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Published: March 17, 2011 r 2011 American Chemical Society 4251 dx.doi.org/10.1021/jp2005343 |J. Phys. Chem. B 2011, 115, 42514258
 

Summary: Published: March 17, 2011
r 2011 American Chemical Society 4251 dx.doi.org/10.1021/jp2005343 |J. Phys. Chem. B 2011, 115, 42514258
ARTICLE
pubs.acs.org/JPCB
Ultraviolet Resonance Raman Study of Side Chain Electrostatic Control
of Poly-L-Lysine Conformation
Lu Ma, Zeeshan Ahmed, and Sanford A. Asher*
Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania 15260, United States
' INTRODUCTION
Developing an understanding of the mechanism of protein
folding is one of the most important unsolved problems in
structural biology.15
The major underlying assumption is that
the protein native structure is the thermodynamically most stable
structure.68
Further, this, native structure is thought to be
defined by the primary amino acid sequence and the protein
solution environment. Thus, the protein primary sequence is
expected to contain all of the information necessary to specify the
protein native structure and its folding mechanisms.

  

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

 

Collections: Materials Science; Chemistry