry coupled with site directed mutations provide insights into the conformational diversity of a metamorphic protein

Autor: Robert C. Tyler, Massimiliano Porrini, Cait E. MacPhee, Perdita E. Barran, Brian F. Volkman, Sophie R. Harvey

Publikováno v: Harvey, S R, Porrini, M, Tyler, R C, MacPhee, C E, Volkman, B F & Barran, P E 2015, ' Electron capture dissociation and drift tube ion mobility-mass spectrometry coupled with site directed mutations provide insights into the conformational diversity of a metamorphic protein ', Physical Chemistry Chemical Physics, vol. 17, no. 16, pp. 10538-10550 . https://doi.org/10.1039/c4cp05136j

Ion mobility mass spectrometry can be combined with data from top-down sequencing to discern adopted conformations of proteins in the absence of solvent. This multi-technique approach has particular applicability for conformationally dynamic systems.

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::577b749ad6cfeb36b93592f2ee536472
https://doi.org/10.1039/c4cp05136j

Electrostatic Optimization of the Conformational Energy Landscape in a Metamorphic Protein

Autor: Brian F. Volkman, Francis C. Peterson, Robert C. Tyler, Jamie C. Wieting

Publikováno v: Biochemistry. 51:9067-9075

The equilibrium unfolding reaction of Ltn, a metamorphic C-class chemokine, was monitored by tryptophan fluorescence to determine unfolding free energies. Measurements revealed that addition of 150 mM NaCl stabilized the Ltn chemokine fold by approxi

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::2c6803e16fb98e6769502843f62b307c
https://doi.org/10.1021/bi300842j