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Organic Compounds
Organic Compounds

... There are 20 different kinds of amino acids in proteins. ...
erp013_60_3_combined 709..714 - Journal of Experimental Botany
erp013_60_3_combined 709..714 - Journal of Experimental Botany

... however, the result is completely unexpected—it was an unknown unknown. There are many known knowns of intracellular protein targeting and, as with many fields of research, it seems that the number of known unknowns increase in parallel. The ...
Basics of Biology (part 3): transcripCon, translaCon ADN, ARNs
Basics of Biology (part 3): transcripCon, translaCon ADN, ARNs

... -> it binds to a specific amino acid! -> it contains the anticodon that binds to the corresponding codon on mRNA! ...
Proteins: Their Bio-Chemistry and Functions
Proteins: Their Bio-Chemistry and Functions

... in four major groups according to their characteristics. ...
EXPLORING PROTEIN STRUCTURE
EXPLORING PROTEIN STRUCTURE

... the proteins that you eat and digest. Every time you eat a burger (vege or beef), you break the proteins down into single amino acids ready for use in building new proteins. And yes, proteins have the job of digesting proteins, they are known as proteases. There are only 20 different amino acids but ...
Organic Chemistry Answer Key
Organic Chemistry Answer Key

Bio-201-chapter-5-MEC
Bio-201-chapter-5-MEC

... • Enzymes that digest starch by hydrolyzing  linkages can’t hydrolyze  linkages in cellulose • Cellulose in human food passes through the digestive tract as insoluble fiber • Some microbes use enzymes to digest cellulose • Many herbivores, from cows to termites, have symbiotic relationships with ...
Self-assembly of Proteins
Self-assembly of Proteins

... catalysts! For example, the enzyme urease acts only on urea to convert it to carbon dioxide and ammonia. It does not act on any other substrate. Proteins also exhibit highly specific binding affinity, which enable enables them to function as membrane bound receptors receptor or as antibodies, an imp ...
Protein Surgery Increases Protein Demands in the Body Getting
Protein Surgery Increases Protein Demands in the Body Getting

... White-Meat Poultry: Stick to the white meat of poultry for excellent, lean protein. Dark meat is higher in fat. The skin is loaded with saturated fat, so remove skin before cooking. Milk, Cheese, Yogurt: Not only are dairy foods excellent sources of protein but they also contain valuable calcium. Ch ...
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What more do we need to know to optimize the

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Chapter 16
Chapter 16

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Unit 10 web
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Chapter 22-23 - Bakersfield College
Chapter 22-23 - Bakersfield College

... • Held by H bonds between the H of N-H group and the O of C=O of the fourth amino acid down the chain (next turn). • looks like a coiled “telephone cord.” • All R- groups point outward from the helix. • Myosin in muscle and α-Keratin in hair ...
the essence of life
the essence of life

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18.2 Protein Structure and Function: An Overview
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... carbon. The remaining amino acid (proline) is a secondary amine whose nitrogen and carbon atoms are joined in a five-membered ring. ► Each amino acid has a three-letter shorthand code: Ala (alanine), Gly (glycine), Pro (proline), etc. ► The 20 protein amino acids are classified as neutral, acidic, o ...
Molecular Machines (1MB429) Exam 2011-12-21
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... (b) Arp2/3 complex (Arp=Actin related protein) nucleates the branching of actin filaments. What is the mechanism of this nucleation? What role does the activator domain of WASP protein play in this process? How does Cdc42 GTPase activate WASP? (6p) Answer: The Arp2/3 complex contains, apart from oth ...
Biochemical Analysis of the Binding Interaction between LanI and its
Biochemical Analysis of the Binding Interaction between LanI and its

... Previous studies have shown that despite the similar amino acid sequence and ring topology conformation between nisin and subtilin, NisI (L. lactis) is only able to interact with nisin (KD of 0.6 - 2.0 uM), but not subtilin, indicating the specificity of LanI proteins. SpaI (B. subtilis), which shar ...
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... 1. Initiation – attachment of mRNA to the ribosome (This was already covered in Step # 3) 2. Elongation – the addition of amino acids to the growing protein chain A Site ...
Unit 1.1 Molecules.pps
Unit 1.1 Molecules.pps

... from two monosaccharides  Joined by a glycosidic bond  A condensation reaction: ...
Enzymes I
Enzymes I

... o a family of enzymes that hydrolyze specific peptide bonds in proteins (i.e., splits the protein into smaller polypeptides) o Each enzyme in the family hydrolyzes amide bonds adjacent to specific amino acid residues. o Main area of function: Digestion o Serine proteases are synthesized in the pancr ...
Bio392 - Chapter 2-3 - notes
Bio392 - Chapter 2-3 - notes

... • Monomer =  Amino acid There are 20 amino acids total ...
CHM 20 EXAM 3 – REVIEW Name Ms Dang Indicate whether each
CHM 20 EXAM 3 – REVIEW Name Ms Dang Indicate whether each

... In each case, the two adjacent amino acids each have a negative charge. Two adjacent side chains will be close to one another if they are in the helix, so they will repel each other if they have the same charge 14. Why does the body need so many different enzymes? There are thousands of different ki ...
09.06.11 Intro to Biochemistry w. Clinical
09.06.11 Intro to Biochemistry w. Clinical

... •  Historical: 1957 Solved Crystal Structures –  The first three-dimensional protein structures (myoglobin and hemoglobin) were determined by M.F.Perutz and J. C. Kendrew (Mb at 6 A resolution in 1957, Nobel Prize in Chemistry in 1962). The entries are included in the PDB (PDB codes: 1mbn and 2dhb). ...
Name: JJJJJJJJJJJJJJJJJJJJ Student ID: JJJJJJJJJJJJJJJJJJJJJJJ
Name: JJJJJJJJJJJJJJJJJJJJ Student ID: JJJJJJJJJJJJJJJJJJJJJJJ

Exam 2 Full KEY v1 Bio200 Sum12
Exam 2 Full KEY v1 Bio200 Sum12

... necessary. You should do this in less than one sentence for each mutation (If necessary, you can use two short sentences). Research outside of Bio200 lectures and labs is not necessary, but is allowed if you want to find specific examples of parts of this question. Show the diversity of what you kno ...
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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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