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Magnetic susceptibility artifact in orbital magnetic resonance imaging.

Case report of a 16-year-old boy presenting with total hyphema due to blunt trauma to the left eye. During a subsequent cinematic MRI scan to identify salvageable lateral rectus muscle, the attachment of the left lateral rectus was obscured by a 20-mm diameter signal void. A subsequent CT scan for a suspected metallic foreign body revealed the muscle attachment after all. The theoretical explanations for this finding are discussed.

Adolescent↗

Nuclear magnetic resonance chemical shift: comparison of estimated secondary structures in peptides by nuclear magnetic resonance and circular dichroism.

Traditionally, CD has been used extensively for peptides in secondary structure analysis. In recent years, NMR chemical shifts and nuclear Overhauser enhancements have been widely used in conjunction with CD to assess the secondary structures of peptides and proteins; however, there are many instances where the estimation of secondary structure contents differs significantly between the two methods. In order to elucidate the perceived differences between the two methods, secondary structure estimations by CD and 1H NMR chemical shifts were compared for over 50 peptides. The linear peptides investigated were largely unstructured, approximately 15-50 residues in size, and lacked stable tertiary conformation. These peptides were studied in different solvent systems including water, alcohol-water, micelles and urea. A strong correlation exists for secondary structure assessment by CD and NMR chemical shifts; however, an interesting trend of higher estimation of helical contents by NMR was observed for peptide fragments from globular proteins studied in water. This may be a result of associative properties of these peptides in water. Additionally, a new method of quantitating secondary structure contents based on 1H NMR chemical shifts is reported.

Alcohols↗

Changes in size and magnetic resonance signal intensity of the cerebral CSF spaces during the cardiac cycle as studied by gated, high-resolution magnetic resonance imaging.

In 1966, du Boulay demonstrated the pulsatile nature of CSF flow in the cerebral aqueduct by using air cineventriculography, which disturbs normal CSF dynamics by replacing part of the incompressible CSF with air. To investigate this phenomenon noninvasively, 35 normal volunteers were studied using high-resolution, cardiac-gated MR imaging. Specifically, we wished to document changes in size and configuration of the CSF spaces and the incidence and magnitude of signal loss (an indication of CSF motion) in these spaces as they related to time in the cardiac cycle. Changes in size and configuration were measurable in the third ventricle only (size increased during systole in seven of the 35 volunteers). Except for the lateral ventricles, some loss in signal intensity was seen in all CSF spaces at least during systole in all 35 volunteers--findings consistent with those of du Boulay. However, contrary to du Boulay's observations, asymmetric loss of signal, consistent with pulsatile CSF flow, was demonstrated at the level of the foramen of Monro in 15 of the 35 volunteers. Based on the pattern of flow void at the level of the foramen of Monro and on the expansion of the third ventricle during systole, we propose a theory of synchronous CSF flow at the foramen of Monro and aqueduct, which unifies our MR findings with du Boulay's cineventriculographic observations.

Adult↗

Nuclear magnetic resonance studies on huwentoxin-XI from the Chinese bird spider Ornithoctonus huwena: 15N labeling and sequence-specific 1H, 15N nuclear magnetic resonance assignments.

Huwentoxin-XI purified from the Chinese bird spider Ornithoctonus huwena is a toxin with both antiprotease activity and potassium channel blocking activity. To determine its solution structure, huwentoxin-XI was expressed in a yeast eukaryotic expression system and studied by NMR. The 15N labeling strategy was used to facilitate the process of resonance assignments. The nearly complete sequence-specific assignments of proton and nitrogen resonances were obtained by analyzing a series of two-dimensional (2D) and three-dimensional (3D) spectra, including DQF-COSY, TOCSY, NOESY, 15N-1H HSQC, 15N-1H HNHA, 15N-1H HNHB, 15N-1H TOCSY-HSQC and 15N-1H NOESY-HSQC spectra. Secondary structure analysis of huwentoxin-XI showed that it mainly contains an N-terminal 310-helix from Thr3 to Arg5 and a C-terminal alpha-helix from Gln45 to Cys52, plus a triple-stranded antiparallel beta-sheet of Glu18-Asn23, Thr26-Ile31 and Asn40-Lys41. These studies provide a solid basis for the final structure determination of huwentoxin-XI.

Animals↗