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Proton Transverse Relaxation as a Sensitive Probe for Structure Determination in Solid Proteins
Author(s) -
Rovó Petra,
Grohe Kristof,
Giller Karin,
Becker Stefan,
Linser Rasmus
Publication year - 2015
Publication title -
chemphyschem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201501040
Subject(s) - proton , chemistry , relaxation (psychology) , paramagnetism , solid state , transverse plane , spin (aerodynamics) , front cover , chemical physics , solid state nuclear magnetic resonance , analytical chemistry (journal) , cover (algebra) , nuclear magnetic resonance , crystallography , physics , condensed matter physics , organic chemistry , nuclear physics , thermodynamics , psychology , social psychology , structural engineering , engineering , mechanical engineering
Abstract The front cover artwork is provided by the group of Dr. Rasmus Linser from the Max Planck Institute for Biophysical Chemistry. The image shows a protein chemically modified to contain a paramagnetic spin label. By quantifying the effects on proton spin states in solid‐state NMR, this effect is employed to shed light on the protein structure. Read the full text of the article at 10.1002/cphc.201500799