Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins. | J Magn Reson;219: 75-82, 2012 Jun. | MEDLINE

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Heteronuclear Adiabatic Relaxation Dispersion (HARD) for quantitative analysis of conformational dynamics in proteins.

Traaseth, Nathaniel J; Chao, Fa-An; Masterson, Larry R; Mangia, Silvia; Garwood, Michael; Michaeli, Shalom; Seelig, Burckhard; Veglia, Gianluigi.

Affiliation

Traaseth NJ; Department of Biochemistry, Molecular Biology, and Biophysics, University of Minnesota, Minneapolis, MN 55455, USA.

J Magn Reson ; 219: 75-82, 2012 Jun.

Article in En | MEDLINE | ID: mdl-22621977

Subject(s)

Algorithms; Nuclear Magnetic Resonance, Biomolecular/methods; Proteins/chemistry; Proteins/ultrastructure; Protein Conformation

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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Algorithms / Proteins / Nuclear Magnetic Resonance, Biomolecular Language: En Journal: J Magn Reson Year: 2012 Document type: Article

Search on Google

Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Algorithms / Proteins / Nuclear Magnetic Resonance, Biomolecular Language: En Journal: J Magn Reson Year: 2012 Document type: Article