New answers tagged proteins
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In their active forms, various proteins have post-translational modifications (i.e. glycosylation) which are difficult to reproduce in bacteria. This is the rationale for the choice of higher organisms as the producing source. Mammalian cell lines are easier to generate and maintain but suffer from genetic and epigenetic instability (the transgene can be ...
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Yes. All proteins actually begin to get synthesized on cytoplasmic ribosomes but if they are going to be used for extracellular purposes, they are tagged and whole ribosome is taken to ER where protein synthesis is completed. The proteins are exocytosed with help of Golgi body, the post office tagging and packaging organelle (the Golgi body packages these ...
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ATryn is a human antithrombin produced in the milk of transgenic goats by GTC Biotherapeutics. It has FDA approval and I believe that it is available for prescription in the USA.
Added later, after the emphasis of the question changed somewhat.
Proteins produced in a mammalian system are more likely to have post-translational modifications that are much ...
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The answer is more like "It depends on the protein, and the renaturation (or refolding) process." There are a lot of factors that contribute to an individual protein's ability to refold, including size, sequence, secondary structure, amount and type of inter-amino acid links like disulfide bonds, number of subunits, the presence of chaperones/heat shock ...
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Well SNPs are single nucleotide polymorphisms. Some SNPs are in the coding regions of genes and they can result in changes in the resulting protein. For example, the SNP rs1801131 is a human variation where some individuals have a G instead of an A at position 1515 of the gene MTHFR. When the gene is transcribed and then translated into protein, this ...
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please go through the journal: S. Jo, K. Park, Biomaterials 21 (2000) 605-616.
The time and temperature probably helps to hydrolyze, formation of hydrogen bond and covalent bond formation. Hope this paper will help you.
Good luck!
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This is a perfectly reasonable result. Remember that you are measuring an average value for a very large population of BSA molecules. Essentially what the 0.4 means is that at any one time, about 40% of the BSA molecules have a free thiol, while the rest of the cysteine residues are disulfide-bonded.
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Scientists are recently finding (or coming to accept the notion) that, at least in eukaryotes, mRNA expression is poorly correlated to protein expression. There are several factors influencing translation regulation, such as siRNA or microRNAs, sequestering mRNAs while they are transported to various cell compartments, and others. Even after the protein is ...
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This is almost more a philosophical question about how you would like to define helices and sheets, which I would argue is not so well defined. shigeta mentions that they have well defined ramachandran coordinates, but that's for the central residues. Terminal residues are far more flexible. The more traditional definition is along the lines of the DSSP ...
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What biochemical molecule viewer allows for changes in amino acids and resulting tertiary structure?
If I understand what you're attempting to accomplish, as David said, this is a vigorous area of study in structural biology. I'll start by saying that a single amino acid substitution will often make virtually no difference in a structure, but there are proteins where a couple substitutions will convert an all alpha-helical protein to all beta-sheet, so I'll ...
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