Disordered proteins studied by chemical shifts

TY - JOUR

T1 - Disordered proteins studied by chemical shifts

AU - Kjærgaard, Magnus

AU - Poulsen, Flemming Martin

PY - 2012/1

Y1 - 2012/1

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

U2 - 10.1016/j.pnmrs.2011.10.001

DO - 10.1016/j.pnmrs.2011.10.001

M3 - Journal article

C2 - 22293398

SN - 0079-6565

VL - 60

SP - 42

EP - 51

JO - Progress in Nuclear Magnetic Resonance Spectroscopy

JF - Progress in Nuclear Magnetic Resonance Spectroscopy

ER -