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Published: March 22, 2011 r 2011 American Chemical Society 4234 dx.doi.org/10.1021/jp112238q |J. Phys. Chem. B 2011, 115, 42344243
 

Summary: Published: March 22, 2011
r 2011 American Chemical Society 4234 dx.doi.org/10.1021/jp112238q |J. Phys. Chem. B 2011, 115, 42344243
ARTICLE
pubs.acs.org/JPCB
Circular Dichroism and Ultraviolet Resonance Raman Indicate Little
Arg-Glu Side Chain r-Helix Peptide Stabilization
Zhenmin Hong, Zeeshan Ahmed,
and Sanford A. Asher*
Department of Chemistry, University of Pittsburgh, Pennsylvania 15260, United States
bS Supporting Information
' INTRODUCTION
For most proteins, the information needed to fold into their
native states is encoded in their primary sequences.1,2
Despite
decades of studies of protein folding, it is still impossible to
predict the secondary structure of a protein from only its primary
sequence, if an analogous sequence has not been previously
characterized. The native structure is determined by amino acid
side chain interactions such as hydrophobic interactions, hydro-
gen bonding, and electrostatic interactions. The strength and

  

Source: Asher, Sanford A. - Department of Chemistry, University of Pittsburgh

 

Collections: Materials Science; Chemistry