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SUMMARY:Turning Up the Heat on Dynamic Proteins with Temperature-Jump X-ra
 y Crystallography
DTSTART;VALUE=DATE-TIME:20250924T081500Z
DTEND;VALUE=DATE-TIME:20250924T084500Z
DTSTAMP;VALUE=DATE-TIME:20260525T050112Z
UID:indico-contribution-1858@lindico453.srv.lu.se
DESCRIPTION:Speakers: Michael Thompson (University of California\, Merced)
 \nProtein dynamics are critical for function\, but it remains challenging 
 to understand\, in atomic detail\, how a molecule’s biological activity 
 is enabled by the physical coupling of its conformational fluctuations acr
 oss varied length and time scales. Time-dependent X-ray crystallographic m
 easurements of molecular structure can overcome some of the limitations of
  traditional structural biology and yield deep insight into protein confor
 mational landscapes\, but it remains challenging to initiate synchronous c
 onformational changes in crystallized macromolecules\, which is a requirem
 ent for such experiments. I will describe how observations from multi-temp
 erature structural measurements motivated the development of temperature-j
 ump (T-jump) crystallography\, and summarize the results of our early T-ju
 mp experiments on the model enzyme lysozyme. I will also discuss ongoing e
 fforts to democratize these experiments and apply them to increasingly com
 plex biological systems\, including the metalloenzyme soybean lipoxygenase
 \, whose catalytic mechanism involves a rate-limiting hydrogen tunneling s
 tep that is coupled to motion of the protein scaffold.\n\nhttps://lindico4
 53.srv.lu.se/event/583/contributions/1858/
LOCATION:LINXS at The Loop
URL:https://lindico453.srv.lu.se/event/583/contributions/1858/
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