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Protein Denaturation with Guanidinium: A 2D-IR Study.
MedLine Citation:
PMID:  24163724     Owner:  NLM     Status:  Publisher    
Abstract/OtherAbstract:
Guanidinium (Gdm(+)) is a widely used denaturant, but it is still largely unknown how it operates at the molecular level. In particular, the effect of guanidinium on the different types of secondary structure motifs of proteins is at present not clear. Here, we use two-dimensional infrared spectroscopy (2D-IR) to investigate changes in the secondary structure of two proteins with mainly α-helical or β-sheet content upon addition of Gdm-(13)C(15)N3·Cl. We find that upon denaturation, the β-sheet protein shows a complete loss of β-sheet structure, whereas the α-helical protein maintains most of its secondary structure. These results suggest that Gdm(+) disrupts β-sheets much more efficiently than α-helices, possibly because in the former, hydrophobic interactions are more important and the number of dangling hydrogen bonds is larger.
Authors:
Adriana Huerta-Viga; Sander Woutersen
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2013-9-23
Journal Detail:
Title:  The journal of physical chemistry letters     Volume:  4     ISSN:  1948-7185     ISO Abbreviation:  J Phys Chem Lett     Publication Date:  2013 Oct 
Date Detail:
Created Date:  2013-10-28     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101526034     Medline TA:  J Phys Chem Lett     Country:  -    
Other Details:
Languages:  ENG     Pagination:  3397-3401     Citation Subset:  -    
Affiliation:
Van't Hoff Institute for Molecular Sciences (HIMS), University of Amsterdam , Science Park 904, Amsterdam, The Netherlands.
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