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BIOL 1322 - Victoria College
BIOL 1322 - Victoria College

... What are enzymes? What roles do they play in chemical reactions? Describe the differences between enzymes and hormones. ...
Cellular Functions PP
Cellular Functions PP

... The protons then diffuse through a special proton channels called ATP synthase, down the concentration gradient back into the matrix of the mitochondria, creating ATP in the process. Chemiosmosis is the coupling of the protonmotive force and ATP synthesis. The final electron acceptor is Oxygen which ...
Unit 15.1 Water and Protein as Nutrients
Unit 15.1 Water and Protein as Nutrients

... B. Digestion to breakdown nutrients C. Movement of feed through the digestive tract D. Produces milk E. Provides cells with pressure to maintain their shape F. Helps the body maintain a constant temperature G. Flushes the animal=s body wastes and toxic materials ...
Protein Synthesis Notes
Protein Synthesis Notes

... to a transfer RNA molecule. The tRNA molecule is a single strand of RNA that loops back on itself. At one end it has 3 bases called an ANTICODON, At the other end the corresponding amino acid is attached. The CODON of the mRNA attaches to the ANTICODON of the tRNA molecule. For example, if the mRNA ...
Slide 1
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... are central to whole body amino acid catabolism. Ammonia released from aa oxidation is transported to the liver in the form of glutamine for urea synthesis. Alanine production from the muscles serves as the main gluconeogenic precursor for both liver and kidney. ...
FPIA - IMGT
FPIA - IMGT

... 1. The notion of ligand is often associated to ‘soluble’ or ‘secreted’ protein, however in the immune system many of the interactions are between membrane proteins. So a ligand can be either a soluble protein or a membrane protein at the cell surface (GPI-anchored or transmembrane). It can be also i ...
activity 2-2. organic chemistry
activity 2-2. organic chemistry

... Enzymes are proteins that act as catalysts in living cells. A catalyst increases the rate of a chemical reaction, allowing it to proceed rapidly when it would otherwise occur only very slowly. Enzymes are highly specific in their catalytic activity. The specificity of enzyme action is the result of ...
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... BACK AND CHECK THE STRUCTURES AND SEE WHY THIS SHOULD BE SO. ...
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August 31, 2016 - Iowa State University

... 1. How many amino acids are there and what are their four main groups? ...
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... Consists of four types of nucleotides A bound to T C bound to G ...
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... There are about 20 different amino acids in nature and these differ in the atoms which make the R group. The body cannot make all the amino acids required for body proteins and is dependent on dietary protein for supply of certain amino acids known as essential amino acids. Only eight amino acids ar ...
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Lecture 5-Bioinorganic Chemistry

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`Chargaff`s Rules` for Protein Folding: Stoichiometric Leitmotif Made
`Chargaff`s Rules` for Protein Folding: Stoichiometric Leitmotif Made

... peptide backbones (14). In the case of oxidative folding of antibody Fab fragment, formation and re-arrangement of disulfide bonds is involved, and so, enzymes such as protein disulfide isomerase need to enter into the picture. Thus, it is apparent that it is not just stoichiometry (two cysteine mol ...
Protein Synthesis Instructions
Protein Synthesis Instructions

... Understand how a cell manufactures proteins from amino acids, using information stored in the genetic code. Assemble models of four very short proteins based on four mRNA sequences. ...
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introduction

... A and B sequences have been selected to present different challenges. The team members should work together on both sequences, discussing the findings between them and making notes for the final report (presentation). Sequences are here: ...
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... o Understanding chemical equations, what all the symbols and numbers mean and which substances are the reactants and products. Example: photosynthesis and cellular respiration o Determine if an equation is balanced: Law of Conservation of Matter o Identify the number of atoms of each element found i ...
Molecular Biology Final Exam (Set A)
Molecular Biology Final Exam (Set A)

... basepairs wherever its sequence allows. Since this internal basepairing relies on self-complementary sequence, the way in which an RNA molecule folds is dependent on its nucleotide base sequence, and thus is different for every RNA. The implications of this are that RNA has a much wider range of thr ...
(codons) make a specific amino acid
(codons) make a specific amino acid

Solubility of proteins
Solubility of proteins

... Not all Proteins are produced by the cell in equal amounts! Favored research drug targets (signal proteins) are actually low in abundance! ◦ kinases, ◦ proteases ◦ hydrolases of all sorts ◦ receptors (most likely) ◦ Researcher needs to aim for regulatory choke point and bottleneck proteins for targ ...
Protein Synthesis and Degradation
Protein Synthesis and Degradation

... Crystal Structure of the Ribosome at 5.5 A Resolution. We describe the crystal structure of the complete Thermus thermophilus 70S ribosome containing bound mRNA and tRNAs at 5.5 A resolution. All of the 16S, 23S and 5S rRNA chains, the A-, P- and E-site tRNAs, and most of the ribosomal proteins can ...
Biomolecule SG_answers
Biomolecule SG_answers

... -- made up of 20 different ___amino acids____ -- transport minerals (hemoglobin carries _oxygen__) -- controls chemical reactions (__enzymes_____) -- produces antibodies – fight germs -- assist in muscle movement ...
Protein Model Refinement
Protein Model Refinement

... a) Global alignment of regions that lack similarity and then search for similar regions. b) Local alignment in regions with significant similarity first, and then align regions of optimally aligned residues. To prepare sequences a database Sequence to Coordinates (S2C) is used to examine the differe ...
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Module name Bioinformatics Module code B

... Non-contact hours (students' own work) – 15 Total number of non-contact hours – 15 Number of ECTS points for non-contact hours – 0.5 Total number of ECTS points for the module - 1 Continuous evaluation of the computer classes The course will familiarize students with the bioinformatics tools for sea ...
Fibrous and globular proteins Structure
Fibrous and globular proteins Structure

... Function of cross-linking These cross-links stabilize the side-by-side packing of collagen molecules and generate a strong fibril If cross-linking is inhibited, the tensile strength of the fibrils is drastically reduced; collagenous tissues become fragile, and structures such as skin, tendons, and ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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