Disordered proteins studied by chemical shifts

Magnus Kjærgaard; Flemming Martin Poulsen

doi:10.1016/j.pnmrs.2011.10.001

Disordered proteins studied by chemical shifts

Magnus Kjærgaard, Flemming Martin Poulsen

Biomolecular Sciences

44 Citations (Scopus)

Abstract

Several researchers conducted a study to investigate disordered chemical shifts in intrinsically disordered proteins (IDP). The chemical shifts of the nuclei in a protein were determined by several factors including the structure of the protein and its solvent surroundings. The secondary structure elements were only populated transiently in disordered proteins and the challenge was to identify both their location in the protein sequence and their time-averaged populations. The most important variables relating to external conditions were pH, co-solvents, and temperature. The chemical shift perturbations from datasets recorded at pH values above the average were not canceled by the perturbations from below the average value. It was also observed that temperature affected the random coil chemical shifts, but the importance of temperature varied significantly between nuclei.

Original language	English
Journal	Progress in Nuclear Magnetic Resonance Spectroscopy
Volume	60
Pages (from-to)	42-51
Number of pages	10
ISSN	0079-6565
DOIs	https://doi.org/10.1016/j.pnmrs.2011.10.001
Publication status	Published - Jan 2012

Keywords

Animals
Humans
Mutation
Nuclear Magnetic Resonance, Biomolecular
Protein Structure, Secondary
Proteins

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10.1016/j.pnmrs.2011.10.001

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abstract = "Several researchers conducted a study to investigate disordered chemical shifts in intrinsically disordered proteins (IDP). The chemical shifts of the nuclei in a protein were determined by several factors including the structure of the protein and its solvent surroundings. The secondary structure elements were only populated transiently in disordered proteins and the challenge was to identify both their location in the protein sequence and their time-averaged populations. The most important variables relating to external conditions were pH, co-solvents, and temperature. The chemical shift perturbations from datasets recorded at pH values above the average were not canceled by the perturbations from below the average value. It was also observed that temperature affected the random coil chemical shifts, but the importance of temperature varied significantly between nuclei.",

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AU - Kjærgaard, Magnus

AU - Poulsen, Flemming Martin

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N2 - Several researchers conducted a study to investigate disordered chemical shifts in intrinsically disordered proteins (IDP). The chemical shifts of the nuclei in a protein were determined by several factors including the structure of the protein and its solvent surroundings. The secondary structure elements were only populated transiently in disordered proteins and the challenge was to identify both their location in the protein sequence and their time-averaged populations. The most important variables relating to external conditions were pH, co-solvents, and temperature. The chemical shift perturbations from datasets recorded at pH values above the average were not canceled by the perturbations from below the average value. It was also observed that temperature affected the random coil chemical shifts, but the importance of temperature varied significantly between nuclei.

AB - Several researchers conducted a study to investigate disordered chemical shifts in intrinsically disordered proteins (IDP). The chemical shifts of the nuclei in a protein were determined by several factors including the structure of the protein and its solvent surroundings. The secondary structure elements were only populated transiently in disordered proteins and the challenge was to identify both their location in the protein sequence and their time-averaged populations. The most important variables relating to external conditions were pH, co-solvents, and temperature. The chemical shift perturbations from datasets recorded at pH values above the average were not canceled by the perturbations from below the average value. It was also observed that temperature affected the random coil chemical shifts, but the importance of temperature varied significantly between nuclei.

KW - Animals

KW - Humans

KW - Mutation

KW - Nuclear Magnetic Resonance, Biomolecular

KW - Protein Structure, Secondary

KW - Proteins

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SP - 42

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JO - Progress in Nuclear Magnetic Resonance Spectroscopy

JF - Progress in Nuclear Magnetic Resonance Spectroscopy

ER -

Disordered proteins studied by chemical shifts

Abstract

Keywords

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