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Theoretical reason ...
Theoretical reason for the lack of influence of 1H–14N cross-relaxation on the water proton T 1 NMRD profile in slow tumbling proteins
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- Westlund, Per-Olof (författare)
- Umeå universitet,Kemiska institutionen
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(creator_code:org_t)
- Informa UK Limited, 2012
- 2012
- Engelska.
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Ingår i: Molecular Physics. - : Informa UK Limited. - 0026-8976 .- 1362-3028. ; 110:18, s. 2251-2255
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
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- For immobilized protein the water proton T 1-NMRD profile displays three enhanced relaxation peaks (QP). For slow tumbling proteins these relaxation peaks are not experimentally observed. However, the theoretically determined QP effect on the amide proton T 1-NMRD profile displays a distorted Lorentzian dispersion profile. The question arises as to whether there is also a distortion of the water-proton T 1-NMRD profile due to QP. The model of Sunde and Halle [J. Magn. Reson. 203, 257 (2010)] predicts a decreasing QP relaxation contribution and, with the aid of a model for tumbling proteins [P.-O. Westlund, Phys. Chem. Chem. Phys, 12, 3136 (2010)], it is shown that the QP effect is absent in water-proton T 1-NMRD profiles for slow tumbling proteins with τR < 1 µs, τI.
Ämnesord
- NATURVETENSKAP -- Kemi (hsv//swe)
- NATURAL SCIENCES -- Chemical Sciences (hsv//eng)
Nyckelord
- H–N cross-relaxation
- quadrupole peak effect
- stochastic Liouville equation
- water T 1-NMRD profiles
- slow tumbling proteins
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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