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univERsity oF copEnhAGEn
univERsity oF copEnhAGEn

... did not change, except for a small fall in malate at 60s. The results indicate that there was a decrease in glycolytic flux due to an inhibition of the phosphofructokinase reaction. Since the tissue levels of phosphocreatine, ATP, ADP and AMP were unchanged inhibition of phosphofructokinase was prob ...
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Section 7-1

... Section 7-1 VOCABULARY REVIEW 1. Cellular respiration is the process in which cells make ATP by breaking down organic compounds. 2. Glycolysis is a biochemical pathway in which one molecule of glucose is oxidized to two molecules of pyruvic acid. 3. Lactic acid fermentation is an anaerobic pathway i ...
19 Dr. Nafez Abu Tarboosh Qusai Al Sharef
19 Dr. Nafez Abu Tarboosh Qusai Al Sharef

... So in the solution (cytoplasm) you can find NAD+ or NADH only. -The catalitic part of NAD+ is a carbon in the ring that H- adds to, so it takes electrons. -Where can we find them? Since it takes up a hydrogen we can find it in most dehydrogenases which donates electrons (in the form of hydride ion) ...
ERT320 BIOSEPARATION ENGINEERING
ERT320 BIOSEPARATION ENGINEERING

... defining the final product objective (therapeutic for human or animals, industrial enzymes)  Characterizing the starting material (from bacteria, yeast, mammalian cell, knows the physicochemical properties of the product such as surface hydrophobicity, pI, stability etc.)  Defining possible separa ...
AP Biology
AP Biology

... There are only 20 different amino acids Most amino acids correspond to more than one codon ...
DNA Message Conversion Activity
DNA Message Conversion Activity

... DNA » mRNA » tRNA » amino acid » protein In order to reap the benefits of this "secret message," you must be able to use a genetic code chart to decode the DNA sequence. You should separate the message into codons (Three Nitrogen Bases) and match those codons with their corresponding mRNA sequences ...
Ch. 13: Translation and Proteins
Ch. 13: Translation and Proteins

... protein fingerprinting, and amino acid analysis. Hemoglobin from individuals with sickle-cell anemia (HbSHbS) (a) migrates differently in an electrophoretic field, (b) shows an altered peptide in fingerprint analysis, and (c) shows an altered amino acid, valine, at the sixth position in the Beta cha ...
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Chapt21 Lecture 13ed Pt 2

... ribosome has moved to the right and the tRNA polypeptide at the P site is now longer by one amino acid. One tRNA is outgoing and another tRNA is incoming. ...
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BASIC CHEMISTRY

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Amino Acid and Protein Structure

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lec1-introduction

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nutritional terminology

... Adenosine Triphosphate; the ‘energy currency’ of the body; a nucleotide containing high-energy phosphate bonds which, when broken, release energy to power cellular metabolism. ...
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... 5. What are ketone bodies? 6. Give the energy value of one ATP molecule. 7. What is meant by β - oxidation? 8. What are porphyrins? 9. Mention the role of glutamate dehydrogenase. 10. What are primary metabolites? Part - B (8 x 5 = 40) Answer any five of the following questions, each within 350 word ...
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6 Review of Molecular Biology
6 Review of Molecular Biology

... codon) formed from a sequence of three nucleotides (e.g. ACT, CAG, TTT). These codons can then be transcribed into messenger RNA. The code is then translated for each amino acid to make a protein. Most amino acid, have more than one possible codon. There are also three 'stop' or 'nonsense' codons. ...
Biochemical Observations on a Non-Elite Marathon
Biochemical Observations on a Non-Elite Marathon

... changes, were seen in other non-essential amino acids (glycine, glutamine, serine). In contrast, the plasma concentration of valine (and other branched chain amino acids) was maintained during the whole period of running, and there were no substantial changes in other essential amino acids with the ...
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Lecture 14: Protein and Fat Synthesis

... (cutting) by endonuclease enzyme and coding sequences are ligased together to from mRNA. The spliced non-coding sequences are degraded within nucleus. It never goes out of nucleus. Thus, only fraction of hnRNA is translocated to cytoplasm from nucleus via nuclear pore. In eukaryotes migration of mRN ...
Biochemistry 2007
Biochemistry 2007

... The following statement is INCORRECT: (a) Oxygen (O2) molecule is positioned in oxyhemoglobin between the Fe2+ iron ion of the heme group and the proximal histidine residue HisF8 in the globin chain. (b) The secondary structure of globin chains in myoglobin and hemoglobin is characterized by a serie ...
PHARMACY BIOMEDICAL PREVIEW PROGRAM 2014
PHARMACY BIOMEDICAL PREVIEW PROGRAM 2014

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... • serial carrier molecules that are oxidized and reduced as electrons are passed down the chain • released energy can be used to produce ATP by chemiosmosis ...
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Amino Acid Synthesis Inhibitors-Group 2 Mode of

... Site of Action – Light causes the formation of free radicals. These radicals rupture plant cell membranes resulting in a rapid browning of tissue Translocation – None or very limited, necrotic spots Uses / Notes – Mostly foliar-applied - uptake into leaves – Some soil-applied - root and shoot uptake ...
Gene Section LTA (Lymphotoxin-A) Atlas of Genetics and Cytogenetics in Oncology and Haematology
Gene Section LTA (Lymphotoxin-A) Atlas of Genetics and Cytogenetics in Oncology and Haematology

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... 14. How does phosphorylation affect glycogen synthase and glycogen phosphorylase? 15. Enzymes called ______________________ oppose the action of kinases, turning off glycogen degradation and turning on glycogen synthesis. 16. Liver cells respond to glucagon by _________________________. 17. Muscle d ...
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L5 Metabolism Part2 Fa08

... Allosteric regulation • The binding of a regulatory molecule at one site on a protein that affects the function of the protein at another site • Most allosteric proteins have 2 or more subunits • Activator – stabilizes active form ...
SBI3U
SBI3U

...  Monomer is called a nucleotide (nt)  made up of a phosphate, sugar, and nitrogenous base ...
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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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