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Rigid protein motion as a model for crystallographic temperature factors.

ABSTRACT: The extent to which the librations of rigid molecules can model the crystallographic temperature factor profiles of proteins has been examined. For all proteins considered, including influenza virus hemagglutinin, glutathione reductase, myohemerythrin, myoglobin, and streptavidin, a simple 10-parameter model [V. Schomaker and K. N. Trueblood (1968) Acta Crystallogr. Sect. B 24, 63-76] is found to reproduce qualitatively the patterns of maxima and minima in the isotropic backbone meansquare displacements. Large deviations between the rigid molecule and individual atomic temperature factors are found to be correlated with a region in hemagglutinin for which the refined structural model is unsatisfactory and with errors in the structure in a partially incorrect model of myohemerythrin. For the high-resolution glutathione reductase structure, better results are obtained on treating each of the compact domains in the structure as independent rigid bodies. The method allows for the refinement of reliable temperature factors with the introduction of minimal parameters and may prove useful for the evaluation of models in the early stages of x-ray structure refinement. While these results by themselves do not establish the nature of the underlying displacements, the success of the rigid protein model in reproducing qualitative features of temperature factor profiles suggests that rigid body refinement results should be considered in any interpretation of crystallographic thermal parameters.

SUBMITTER: Kuriyan J

PROVIDER: S-EPMC51321 | biostudies-other | 1991 Apr

REPOSITORIES: biostudies-other

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Rigid protein motion as a model for crystallographic temperature factors.

Kuriyan J J Weis W I WI

Proceedings of the National Academy of Sciences of the United States of America 19910401 7

The extent to which the librations of rigid molecules can model the crystallographic temperature factor profiles of proteins has been examined. For all proteins considered, including influenza virus hemagglutinin, glutathione reductase, myohemerythrin, myoglobin, and streptavidin, a simple 10-parameter model [V. Schomaker and K. N. Trueblood (1968) Acta Crystallogr. Sect. B 24, 63-76] is found to reproduce qualitatively the patterns of maxima and minima in the isotropic backbone meansquare displ ...[more]

PMID: 2011586

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Project description:BackgroundCardiovascular magnetic resonance T1ρ mapping may detect myocardial injuries without exogenous contrast agent. However, multiple co-registered acquisitions are required, and the lack of robust motion correction limits its clinical translation. We introduce a single breath-hold myocardial T1ρ mapping method that includes model-based non-rigid motion correction.MethodsA single-shot electrocardiogram (ECG)-triggered balanced steady state free precession (bSSFP) 2D adiabatic T1ρ mapping sequence that collects five T1ρ-weighted (T1ρw) images with different spin lock times within a single breath-hold is proposed. To address the problem of residual respiratory motion, a unified optimization framework consisting of a joint T1ρ fitting and model-based non-rigid motion correction algorithm, insensitive to contrast change, was implemented inline for fast (~ 30 s) and direct visualization of T1ρ maps. The proposed reconstruction was optimized on an ex vivo human heart placed on a motion-controlled platform. The technique was then tested in 8 healthy subjects and validated in 30 patients with suspected myocardial injury on a 1.5T CMR scanner. The Dice similarity coefficient (DSC) and maximum perpendicular distance (MPD) were used to quantify motion and evaluate motion correction. The quality of T1ρ maps was scored. In patients, T1ρ mapping was compared to cine imaging, T2 mapping and conventional post-contrast 2D late gadolinium enhancement (LGE). T1ρ values were assessed in remote and injured areas, using LGE as reference.ResultsDespite breath holds, respiratory motion throughout T1ρw images was much larger in patients than in healthy subjects (5.1 ± 2.7 mm vs. 0.5 ± 0.4 mm, P < 0.01). In patients, the model-based non-rigid motion correction improved the alignment of T1ρw images, with higher DSC (87.7 ± 5.3% vs. 82.2 ± 7.5%, P < 0.01), and lower MPD (3.5 ± 1.9 mm vs. 5.1 ± 2.7 mm, P < 0.01). This resulted in significantly improved quality of the T1ρ maps (3.6 ± 0.6 vs. 2.1 ± 0.9, P < 0.01). Using this approach, T1ρ mapping could be used to identify LGE in patients with 93% sensitivity and 89% specificity. T1ρ values in injured (LGE positive) areas were significantly higher than in the remote myocardium (68.4 ± 7.9 ms vs. 48.8 ± 6.5 ms, P < 0.01).ConclusionsThe proposed motion-corrected T1ρ mapping framework enables a quantitative characterization of myocardial injuries with relatively low sensitivity to respiratory motion. This technique may be a robust and contrast-free adjunct to LGE for gaining new insight into myocardial structural disorders.

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Rigid protein motion as a model for crystallographic temperature factors.

Publications

Rigid protein motion as a model for crystallographic temperature factors.

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