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SUMMARY:Low Viscosity Fluids for the Structural Determination of Proteins b
 y 2D NMR
LOCATION:Chemistry A101
TZID:America/Denver
DTSTART:20180001T000000
UID:2026-05-17-17-16-45@natsci.colostate.edu
DTSTAMP:20260517T171645
Description:Literature Seminar Abstract\n\nAlthough x-ray crystallography h
 as been the gold standard\, nuclear magnetic resonance spectroscopy (NMR) 
 has also been demonstrated as an effective method for protein structure de
 termination. NMR spectroscopy has the ability to view a protein beyond its
  static structure\; it can yield data that gives information about its dyn
 amic behavior as it interacts with other analytes\, solutions\, or altered
  conditions. However\, NMR spectroscopy remains limited by the slow tumbli
 ng rates of macromolecules with molecular masses greater than 30kDa. Slow 
 molecular tumbling rates broaden spectral linewidths\, making elucidation 
 of specific cross peaks challenging. To address this problem\, the Wand re
 search group combines the encapsulation of large proteins within reverse m
 icelles suspended in a low viscosity fluid to increase tumbling times and 
 minimize the rotational correlation constant that governs the speed of T2 
 relaxation. Using previously optimized surfactant mixtures\, Nucci et al. 
 demonstrate the successful application of this novel technique towards pro
 teins as well as the promising potential to investigate future\, more comp
 lex macromolecule analytes.  4:00 pm
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