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Biochemistry Lit Exam Concepts Soluble/Membrane protein function
Biochemistry Lit Exam Concepts Soluble/Membrane protein function

... Metabolism: Be able to explain the chemical logic of a metabolic pathway, particularly those from primary metabolism (e.g. glycolysis, citric acid cycle, fatty acid biosynthesis, etc.). be able to adapt the chemical logic from a primary metabolic pathway to that of a secondary metabolic pathway. DNA ...
Chapter 5 – Quiz #2-A Take Home Quiz
Chapter 5 – Quiz #2-A Take Home Quiz

N-terminal derivatization for de novo sequencing
N-terminal derivatization for de novo sequencing

... 7. Guanidination. Conversion of carboxy-terminal lysine residues (from tryptic digestion) to homoarginines prevents unwanted sulfonate tagging of these residues, increases their basicities and can improve the selective formation of y-series ions; and so the following procedure may be used on peptide ...
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...  The function of a protein is closely correlated with its subcellular location.  The protein cellular location plays a important role in molecular biology, cell biology, pharmacology, and medical science.  Although there are many experiments to prediction protein location, but it is time consumin ...
Black and White Nucleotide Metabolism english document for
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Ultramer® Oligonucleotides - Integrated DNA Technologies
Ultramer® Oligonucleotides - Integrated DNA Technologies

... Standard desalted Ultramer Oligonucleotides are perfect for site-directed mutagenesis, for use as templates for in vitro transcription, and in a variety of other molecular biology applications that require high purity oligonucleotides of length 45–200 nt. For applications in which higher purity is r ...
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Peptides and Protein Primary Structure
Peptides and Protein Primary Structure

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Probing the active site of homoserine trans

... post-translational modifications that result in addition or neutralization of charged groups. Therefore, further mass spectrometric analysis was carried out for characterization of the differences between the four protein populations. 3.2. The two acidic spots contain modified lysine residues Compariso ...
Increasing the thermostability of sucrose
Increasing the thermostability of sucrose

... desired improvement is achieved. In this way, the T50 of the lipase from Bacillus subtilis could be increased from 48 to 938C by the substitution of only seven amino acid residues (Reetz et al., 2006). To reduce the size of the libraries and thus the screening effort, an extension of the B-FIT proce ...
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Rapid communication: Nucleotide sequence of red seabream
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... amino acids and 14 amino acids from gilthead seabream and red seabream β-actin amino acid sequences, respectively (Figure 1). The amino acid sequences of red seabream β-actin differed from those of β-actin of gilthead seabream, which belongs to the same family as red seabream, by 16 amino acids out ...
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how cells obtain energy from food

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... Glycolysis can be slowed down by feedback inhibition • When the cell acquires more ATP that it needs, this inhibits the phosphofructokinase. • When the ATP is low again, the enzyme works as normal, speeding up glycolysis. The citric acid cycle can also be controlled through inhibition • Inhibition a ...
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... for meteoritic amino acids, laboratory studies in this area have focused primarily on the mechanisms most relevant to the more heavily studied aqueously altered meteorites, such as Streckertype syntheses leading to α-amino acids. Future work is needed to assess the formation potential of other mecha ...
Protein folding - UMass Boston Computer Science
Protein folding - UMass Boston Computer Science

... polypeptides are not a random selection from the natural universe • Which shapes can occur as the minimum energy configurations of polypeptides? – which are beautiful? (polypeptide tangrams) – which are interesting? (designer drugs) (I like cool rings, Brian White likes hot cores) ...
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1 Irreversible Enzyme Inhibition Affinity labels for studying enzyme

... • DFP reacts with the active site serine (Ser-195) of chymotrypsin to form DFP-chymotrypsin • Such organophosphorous inhibitors are used as insecticides or for enzyme research • These inhibitors are toxic because they inhibit acetylcholinesterase (a serine protease that hydrolyzes the neurotransmitt ...
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Metabolism 2 PDF

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acetyl CoA carboxylase
acetyl CoA carboxylase

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Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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