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Lect1.AAs.Peptides.pH.pK
Lect1.AAs.Peptides.pH.pK

... Asn is amidated version of Asp Gln is amidated version of Gln Asn and Gln are NOT charged, but are higly polar NH2 group on Gln in proteins can be site for carbohydrate addition (N-linked glycosylation) ...
CHAPTER 2 OBJECTIVE EXERCISE
CHAPTER 2 OBJECTIVE EXERCISE

... Secondary (2o) = twisting of amino acid chain; due to hydrogen bonding; Tertiary (3o) = folding of the amino acid chain; due to ionic bonds, disulfide bridges, and hydrophobic interactions; Quaternary (4o) = interactions between different amino acid chains A protein must be in its Quaternary structu ...
Classification of Enzymes - Lectures For UG-5
Classification of Enzymes - Lectures For UG-5

... Biochemistry an enzyme name has two parts: -First part is the name of the substrates for the enzyme. -Second part is the type of reaction catalyzed by the enzyme.This part ends with the suffix “ase”. Example: Lactate dehydrogenase ...
Ch. 2 Notes Organic Chemistry
Ch. 2 Notes Organic Chemistry

...  Example: salivary amylase in saliva– begins process of digestion ...
Topic 2: Molecular biology (21 hours)
Topic 2: Molecular biology (21 hours)

... carbohydrates, lipids, proteins and nucleic acids. • Aim 7: ICT can be used for molecular visualization of • Metabolism is the web of all the enzyme-catalysed carbohydrates, lipids and proteins in this sub-topic and reactions in a cell or organism. in 2.3 and 2.4. • Anabolism is the synthesis of com ...
Evolution of Metabolic Pathway
Evolution of Metabolic Pathway

... synthesized from oxaloacetates in a PEP carboxykinase-catalyzed ...
Proteins
Proteins

... • Protein conformation depends on the physical and chemical conditions of the protein’s environment • pH, salt concentration, temperature, and other aspects of the environment (aqueous or organic solvent) can unravel or change the conformation of the protein. • Change in protein shape causes it to l ...
MCB Lecture 7 – Peroxisomes
MCB Lecture 7 – Peroxisomes

... Does input require ATP? o Yes The Peroxisome can be biosynthetic. What is one of the important molecules it synthesizes? o It undergoes Plasmalogen synthesis, which is used in Myelin Sheaths of Axons The Peroxisome is also degradative. What is one of the important molecules it breaks down? o VLCFA ( ...
Topic 2: Molecular biology (21 hours)
Topic 2: Molecular biology (21 hours)

... Essential idea: Enzymes control the metabolism of the cell. 2.5 Enzymes Nature of science: 2.5.NOS1 Experimental design—accurate, quantitative measurements in enzyme experiments require replicates to ensure reliability. (3.2) Understandings: Theory of knowledge: 2.5.U1 Enzymes have an active site to ...
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... Molecule Z will function at any temperature above 20°C. Molecule Z is composed of a string of molecular bases represented by A, T, G, and Molecule Z will function best at a specific pH. Molecule Z is not specific, so this reaction can be controlled by any other chemical in the body. ...
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Nerve activates contraction

... • Are major sources of energy for cells! – Ex. Glucose – cellular respiration ...
Biochemistry Test Review (Vocabulary on the back page
Biochemistry Test Review (Vocabulary on the back page

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peptides - WordPress.com

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Ras and macropinocytosis: trick and treat

... and proliferation. Macropinocytosis, a clathrin- and caveolin-independent endocytotic process that had previously been linked to the action of oncogenic Ras and Src, is now shown to contribute to amino acid uptake via enhanced delivery of extracellular proteins to lysosomes. Tumorigenesis is a multi ...
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Name: MACROMOLECULES Date: I. ELEMENTS AND

... inside organisms. They also act as enzymes helping to control metabolic reactions in organisms. Amino acids contain two functional groups, the carboxyl group (-COOH) and the amino group (-NH2). Task: Color code the amino acid to the right ------------------> (carbon-black, hydrogen-yellow, and oxyge ...
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Option C - Human biochemistry C.1 Diet-

... C.5.1 Role in Metabolism: • -Metabolism- all of an organism's biochemical reactions • -In order for reactions to take place in the body, catalysts are needed-these are called enzymes (see section on enzymes for more info) • -Enzymes do not work alone, and sometimes require the help of coenzymes in ...
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документ

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Slide 1

... body  Examples (that were not mentioned in class or text) of a solution, a colloid, a suspension and a homogenous mixture with the reasons why. ...
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Supplementary Information

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Preparation and transformation of competent bacteria: Calcium
Preparation and transformation of competent bacteria: Calcium

... 12. Explain what refseq is. (You will have to search the NCBI Web Site to find this – go back to the home page and select NCBI Web Site from the drop down list). ...
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... reactant binds to an enzyme at a region known as the_______ • Active site ...
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File

... • Double helix (Watson and Crick, 1953). 2 chains of nucleotides with sugar and phosphate on the outside (hydrophilic) and nitrogenous bases on the inside (hydrophobic). • Precise pairing of bases such that A = T and C = G. Chains held together with hydrogen bonds. Each strand is the template of the ...
E U F T DG Unfolded state, ensemble Native fold, one
E U F T DG Unfolded state, ensemble Native fold, one

... • “Breathing” motions on pico- to nanosecond scale. • Allows substrates/products to enter/leave enzymes. • Allows allosteric regulation of activity. ...
Understanding an Enzyme Active Site
Understanding an Enzyme Active Site

... alpha helices and/or beta sheets (secondary structure) connected by short turns of less regular protein structure. In the space below, draw and label examples of primary, secondary and tertiary structures. ...
Protein synthesis
Protein synthesis

... are coded for by an mRNA sequence. For example, the codon 5'-AUG-3' codes for methionine Sixty-one of the 64 codons code for the 20 common amino acids. ...
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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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