K
Karl A.T. Makepeace
Researcher at University of Victoria
Publications - 15
Citations - 464
Karl A.T. Makepeace is an academic researcher from University of Victoria. The author has contributed to research in topics: Chaperone (protein) & Mass spectrometry. The author has an hindex of 11, co-authored 15 publications receiving 378 citations.
Papers
More filters
Journal ArticleDOI
Structure of EspB from the ESX-1 Type VII Secretion System and Insights into its Export Mechanism.
Matthew Solomonson,Dheva Setiaputra,Karl A.T. Makepeace,Emilie Lameignere,Evgeniy V. Petrotchenko,Deborah G. Conrady,Julien R. C. Bergeron,Marija Vuckovic,Frank DiMaio,Christoph H. Borchers,Calvin K. Yip,Natalie C. J. Strynadka +11 more
TL;DR: It is demonstrated that EspB adopts a PE/PPE-like fold that mediates oligomerization with apparent heptameric symmetry, generating a barrel-shaped structure with a central pore that is proposed contributes to the macrophage killing functions of EspB.
Journal ArticleDOI
Structural and Biochemical Characterization of Plasmodium falciparum 12 (Pf12) Reveals a Unique Interdomain Organization and the Potential for an Antiparallel Arrangement with Pf41
Michelle L. Tonkin,Silvia A. Arredondo,Bianca Loveless,Jason J. Serpa,Karl A.T. Makepeace,Natarajan Sundar,Evgeniy V. Petrotchenko,Louis H. Miller,Michael E. Grigg,Martin J. Boulanger +9 more
TL;DR: It is shown that Pf12 is highly conserved and under purifying selection, and details of its interaction with Pf41 reveal important insight into the structural and functional properties of this archetypal member of the 6-Cys protein family.
Journal ArticleDOI
Super Spy variants implicate flexibility in chaperone action
Shu Quan,Lili Wang,Evgeniy V. Petrotchenko,Karl A.T. Makepeace,Scott Horowitz,Jianyi Yang,Yang Zhang,Christoph H. Borchers,James C.A. Bardwell +8 more
TL;DR: A genetic selection that links protein stability to antibiotic resistance to isolate variants of the newly discovered chaperone Spy that show an up to 7 fold improved chaper one activity against a variety of substrates provide evidence for the importance of disorder and flexibility in chaperones function.
Journal ArticleDOI
Isotopically-coded short-range hetero-bifunctional photo-reactive crosslinkers for studying protein structure
TL;DR: Hetero-bifunctional crosslinkers containing both a photo-reactive functional group and an NHS-ester group can be used to enable non-specific crosslinking within the proximity of lysine residues, and their effectiveness for studying the native α-synuclein protein structure is demonstrated.
Journal ArticleDOI
Protein unfolding as a switch from self-recognition to high-affinity client binding.
Bastian Groitl,Scott Horowitz,Karl A.T. Makepeace,Evgeniy V. Petrotchenko,Christoph H. Borchers,Dana Reichmann,Dana Reichmann,James C.A. Bardwell,Ursula Jakob +8 more
TL;DR: Using site-specific Fluorine-19 nuclear magnetic resonance experiments guided by in vivo crosslinking studies, it is revealed that the partial unfolding of HSp33's linker region facilitates client binding to an amphipathic docking surface on Hsp33.