---
res:
  bibo_abstract:
  - We demonstrate for different protein samples that 2D 1H−15N correlation NMR spectra
    can be recorded in a few seconds of acquisition time using a new band-selective
    optimized flip-angle short-transient heteronuclear multiple quantum coherence
    experiment. This has enabled us to measure fast hydrogen−deuterium exchange rate
    constants along the backbone of a small globular protein fragment by real-time
    2D NMR.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Paul
      foaf_name: Schanda, Paul
      foaf_surname: Schanda
      foaf_workInfoHomepage: http://www.librecat.org/personId=7B541462-FAF6-11E9-A490-E8DFE5697425
    orcid: 0000-0002-9350-7606
  - foaf_Person:
      foaf_givenName: Bernhard
      foaf_name: Brutscher, Bernhard
      foaf_surname: Brutscher
  bibo_doi: 10.1021/ja051306e
  bibo_issue: '22'
  bibo_volume: 127
  dct_date: 2005^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/0002-7863
  - http://id.crossref.org/issn/1520-5126
  dct_language: eng
  dct_publisher: American Chemical Society@
  dct_subject:
  - Colloid and Surface Chemistry
  - Biochemistry
  - General Chemistry
  - Catalysis
  dct_title: Very fast two-dimensional NMR spectroscopy for real-time investigation
    of dynamic events in proteins on the time scale of seconds@
...