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Hydrogen exchange mass spectrometry for the analysis of protein
Hydrogen exchange mass spectrometry for the analysis of protein

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a review of the BLAST meeting, ï - Bacterial Locomotion and Signal
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... monochrome CoolSnapHQ digital camera (Photometrics) using Metamorph software (Universal Imaging). The lipophylic membrane dye TMA-DPH (Molecular Probes) was used at a VOLUME 283 • NUMBER 8 • FEBRUARY 22, 2008 ...
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In Depth Analysis of Protein Amino Acid Sequence and PTMs with
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Role of protein methylation in chromatin remodeling and
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... vitro was found in transcriptionally active macronuclei of Tetrahymena but not in transcriptionally inactive micronuclei (Strahl et al., 1999). In the same study methylation of yeast histones was found preferentially on H3 molecules that were also acetylated, thus providing another indication that h ...
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The evolution, function, structure, and expression
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... oligomeric form with a β-sandwich that forms a hollow ball. This conservation occurs despite significant divergence in primary sequences. It is well established that sHSPs are molecular chaperones that prevent misfolding and irreversible aggregation of their client proteins. Most notably, the sHSPs ...
Preventing Shipping Fever Pneumonia in Calves
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... Shipping fever pneumonia is a respiratory disease typically found in calves that causes high fever, rapid and shallow respiration, coughing and a reduced appetite. The costs of prevention and treatment may vary but can be quite considerable for cattle producers. It is believed that exposure to stres ...
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Intrinsically disordered proteins



An intrinsically disordered protein (IDP) is a protein that lacks a fixed or ordered three-dimensional structure. IDPs cover a spectrum of states from fully unstructured to partially structured and include random coils, (pre-)molten globules, and large multi-domain proteins connected by flexible linkers. They constitute one of the main types of protein (alongside globular, fibrous and membrane proteins).The discovery of IDPs has challenged the traditional protein structure paradigm, that protein function depends on a fixed three-dimensional structure. This dogma has been challenged over the last decades by increasing evidence from various branches of structural biology, suggesting that protein dynamics may be highly relevant for such systems. Despite their lack of stable structure, IDPs are a very large and functionally important class of proteins. In some cases, IDPs can adopt a fixed three-dimensional structure after binding to other macromolecules.
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