Measuring protein dynamics with ultrafast two-dimensional infrared spectroscopy

2012 ◽  
Vol 23 (6) ◽  
pp. 062001 ◽  
Author(s):  
Katrin Adamczyk ◽  
Marco Candelaresi ◽  
Kirsty Robb ◽  
Andrea Gumiero ◽  
Martin A Walsh ◽  
...  
2021 ◽  
Vol 14 (1) ◽  
pp. 299-321
Author(s):  
Goran W. Tumbic ◽  
Md Yeathad Hossan ◽  
Megan C. Thielges

Proteins function as ensembles of interconverting structures. The motions span from picosecond bond rotations to millisecond and longer subunit displacements. Characterization of functional dynamics on all spatial and temporal scales remains challenging experimentally. Two-dimensional infrared spectroscopy (2D IR) is maturing as a powerful approach for investigating proteins and their dynamics. We outline the advantages of IR spectroscopy, describe 2D IR and the information it provides, and introduce vibrational groups for protein analysis. We highlight example studies that illustrate the power and versatility of 2D IR for characterizing protein dynamics and conclude with a brief discussion of the outlook for biomolecular 2D IR.


2021 ◽  
Author(s):  
Dean N. Edun ◽  
Meredith R. Flanagan ◽  
Arnaldo L. Serrano

Two-dimensional infrared spectroscopy reveals folding of an intrinsically disordered peptide when sequestered into a model “membrane-less” organelle.


2019 ◽  
Vol 10 (39) ◽  
pp. 8981-8989 ◽  
Author(s):  
Marius Horch ◽  
Janna Schoknecht ◽  
Solomon L. D. Wrathall ◽  
Gregory M. Greetham ◽  
Oliver Lenz ◽  
...  

A proof-of-concept study on a catalytic [NiFe] intermediate reveals structural and dynamical details of hydrogenases by ultrafast and two-dimensional infrared spectroscopies.


2004 ◽  
Vol 126 (25) ◽  
pp. 7981-7990 ◽  
Author(s):  
Nurettin Demirdöven ◽  
Christopher M. Cheatum ◽  
Hoi Sung Chung ◽  
Munira Khalil ◽  
Jasper Knoester ◽  
...  

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