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DTSTAMP:20260505T142855Z
UID:1782201600@ist.ac.at
DTSTART:20260623T100000
DTEND:20260623T110000
DESCRIPTION:Speaker: Lea Becker\nhosted by Robert Seiringer\nAbstract: Char
 acterizing protein dynamics at the atomic level is essential for our under
 standing of biological mechanisms. Whether it is to facilitate metabolite 
 transport\, catalyze reactions\, transmit signals\, or regulate metabolism
  – proteins are constantly in motion and sample multiple conformational 
 states to fulfill their function. Nuclear magnetic resonance (NMR) spectro
 scopy is particularly well suited to elucidate the dynamics of biomolecule
 s on their complex free-energy landscape. In particular\, solid-state magi
 c-angle spinning (MAS) NMR enables the study of large molecular assemblies
 \, protein crystals\, or insoluble proteins at atomic resolution without a
 n inherent molecular size limitation. MAS NMR experiments to probe protein
  dynamics are extremely versatile and sensitive to motional timescales fro
 m picoseconds to seconds. Over the past decades\, technological advances\,
  developments in experimental design\, and new isotope-labeling approaches
  have further expanded the possibilities of this technique and significant
 ly improved the accuracy of the determined motional parameters.Functionall
 y important sites of proteins often contain aromatic residues. Their side-
 chain motions have therefore long served as valuable indicators of mechani
 stically relevant dynamics in NMR studies. In this thesis\, site-specifica
 lly labeled aromatic residues act as sensitive reporters for MAS NMR studi
 es of protein dynamics. The first part addresses how different environment
 s impact side-chain motion by probing ring flips of phenylalanines and tyr
 osines in crystalline proteins and amyloid fibrils. It provides important 
 insights for the analysis of dynamics obtained in non-native protein envir
 onments and emphasizes the complex factors that determine the timescale of
  internal dynamics. In the second part\, the focus shifts towards methodol
 ogical questions regarding the investigation of protein dynamics by 19F MA
 S NMR. The fluorine nucleus exhibits promising characteristics for NMR stu
 dies but also presents significant challenges\, which is why the full meth
 odological potential of 19F MAS NMR has not been fully realized yet. This 
 work demonstrates that paramagnetic doping can considerably reduce the mea
 surement time and improve the sensitivity of fluorinated samples. Finally\
 , 19F MAS NMR is evaluated as a tool for studying protein side-chain dynam
 ics on the example of tryptophans. The results illustrate the challenges i
 n analyzing such experiments and lay the foundation for further developmen
 t of 19F MAS NMR relaxation studies.Taken together\, this thesis highlight
 s the potential of combining specific isotope labeling\, MAS NMR\, and com
 plementary methods such as crystallography and computational simulations t
 o elucidate internal protein dynamics. The further development of such int
 egrative approaches will be crucial to improving our understanding of comp
 lex mechanisms and protein function.
LOCATION:Central Bldg / O1 / Mondi 2a (I01.O1.008)\, ISTA
ORGANIZER:
SUMMARY:Lea Becker: Thesis Defense: Exploring protein dynamics using specif
 ic labeling approaches for solid-state MAS NMR
URL:https://talks-calendar.ista.ac.at/events/6447
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