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Cloning of a cDNA Encoding a Plasma Membrane
Cloning of a cDNA Encoding a Plasma Membrane

... The Plant Cell, Vol. 8, 2265-2276, December 1996 O 1996 American Society of Plant Physiologists ...
ANTI_EPILEPTIC_DRUGS
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CHAPTER 22
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Peroxisomes - University of California San Diego
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21 О О О Termination of Polypeptide Synthesis Requires a Stop
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... have a hydrophobic signal peptide, usually at or near their amino terminus. There is no unique signal peptide sequence, but its characteristics include a positively charged N terminus, a core of 8–12 hydrophobic amino acids, and a more polar C-terminal segment that eventually serves as a cleavage si ...
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... Several conserved amino acids in the Isp2 and its homologous proteins have been found. Appling site directed point mutagenesis, I have replaced these amino acids by residues of completely different property. I have identified few residues which had important or essential role in the in vivo Isp2 dri ...
mechanism of the flagellar export system and its potential
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... denaturation experiments show that FliS unfolds in an unusally broad range (40-100 °C). Molecular dynamics simulations showed that the terminal region of FliS is much more flexible compared to that of stable proteins exhibiting cooperative unfolding transitions with similar temperature midpoints. Te ...
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... endoplasmic reticulum. N-terminal deletion to the transmembrane domain of this protein produced a dominantnegative mutant that blocked the trafficking of specific NCAPs such as CmPP16 and the movement protein (MP) of tobacco mosaic virus (TMV). Transgenic tobacco plants expressing the mutant form of ...
Mapping the Intramolecular Vibrational Energy Flow in Proteins
Mapping the Intramolecular Vibrational Energy Flow in Proteins

... ibrational energy transfer in proteins is particularly complex because proteins can be simultaneously highly anisotropic and strongly correlated environments at a molecular level. Highresolution protein structures carry functional information that is hidden from immediate inspection, particularly fo ...
Package `PPInfer`
Package `PPInfer`

... Title Inferring functionally related proteins using protein interaction networks Description Interactions between proteins occur in many, if not most, biological processes. Most proteins perform their functions in networks associated with other proteins and other biomolecules. This fact has motivate ...
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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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