---
res:
  bibo_abstract:
  - Solid-state NMR provides insight into protein motion over time scales ranging
    from picoseconds to seconds. While in solution state the methodology to measure
    protein dynamics is well established, there is currently no such consensus protocol
    for measuring dynamics in solids. In this article, we perform a detailed investigation
    of measurement protocols for fast motions, i.e. motions ranging from picoseconds
    to a few microseconds, which is the range covered by dipolar coupling and relaxation
    experiments. We perform a detailed theoretical investigation how dipolar couplings
    and relaxation data can provide information about amplitudes and time scales of
    local motion. We show that the measurement of dipolar couplings is crucial for
    obtaining accurate motional parameters, while systematic errors are found when
    only relaxation data are used. Based on this realization, we investigate how the
    REDOR experiment can provide such data in a very accurate manner. We identify
    that with accurate rf calibration, and explicit consideration of rf field inhomogeneities,
    one can obtain highly accurate absolute order parameters. We then perform joint
    model-free analyses of 6 relaxation data sets and dipolar couplings, based on
    previously existing, as well as new data sets on microcrystalline ubiquitin. We
    show that nanosecond motion can be detected primarily in loop regions, and compare
    solid-state data to solution-state relaxation and RDC analyses. The protocols
    investigated here will serve as a useful basis towards the establishment of a
    routine protocol for the characterization of ps–μs motions in proteins by solid-state
    NMR.@eng
  bibo_authorlist:
  - foaf_Person:
      foaf_givenName: Jens D.
      foaf_name: Haller, Jens D.
      foaf_surname: Haller
  - 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
  bibo_doi: 10.1007/s10858-013-9787-x
  bibo_issue: '3'
  bibo_volume: 57
  dct_date: 2013^xs_gYear
  dct_isPartOf:
  - http://id.crossref.org/issn/0925-2738
  - http://id.crossref.org/issn/1573-5001
  dct_language: eng
  dct_publisher: Springer Nature@
  dct_subject:
  - Spectroscopy
  - Biochemistry
  dct_title: 'Amplitudes and time scales of picosecond-to-microsecond motion in proteins
    studied by solid-state NMR: a critical evaluation of experimental approaches and
    application to crystalline ubiquitin@'
...