Dipolar relaxation and slow molecular motions in solid proteins

R. Gáspár, E. R. Andrew, D. J. Bryant, E. M. Cashell

Research output: Contribution to journalArticle

23 Citations (Scopus)

Abstract

The proton dipolar relaxation time T1 D has been measured in solid α-chymotrypsin and solid lysozyme between 10 and 300 K enabling slower molecular motions to be investigated.

Original languageEnglish
Pages (from-to)327-330
Number of pages4
JournalChemical Physics Letters
Volume86
Issue number4
DOIs
Publication statusPublished - Feb 26 1982

Fingerprint

proteins
lysozyme
Chymotrypsin
Muramidase
Relaxation time
Protons
Proteins
relaxation time
protons

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Spectroscopy
  • Condensed Matter Physics
  • Atomic and Molecular Physics, and Optics
  • Surfaces and Interfaces

Cite this

Dipolar relaxation and slow molecular motions in solid proteins. / Gáspár, R.; Andrew, E. R.; Bryant, D. J.; Cashell, E. M.

In: Chemical Physics Letters, Vol. 86, No. 4, 26.02.1982, p. 327-330.

Research output: Contribution to journalArticle

Gáspár, R. ; Andrew, E. R. ; Bryant, D. J. ; Cashell, E. M. / Dipolar relaxation and slow molecular motions in solid proteins. In: Chemical Physics Letters. 1982 ; Vol. 86, No. 4. pp. 327-330.
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