Publications by authors named "J Czaplicki"

Chronobiology is the study of biological rhythms. Chronomics investigates interactions with environmental cycles in a genetically coded autoresonance of the biosphere with wrangling space and terrestrial weather. Analytical global and local methods applied to human blood pressure records of around-the-clock measurements covering decades detect physiological-physical interactions, a small yet measurable response to solar and terrestrial magnetism.

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A new solid-state NMR-based strategy is established for the precise and efficient analysis of orientation and dynamics of transmembrane peptides in fluid bilayers. For this purpose, several dynamically averaged anisotropic constraints, including (13)C and (15)N chemical shift anisotropies and (13)C-(15)N dipolar couplings, were determined from two different triple-isotope-labeled WALP23 peptides ((2)H, (13)C, and (15)N) and combined with previously published quadrupolar splittings of the same peptide. Chemical shift anisotropy tensor orientations were determined with quantum chemistry.

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The monosaccharides GlcNAc (N-acetylglucosamine) and the home-made GlcNC(16) (N-palmitoyl-D-glucosamine) were labeled with 2-AB (2-aminobenzamide) by reductive amination of the sugar. The aldehyde group of the monosaccharide reacts with the amino group of 2-AB, forming a Schiff base. In the second step, the Schiff base is reduced with sodium cyanoborohydride to yield a stable secondary amine.

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CD1-restricted lipid-specific T lymphocytes are primed during infection with Mycobacterium tuberculosis, the causative agent of tuberculosis. Here we describe the antigenicity of glycerol monomycolate (GroMM), which stimulates CD1b-restricted CD4(+) T cell clones. Chemical characterization of this antigen showed that it exists as two stereoisomers, one synthetic isomer being more stimulatory than the other.

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Article Synopsis
  • The outer membrane protein A from Klebsiella pneumoniae was studied using NMR to determine its three-dimensional structure, making it one of the largest integral membrane proteins analyzed so far.
  • The protein plays a significant role in immune responses and serves as an effective carrier protein, with a total of 210 amino acids.
  • The structure was refined using 920 experimental constraints, producing 20 optimal structures with minimal deviation in the core beta-barrel region, and the protein dynamics were investigated over various timescales.
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