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Structural
Structural

... Reduced ...
The Molecules of Life
The Molecules of Life

... Tertiary is based on other interactions (hydrophobic and hydrophilic interactions, covalent, and non-covalent bonds) Quaternary is based on the various interactions between two or more polypeptides to give a functional protein Because the 3-D shape of a protein is crucial to its function, even sligh ...
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Nuclear Envelope - Plain Local Schools
Nuclear Envelope - Plain Local Schools

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... Nonpolar (hydrophobic):glycine, alanine, valine, leucine, isoleucine, methionine, phenylalanine, tryptophan and proline ...
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Recombinant Human Neuregulin-1 (rh NRG-1)

... Introduction: Neuregulin/Heregulin is a family of structurally related polypeptide growth factors derived from alternatively spliced genes (NRG-1, NRG-2, NRG-3 and NRG-4). To date, there are over 14 soluble and transmembrane proteins derived from the NRG-1 gene. Proteolytic processing of the extrace ...
NS 315 Unit 6: Proteins
NS 315 Unit 6: Proteins

...  Protein: Large organic compounds made of amino acids arranged in a linear chain and joined together by peptide bonds between the carboxyl and amino groups of adjacent amino acid groups ...
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... Complete protein foods have all the essential amino acids. In general, animal food such meat, poultry, eggs, diary and fish are complete protein sources. Incomplete protein source have only low amount of some of the essential amino acid. Combining two or more incomplete proteins, can provide adequat ...
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Summary of Endomembrane

... (1)Glycosylation. (2)Protein sorting (3)Cell secretion (4)Biogenesis of Lysosomes. 20. Golgi complex plays a key role in the assembly of the carbohydrate component of glycoproteins and glycolipids. 21. The core carbohydrate of N-linked oligosaccharides is assembled in the rER. Modifications to N-lin ...
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The macromolecular sites of action through which drugs

... hydrophobic residues to solvent, and may contain partially desolvated hydrophilic groups that are not paired with complementary hydrogen bonding residues. These hydrophilic groups in this area are probably not exposed to sufficient solvent due to the steric constraints of protein folding. This means ...
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Protein Synthesis - Helena High School
Protein Synthesis - Helena High School

... 4. What is the goal of transcription? 5. Where does transcription take place in eukaryotic cells? 6. What RNA molecule copies the DNA code to serve as a template to make proteins? 7. If a section of DNA has the following order of bases, what would the complementary mRNA be? DNA segment: ...
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The Basics: A general review of molecular biology: DNA

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Supplemental Materials and Methods

... tetracycline, IPTG, and X-gal per the manufacturer’s protocols. White colonies were selected from these plates, and bacmid DNA was generated by alkaline lysis plasmid preparation and verified by PCR amplification across the bacmid junctions. Proteins were expressed in either insect SF5 or HEK293 mam ...
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Proteins in nutrition

... amino acids (see above). Higher amount is utilized as energy source after deamination: ...
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AASK Student Handout 3

... which are present in alpha helices and beta sheets, stabilize the structure of a real protein. You now have a stable 3D structure – upon which you can precisely place three specific amino acid side chains to create an enzyme active site. ...
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Study Guide for Understanding the Concept of Protein Synthesis

... Transfer RNA (tRNA) acts as a "taxi" by which the "escort" ribosomes take the amino acids and position them into place as Ribosomal RNA (rRNA). Step #5: Ribosomes: From the rRNA, the amino acids continue their journey within the cytoplasm, resting on "floating" ribosomes or on the Rough ER. These ri ...
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... c. May have evolved from gibbons but not rats d. Is more closely related to humans than to rats e. May have evolved from rats but not from humans and gibbons 8. Proteins like hemoglobin and insulin have different structures because they have different ______________________, which is also known as t ...
BIG TEST ON THUR/FRI!
BIG TEST ON THUR/FRI!

... • Histones – “spools” around which DNA winds • ENZYMES!!! – speed up reactions in body, help break down molecules ...
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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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