19F NMR relaxation studies of fluorosubstituted tryptophans.
J Biomol NMR
; 73(8-9): 401-409, 2019 Sep.
Article
em En
| MEDLINE
| ID: mdl-31435857
ABSTRACT
We present 19F longitudinal and transverse relaxation studies for four differently fluorosubstituted L-tryptophans, which carry single F atoms in the indole ring, both in the context of the free amino acid and when located in the cyclophilin A protein. For the free 4F-, 5F-, 6F-, 7F-L-Trp, satisfactory agreement between experimentally measured and calculated relaxation rates was obtained, suggesting that the parameters used for calculating the rates for the indole frame are sufficiently accurate. We also measured and calculated relaxation rates for four differently 19F-tryptophan labeled cyclophilin A proteins, transferring the parameters from the free amino acid to the protein-bound moiety. Our results suggest that 19F relaxation data of the large and rigid indole ring in Trp are only moderately affected by protein motions and provide critical reference points for evaluating fluorine NMR relaxation in the future, especially in fluorotryptophan labeled proteins.
Palavras-chave
Texto completo:
1
Base de dados:
MEDLINE
Assunto principal:
Triptofano
/
Ressonância Magnética Nuclear Biomolecular
/
Flúor
Idioma:
En
Ano de publicação:
2019
Tipo de documento:
Article