Sequence-Specific Protein Secondary-Structure Assignment with Isotope Reverse-Labeled Amide I Spectroscopy

The dramatic advances made recently by protein-structure prediction tools like AlphaFold offer an opportunity for the development of new experimental methods designed to test sequence-based predictions rather than build full atomistic structures from scratch. While atomistic methods such as X-ray cr...

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Bibliographic Details
Main Author:	Jacob H. Wat (22577422) (author)
Other Authors:	Tristen West (22577425) (author), Nicolas J. Pizzala (19442700) (author), Sarah Alvarez (5545145) (author), Yanbin Wang (1758400) (author), Ming Chen (115604) (author), Mike Reppert (1281084) (author)
Published:	2025
Subjects:	Biophysics Biochemistry Molecular Biology Hematology Plant Biology Biological Sciences not elsewhere classified Chemical Sciences not elsewhere classified Physical Sciences not elsewhere classified nuclear magnetic resonance cryogenic electron microscopy concepts experimentally using specific structural information new experimental approach 13 </ sup 12 </ sup whose crystal structure published crystal structure low sample cost based predictions rather labeled protein construct collect ftir spectra resulting isotope reverse labeled ftir spectroscopy specific protein secondary specific secondary labeled amide enriched spectra approach offers structure determination structure content structure assignments structure assignment secondary structure traditional ftir protein ’ enriched protein wide variety transform infrared total fraction spectroscopic methods solubilized membranes sheet present routine characterization ray crystallography producing isotope present contribution often cheaper offer insight obtain assignments live cells isotope reverse expression culture efficient means critical role circular dichroism bulk secondary atomistic methods amino acids
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Sequence-Specific Protein Secondary-Structure Assignment with Isotope Reverse-Labeled Amide I Spectroscopy

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