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Cover Picture: Long‐Lived States to Monitor Protein Unfolding by Proton NMR (ChemPhysChem 15/2011)
Author(s) -
Bornet Aurélien,
Ahuja Puneet,
Sarkar Riddhiman,
Fernandes Laetitia,
Hadji Sonia,
Lee Shirley Y.,
Haririnia Aydin,
Fushman David,
Bodenhausen Geoffrey,
Vasos Paul R.
Publication year - 2011
Publication title -
chemphyschem
Language(s) - English
Resource type - Reports
SCImago Journal Rank - 1.016
H-Index - 140
eISSN - 1439-7641
pISSN - 1439-4235
DOI - 10.1002/cphc.201190075
Subject(s) - chemistry , proton nmr , amino acid , serine , proton , urea , molecular dynamics , crystallography , computational chemistry , stereochemistry , biochemistry , physics , phosphorylation , quantum mechanics
Long‐lived spin states (LLSs) can be used in proton NMR to extract information about the environment and local motions of selected amino acids in a protein. LLSs were encoded and sustained in the terminal glycines of ubiquitin, as well as in serine 65, in order to investigate the effect on protein stability of factors such as urea addition, changes of pH, or residue mutations. This work is presented on p. 2729 by P. R. Vasos et al.