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University of Groningen The influence of peptide structure on
University of Groningen The influence of peptide structure on

... of H2 O (see fig. 2.2). When more α –amino acids are linked this way, a linear polypeptide chain, often called peptide, is formed. Larger peptides are usually referred to as proteins or protein chains. Most natural protein chains contain between 50 and 2000 amino acid residues. Each protein has a un ...
powerpoint 24 Aug
powerpoint 24 Aug

... amylase to break down starch it must bind the starch. It can only bind starch because its tertiary structure results in the formation of a binding site.  Quaternary structure would be more than one peptide chain associated with each other to form a functioning protein, but amylase is just one pepti ...
Protein basics - Crop Genebank Knowledge Base
Protein basics - Crop Genebank Knowledge Base

... moves to the ‘ribosome’, an organelle in charge of making proteins. Every set of three bases in the RNA determines which amino acid is added to the protein molecule in progress. The RNA chain passes through the ribosome until the protein is complete. This process has been called ‘the central dogma’, ...
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Slides - Websupport1

... enerates an ammonia (NH3) molecule or an ammonium ion (NH4+). Ammonia molecules are highly , thus liver (the primary site of deamination) has enzymes that converts the ammonia to urea ...
CHAPTER 4: CELLULAR METABOLISM
CHAPTER 4: CELLULAR METABOLISM

... 1. CR is how animal cells use oxygen to release chemical energy from food to generate cellular energy (ATP). 2. The chemical reactions in CR must occur in a particular sequence, with each reaction being catalyzed by a different (specific) enzyme. There are three major series of reactions: a. glycoly ...
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... __56) The element nitrogen is present in all of the following except: a) proteins b) nucleic acids c) amino acids d) DNA e) lipids __57) Which of the following is true of an amino acid and starch? a) both contain nitrogen c) both are polymers e) both found in DNA b) both contain oxygen d) both are h ...
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A Protein Extract from Chicken Reduces Plasma Homocysteine in Rats

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Isolation and Purification of RP2-L, a Nuclear Protein Fraction of the

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BIO00004C Molecular biology and biochemistry (PDF , 72kb)
BIO00004C Molecular biology and biochemistry (PDF , 72kb)

... depend on the subjects covered in the module. It then covers the basic chemical building blocks of cells, from elements to macromolecules. The structure of nucleic acids will be introduced, and its importance to the mechanism of DNA replication. Then, the different levels of protein structure will b ...
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4 slides pdf

... Unique sequence of amino acids in protein is determined by order of nucleotide bases in gene. Protein’s 3-D structure is critical to its function: • shape and function of protein is determined by amino acid ...
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TCA Cycle - eCurriculum

... ­ Pyruvate carboxylase reaction: Alternate way of using pyruvate to make oxaloacetate.  Important in liver and nervous tissue because they have a constant efflux of intermediates from  the TCA cycle.  ­ Conversion of amino acids (isoleucine, valine, methionine) and odd chain fatty acids into  succin ...
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Homework # 9 Citric Acid Cycle, electron transport Chain, and
Homework # 9 Citric Acid Cycle, electron transport Chain, and

... can also be used to synthesize amino acids needed or not present in the diet. An amino acid may be synthesized if there is an available "root" ketoacid with a synthetic connection to the final amino acid. Since an appropriate "root" ketoacid does not exist for eight amino acids, (lys, leu, ile, met, ...
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Chapter 26 - s3.amazonaws.com

... If ATP c.c. for a reaction in one direction differs from c.c. in the other, the reactions can form a substrate cycle • The point is not that ATP can be consumed by cycling • But rather that the difference in c.c. permits both reactions (pathways) to be thermodynamically favorable at all times • Allo ...
MBMB451A Section1 Fall 2008 KEY These questions may have
MBMB451A Section1 Fall 2008 KEY These questions may have

... sure to highlight the features of the DNA as well as the protein that are important in this intermolecular interaction. (7points) Keywords – DNA sequence recognition ( donor and acceptor sites in neucleotide base and proteins), alpha helix used to bind inside of the major groove and minor groove rec ...
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Exam-2 review

... - 19. Know the 10 functions of proteins. In the face of protein deficiency, understand how health would be affected in the context of any of these functions. - 20. Protein can be used for energy, is this a low or high priority for protein use? - 21. If amino acids are used for energy what must first ...
high energy bond
high energy bond

... molecules Products are large molecules Protein, peptidoglycan, DNA, RNA Mediated by enzymes E required (endergonic) ...
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video slide

... – Are lipids characterized by a carbon skeleton consisting of four fused rings ...
Chapter 5 The Structure & Function of Molecules
Chapter 5 The Structure & Function of Molecules

... – Are lipids characterized by a carbon skeleton consisting of four fused rings ...
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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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