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Biomolecules carbonylation in oxidative stress related human
Biomolecules carbonylation in oxidative stress related human

... neurodegeneration, are characterized by elevated levels of oxidatively modified biomolecules (protein, lipids and DNA). Oxidation of biomolecules results in numerous functional dysfunctions associated with disease progression. One of the most abundant and hazardous class of modifications are reactiv ...
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... pre-proteins are maintained in a loosely folded, translocation-competent conformation through interaction with molecular chaperones. membranes involved in translocation have specific protein receptors exposed on their cytosolic faces. translocons catalyze movement of the proteins across the membrane ...
Macromolecular Interactions
Macromolecular Interactions

... Identification of consensus motif for SH2 Different SH2 domains recognize different sequence around pTyr Low affinity of binding (~ 1 mM) prevents identification of the determinants of sequence specificity In order to improve the binding affinity, construct a randomized pTyr peptide library and scr ...
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Protein Notes (Kim Foglia) - Mr. Ulrich`s Land of Biology
Protein Notes (Kim Foglia) - Mr. Ulrich`s Land of Biology

Minimizing filtration losses
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... ambushed by it. Most of the people who have written to us on this issue were caught by surprise, usually during scale-up. There are a couple of reasons for this. One, during process development, small process volumes make it relatively simple to proceed quickly from process step to process step. Sol ...
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... The alpha subunit of the heterotrimeric G protein is shown as a ribbon; the guanine nucleotide is spacefilled. P-alpha, P-beta, and P-gamma indicate the three phosphoryl groups in the GTP structure. As with most nucleoside triphosphates, there is a magnesium ion associated with GTP. The "ras-like ...
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... Protein is the foundation of a good diet and is made up of amino acids. Amino acids can be thought of as the “building blocks” of protein. Proteins are long “necklaces” of amino acids linked together. Dietary sources of protein are either complete or incomplete protein. Complete proteins contain all ...
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Protein Secondary Structure Prediction
Protein Secondary Structure Prediction

... the coordinates of residues. Tertiary Structure is the native state, or folded form, of a single protein chain. This form is also called the functional form. Tertiary structure of a protein includes the coordinates of its residues in three dimensional space. Quaternary Structure is the structure of ...
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Amino Acids

Proteins are composed of amino acid subunits which form stable
Proteins are composed of amino acid subunits which form stable

EGEE07_FP_October1st2007
EGEE07_FP_October1st2007

...  With 20 different comonomers, a protein chain of just 60 amino acids can theoretically exist in 2060 chemically and structurally unique combinations  But the number of natural proteins (109 to a maximum of 1013) is just a tiny fraction of all possible proteins  There exist a huge number of prote ...
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How to start to crystallise proteins

... There are typically two schools of thought about how one should proceed with a crystal growth trial. One approach would be to utilise a modern sparse matrix screen alongside a good systematic screen. JCSG plus and PACT premier would be a good choice, if there is plenty of protein, as these are both ...
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... MULTIPLE CHOICE: Circle ALL that are TRUE. There may be MORE THAN ONE correct answer. Organisms that can make their own food using chemosynthesis or photosynthesis are called ___________. A. heterotrophic B. autotrophic Organisms whose cells have a nucleus and organelles surrounded by membranes are ...
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Protein domain



A protein domain is a conserved part of a given protein sequence and (tertiary) structure that can evolve, function, and exist independently of the rest of the protein chain. Each domain forms a compact three-dimensional structure and often can be independently stable and folded. Many proteins consist of several structural domains. One domain may appear in a variety of different proteins. Molecular evolution uses domains as building blocks and these may be recombined in different arrangements to create proteins with different functions. Domains vary in length from between about 25 amino acids up to 500 amino acids in length. The shortest domains such as zinc fingers are stabilized by metal ions or disulfide bridges. Domains often form functional units, such as the calcium-binding EF hand domain of calmodulin. Because they are independently stable, domains can be ""swapped"" by genetic engineering between one protein and another to make chimeric proteins.
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