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Islamic University of Gaza Advanced Biochemistry Faculty of
Islamic University of Gaza Advanced Biochemistry Faculty of

... Time: 2 hours ...
03_Physical-chemical properties of proteins
03_Physical-chemical properties of proteins

... Carbohydrates ...
File
File

... movement, and defense against foreign substances. ○ Most important, protein enzymes function as catalysts in cells, regulating metabolism by selectively accelerating certain chemical reactions without being consumed. Lecture Outline for Campbell/Reece Biology, 8th Edition, © Pearson Education, Inc. ...
Class Notes
Class Notes

... movement, and defense against foreign substances. ○ Most important, protein enzymes function as catalysts in cells, regulating metabolism by selectively accelerating certain chemical reactions without being consumed. Lecture Outline for Campbell/Reece Biology, 8th Edition, © Pearson Education, Inc. ...
Lecture outline handouts
Lecture outline handouts

... ○ While polymers built with α glucose form helical structures, polymers built with β glucose form straight structures. ○ The straight structures built with β glucose allow H atoms on one strand to form hydrogen bonds with OH groups on other strands. ○ In plant cell walls, parallel cellulose molecule ...
Biomolecules
Biomolecules

... Disaccharides – are two simple sugars bonded together. (cannot be longer or shorter) Polysaccharides – are greater than 2 simple sugars joined together. ...
Slide 1
Slide 1

... identical molecules, in protein these molecules are different. Protein is made up of chains of amino acids. There are over 20 different kinds of amino acid. Protein is used to allow the body to grow and to repair the body. ...
Pangborn Jon Toronto 2009
Pangborn Jon Toronto 2009

... • Considering ASD people as a group, there are cell-wide and extracellular anomalies. • Don’t get hung up on one enzyme/protein, one cell compartment, one gene, one epigenetic process, one cytokine, one toxicant or infectious agent or any single theory or model. ...
AP Biology
AP Biology

... are reused many times before the body gets rid of them. ...
For lecture notes click here
For lecture notes click here

... down anaerobically to pyruvic acid. Two molecules of NADH are also produced. In most cells, electrons are passed from NADH to FAD by means of an intermediate in the intermembrane space and then to CoQ and the electron transport system. This sequence of events ultimately provides an additional 4 ATP ...
Unit 10 web
Unit 10 web

... ~300g is replaced daily by recycling and intake. We need to take in * ~70g of high quality protein or ~80g of lower quality ...
Protein Synthesis:
Protein Synthesis:

... In eukaryotes amino acid encoded by the start codon is methionine. In bacteria, the protein starts instead with the modified amino acid Nformyl methionine (f-Met). In f-Met, the amino group has been blocked by a formyl group to form an amide, so this amino group can not form a peptide bond. This is ...
Protein Synthesis:
Protein Synthesis:

... In eukaryotes amino acid encoded by the start codon is methionine. In bacteria, the protein starts instead with the modified amino acid Nformyl methionine (f-Met). In f-Met, the amino group has been blocked by a formyl group to form an amide, so this amino group can not form a peptide bond. This is ...
1. Organisms that synthesize organic molecules from inorganic
1. Organisms that synthesize organic molecules from inorganic

... 1. Organisms that synthesize organic molecules from inorganic molecules thereby making their own food are _____. a) autotrophs b) heterotrophs c) prokaryotes d) eukaryotes 2. Which name is another name for the Krebs cycle? a) chemiosmotic cycle b) mediated transport cycle c) Calvin cycle d) citric a ...
Protein Structure
Protein Structure

... ligases to attach additional ubiquitin molecules.  The result is a polyubiquitin chain that is bound by the proteasome, allowing it to degrade the tagged protein. ...


... Available in: http://www.redalyc.org/articulo.oa?id=367937042005 ...
Re-identification of the N-terminal amino acid residue and its
Re-identification of the N-terminal amino acid residue and its

... interpreted in terms of stability of proteins in a living cell. According to the N-end rule (Tobias et al. 1991; Varshavsky 1992), both Ala and Glu in bacteria are stabilizing residues that protect proteins against intracellular proteolytic degradation. The Ala residue does not prevent the removal o ...
Importance of Amino Acid Side Groups for Biologic
Importance of Amino Acid Side Groups for Biologic

... peptide for pressor activity to result. It is possible, however, that an enzynme, contained intracellularly or absorbed on the surface of isolated muscle preparations, might convert angiotensin I to II. The degree of this conversion to angiotensin II was measured by the increase in oxytocie activity ...
Document
Document

... 7. Name molecules can produce ATP(energy) other than sugars. What are the product names can be used as a energy and waste produce after producing ATP or energy source? Protein- Ketone acid(as a energy source), Urea (Waste), Fat – Keto bodies(as a energy source) 8. Name the pathway before an amino ac ...
1 slide per page
1 slide per page

Biological Molecules Review Questions 2015
Biological Molecules Review Questions 2015

... C. are made up of amino acids and glycerol. D. have double bonds in their carbon chains. 38. Which of the following are components of a phospholipid? A. cholesterol, glycerol, fatty acids B. fatty acids, phosphate group, glycerol C. glycerol, amino acids, phosphate group D. phosphate group, choleste ...
6-Catabolism of Pyrimidine Nucleotides
6-Catabolism of Pyrimidine Nucleotides

... Both b-alanine, and b-aminoisobutyrate can be further converted into acetyl-CoA and succinyl-CoA, respectively, or are excreted in the urine. ...
Gene Expression
Gene Expression

... 1. Be able to describe the types of information coded in DNA. 2. Be able to identify the structural components of RNA. 3. Be able to distinguish RNA from DNA both structurally and functionally. 4. Be able to describe, in order, the steps involved in producing a functional mRNA molecule, starting wit ...
Chapter 4 The Importance of High
Chapter 4 The Importance of High

... -How is the protein synthesis (having positive ΔG value of 0.5 kcal/mole for each peptide bond) possible thermodynamically? -Biosynthesis is almost always coupled with energy consumption (소모) of negative ΔG (e.g., hydrolysis of ATP) adenosine-O-P~P~P + H2O Æ adenosine-O-P~P + P (ΔG = -7kcal/mole) ad ...
A^2
A^2

... (C)  Structure  predic>on:
 from  sequence  to  structure (c) Protein threading No homologous structure available? ☞ Into which known fold fits the sequence best? ...
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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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