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Macromolecules
Macromolecules

... • What are the names of the people you sit with? • What are the common elements found in the macromolecules? ...
Chapter 7: Protein
Chapter 7: Protein

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15Nitrogen metabolism

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protein lesson
protein lesson

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A1986A777600001

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Presentation - people.vcu.edu
Presentation - people.vcu.edu

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Remember: Condensation makes bonds: Hydrolysis breaks bonds.
Remember: Condensation makes bonds: Hydrolysis breaks bonds.

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CHEMISTRY Answer ALL questions of the on

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File - What the Shonkalay?

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Power Point 3 - G. Holmes Braddock
Power Point 3 - G. Holmes Braddock

... altered, they can change the rate of the reactions caused by the enzyme. • In the nature, organisms will adjust the conditions of there enzymes to make a more useful rate of reaction if it is necessary.( Most of the times it is ) • Sometimes the organism enzymes adapt to ...
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View PDF

... Whatis the chemical formula for a carbohydrate? Cn(H2O)m n=#of carbon atoms, m=water molecules Glucose is broken down and turned into ATP that gives cells the energy they need. Carbohydrates aren’t always sugary. What is the carbohydrate plants use to store extra sugar called?CELLULOSE ex. FOUND IN ...
Physical Properties - Winthrop Chemistry, Physics, and Geology
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... me to re-evaluate how homework will be handled • I will now be picking up every problem assigned on the Course Schedule – It was readily apparent that very few of you actually did the problems ...
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... 1. Shikimic acid or shikimate: is an important biochemical metabolite in plants and microorganisms. 2. Aromatic compound: is a hydrocarbon with alternating double bonds and single bonds between carbon atoms 3. Amino acids: are molecules containing an amine group, a carboxylic acid group and a side c ...
Modeling a -Sheet of Green Fluorescent Protein
Modeling a -Sheet of Green Fluorescent Protein

... What differences do you see on one side of the β-sheet versus the other? What implications does this have on the spatial arrangement of this sheet with the environment? One of the sides of the β-sheet is predominantly not charged (gray amino acid sidechains) and the other side is mostly charged (red ...
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Chapter 11: DNA and Genes

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How Does Antiretroviral Therapy Affect HIV Mutation and
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Protein Structure and Enzyme Function
Protein Structure and Enzyme Function

... combination with the amino acid sequence gives the protein its unique structure that will allow it to carry out its function. Oftentimes, proteins are described as units like a “lock and a key”. A lock can only be opened by a key of a particular shape. If you get home this afternoon and someone has ...
Proteins in nutrition
Proteins in nutrition

... about 1,2 – 1,5 g / kg / day Pregnancy and breastfeeding: about 1,5 g / kg / day Sportsmen in training: max. 1,3 – 1,5 g / kg / day (higher amount do not use for proteosynthesis, but only as energy source) Excessive intake: The human body is able to use for proteosynthesis only limited amount of ami ...
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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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