C
Can Kayatekin
Researcher at Massachusetts Institute of Technology
Publications - 28
Citations - 1773
Can Kayatekin is an academic researcher from Massachusetts Institute of Technology. The author has contributed to research in topics: Protein folding & Population. The author has an hindex of 16, co-authored 26 publications receiving 1515 citations. Previous affiliations of Can Kayatekin include Sanofi S.A. & Howard Hughes Medical Institute.
Papers
More filters
Journal ArticleDOI
Quantitative Analysis of Hsp90-Client Interactions Reveals Principles of Substrate Recognition
Mikko Taipale,Irina Krykbaeva,Martina Koeva,Can Kayatekin,Kenneth D. Westover,Georgios I. Karras,Susan Lindquist,Susan Lindquist +7 more
TL;DR: In this paper, the authors systematically and quantitatively surveyed most human kinases, transcription factors, and E3 ligases for interaction with HSP90 and its cochaperone CDC37.
Journal ArticleDOI
Luminidependens (LD) is an Arabidopsis protein with prion behavior
Sohini Chakrabortee,Can Kayatekin,Greg A. Newby,Marc L. Mendillo,Alex K. Lancaster,Susan Lindquist,Susan Lindquist +6 more
TL;DR: The results suggest that prion-like conformational switches are evolutionarily conserved and might function in a wide variety of normal biological processes.
Journal ArticleDOI
Zinc binding modulates the entire folding free energy surface of human Cu,Zn superoxide dismutase.
TL;DR: The approximately 100-fold increase in the rate of folding of SOD in the presence of micromolar concentrations of zinc demonstrates a significant role for a preorganized zinc-binding loop in the transition-state ensemble for the rate-limiting monomer folding reaction in this beta-barrel protein.
Journal ArticleDOI
Microsecond acquisition of heterogeneous structure in the folding of a TIM barrel protein.
TL;DR: The earliest kinetic folding events for (βα)8 barrels reflect the appearance of off-pathway intermediates and ready access to locally folded, stable substructures may be a hallmark of repeat-module proteins and the source of early kinetic traps in these very common motifs.
Journal ArticleDOI
Microsecond Hydrophobic Collapse in the Folding of Escherichia coli Dihydrofolate Reductase, an α/β-Type Protein
Munehito Arai,Elena Kondrashkina,Can Kayatekin,C. Robert Matthews,Masahiro Iwakura,Osman Bilsel +5 more
TL;DR: The protein folding trajectories constructed by comparing the development of the compactness and the secondary structure suggest that the specific hydrophobic collapse model rather than the framework model better explains the experimental observations.