Premium
Exploring the peptide 3 10 ‐helix ⇆ α–helix equilibrium with double label electron spin resonance
Author(s) -
Fiori Wayne R.,
Millhauser Glenn L.
Publication year - 1995
Publication title -
biopolymers
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.556
H-Index - 125
eISSN - 1097-0282
pISSN - 0006-3525
DOI - 10.1002/bip.360370403
Subject(s) - chemistry , helix (gastropod) , electron paramagnetic resonance , resonance (particle physics) , site directed spin labeling , spin label , peptide , electron , spin (aerodynamics) , crystallography , nuclear magnetic resonance , atomic physics , physics , nuclear physics , thermodynamics , biochemistry , ecology , snail , biology
Over the last several years we have used spin labeling as a means for exploring the structure of helical peptides. Two nitroxide labels are engineered into a peptide sequence and distances are ranked with electron spin resonance (ESR). We have found that there is a significant amount of 3 10 –helix in 16–residue model peptides containing only L –amino acids. This review covers several facets of the methodology including spin labeling strategy, interpretation of ESR spectra and the influence of molecular dynamics on the spectral line shapes. Also covered are recent findings of a length–dependent 3 l0 ‐helix → α‐helix transition and the role of Arg + in the stabilization of specific helix structures. © 1994 John Wiley & Sons, Inc.