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Variability of the 15N chemical shielding tensors in the B3 domain of protein G from 15N relaxation measurements at several fields. Implications for backbone order parameters

Author
HALL, Jennifer B1 ; FUSHMAN, David1
[1] Department of Chemistry and Biochemistry, Center for Biomolecular Structure and Organization, University of Maryland, College Park, Maryland 20742, United States
Source

Journal of the American Chemical Society. 2006, Vol 128, Num 24, pp 7855-7870, 16 p ; ref : 70 ref

CODEN
JACSAT
ISSN
0002-7863
Scientific domain
Biochemistry, molecular biology, biophysics; Chemistry; Organic chemistry; Atomic molecular physics
Publisher
American Chemical Society, Washington, DC
Publication country
United States
Document type
Article
Language
English
Keyword (fr)
Azote 15 Dynamique moléculaire Déplacement chimique Effet Overhauser Facteur fixant immunoglobuline Paramètre RMN Protéine G Relaxation spin réseau Relaxation spin spin Site spécifique Spectrométrie RMN
Keyword (en)
Nitrogen 15 Molecular dynamics Chemical shift Overhauser effect Immunoglobulin binding factor NMR parameter G protein Spin lattice relaxation Spin spin relaxation Site specificity NMR spectrometry
Keyword (es)
Dinámica molecular Desplazamiento químico Efecto Overhauser Factor fijador immunoglobulina Parámetro RMN Proteína G Relajación spin red Relajación spin spin Sitio específico Espectrometría RMN
Classification
Pascal
002 Biological and medical sciences / 002A Fundamental and applied biological sciences. Psychology / 002A03 Molecular biophysics / 002A03J Spectroscopy : techniques and spectras

Discipline
Molecular biophysics
Origin
Inist-CNRS
Database
PASCAL
INIST identifier
17877867

Sauf mention contraire ci-dessus, le contenu de cette notice bibliographique peut être utilisé dans le cadre d’une licence CC BY 4.0 Inist-CNRS / Unless otherwise stated above, the content of this bibliographic record may be used under a CC BY 4.0 licence by Inist-CNRS / A menos que se haya señalado antes, el contenido de este registro bibliográfico puede ser utilizado al amparo de una licencia CC BY 4.0 Inist-CNRS

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