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Lecture 5: Basic Plant Biochemistry: Carbohydrates, Proteins
Lecture 5: Basic Plant Biochemistry: Carbohydrates, Proteins

... • Physical and chemical conditions of protein’s environment like pH, temperature, salt concentration, etc. Under some conditions, proteins undergo denaturation where in they unravel and loose their conformation. This loss in the conformation may lead to loss in their function. Nucleic Acids: -Are i ...
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Molecular Basis for Relationship between Genotype and Phenotype
Molecular Basis for Relationship between Genotype and Phenotype

... Anticodon of a tRNA molecule recognizes and pairs with an mRNA codon. tRNA contains modified bases: pseudouridine, methylguanosine, dimethylguanosine, ...
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Notes - Part 2.

Protein Nanocages - Nanyang Technological University
Protein Nanocages - Nanyang Technological University

... interactions and acts as a shuttle to ferry the macromolecule cargos into the vault.[7] Towards applications in targeted delivery of the therapeutic cargo, the external surface of the protein nanocages can be decorated with peptides that can aid in binding to the surface of cancer cells.[8] Besides ...
Slide 1
Slide 1

... oil for frying causes some of the cis bonds to convert to trans bonds. If oil is used only once like when you fry an egg, only a few of the bonds do this so it’s not too bad. However, if oil is constantly reused, like in fast food French fry machines, more and more of the cis bonds are changed to tr ...
Enzyme Vs. Extremozyme -32
Enzyme Vs. Extremozyme -32

... decreasing free energy (10-15 KcaVmol) due to disulfide bond and other physical interactions. Sometimes two different polypeptides (subunits) having a tertiary structure interact in space and form a stable structure called quaternary structure. It is in the tertiary and quaternary structural forms t ...
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Milk Synthesis

... used as a source of energy for the cells ( the other half will be used to crate lactose). CH3CH2COOH ...
α-N-Acetylgalactosaminidase as a tools in the synthesis of complex
α-N-Acetylgalactosaminidase as a tools in the synthesis of complex

... cells is via N-glycosidic linkage. The site of carbohydrate attachment to Nlinked glycoproteins is found within a consensus sequence of amino acids, N-XS(T), where X is any amino acid except proline. While the N-glycosylation is governed by the above rules, no exact rules were found for glycosylatio ...
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... • Collagen is a fibrous protein of three polypeptides that are supercoiled like a rope. • This provides the structural strength for their role in ...
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Characteristics of the caspase-like catalytic domain of

... a family of de-sumoylating proteases; and clan CD encompassing the five families, caspases, legumains, gingipains, clostripain, and separase. Recently, bioinformatics approaches have identified two further families within this clan: the paracaspases and the metacaspases (Uren et al., 2000). Each sha ...
Medical Biochemistry and Molecular Basis of Medical
Medical Biochemistry and Molecular Basis of Medical

... 13. A newborn child is eliminating valine in his urine. This suggests the child a. has acaptonuria. b. has a deficiency in the α-ketoacid dehydrogenase needed to metabolize valine. c. cannot metabolize leucine and isoleucine. d. All of the above. 14. You and your study partner are having an argument ...
From DNA to Protein: Transcription and Translation
From DNA to Protein: Transcription and Translation

... mRNA codon pairs up, carrying the corresponding amino acid. •A second tRNA pairs with the next codon, and the two amino acids are joined by a peptide bond. •The mRNA is slide down the ribosome bringing the next codon to the tRNA binding site. •This process continues, building the protein, until a st ...
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Chapter 8

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Overview of Inherited Metabolic Disorders

... function and result in clinical abnormality  Based on physiological function(s) affected  Based on organ(s) affected  Based on severity of mutation and resulting deficiency of protein-mediated biochemical function  Recognition often difficult clinically and usually requires laboratory support fo ...
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Preview Sample 1 - Test Bank, Manual Solution, Solution Manual

... Chemistry has never been a very popular subject among beginning students of microbiology. It is often initially difficult for students to understand that a knowledge of basic, especially organic and biochemical chemistry, is fundamental to a functional understanding of the many structures that bacte ...
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Chapter 3 Molecules

... b. In 2006, the U.S. Food and Drug Administration required the listing of trans fat on food labels. c. Many cities and states have passed laws to eliminate trans fats in unlabeled foods served in restaurants and schools. d. An increasing number of countries have banned trans fats. 4. Experimental st ...
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13.2 Ribosomes and Protein Synthesis

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Ch.24Pt.7_000
Ch.24Pt.7_000

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Biochemistry 3100 Sample Problems Binding proteins, Kinetics & Catalysis eg
Biochemistry 3100 Sample Problems Binding proteins, Kinetics & Catalysis eg

... carboxylate containing residue (Glu most likely) and His. Note: the pkas can be determined by extrapolating the slope of each side of the bell curve and the  plateau region. The intersection between the extrapolated slope and plateau lines gives the pkas. 13b – If the catalytic residues had pKa's th ...
HMK 6 Digestive System - Bannerman High School
HMK 6 Digestive System - Bannerman High School

... The diagram shows a picture of human teeth. 1. Describe the role teeth play in the digestive system? ...
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are PROTEINS!!!!!!

... • Nucleic acids direct the construction of proteins. The genetic information an organism receives from its parents is in the form of nucleic acids. ...
Evolutionary Rate in the Protein Interaction Network
Evolutionary Rate in the Protein Interaction Network

... connectivity of well-conserved proteins in the network is negatively correlated with their rate of evolution. Proteins with more interactors evolve more slowly not because they are more important to the organism, but because a greater proportion of the protein is directly involved in its function. A ...
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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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