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Elements Found in Living Things
Elements Found in Living Things

... ratios. Each small organic molecule can be a unit of a large organic molecule called a macromolecule. If the small organic units are identical or form patterns they are called monomers and the large organic molecule they form is called a polymer. When monomers are joined together the reaction is cal ...
BCH 201 B
BCH 201 B

... of monosaccharide units joined together by covalent bonds (the most abundant are disaccharide) Polysaccharide 2: 2Consist 2of 2long 2chain 2 2having 2hundred 2or thousands of monosaccharide units. Eg. Cellulose (have linear chains), glycogen (have branched chain) Common mono & disaccharide have name ...
Gene Section ATF1 (activating transcription factor 1) Atlas of Genetics and Cytogenetics
Gene Section ATF1 (activating transcription factor 1) Atlas of Genetics and Cytogenetics

... The chimaeric protein is composed of the N-terminal domain of EWS linked to the bZIP domain of ATF-1. Oncogenesis Binds to ATF sites present in cAMP-responsive promoters via the ATF1 bZIP domain and activates transcription constitutively, dependent on the activation domain (EAD) present in EWSR1. ...
biochemistry - Kuliah FTSL
biochemistry - Kuliah FTSL

... Thousands of different enzymes exist in the body Enzymes control the rate of chemical reactions by weakening bonds, thus lowering the amount of activation energy needed for the reaction -> Catalysator -> No not interfere with the equilibrium of reaction -> Enzymes are reusable !!!! ...
Macromolecules: Proteins Chapter 3 pages 44
Macromolecules: Proteins Chapter 3 pages 44

... • Tau protein tangles like those in Benoit’s brain and ß-amyloid: • 1984: Scientists purified protein from the tangled fibrils seen in Alzheimer’s brains. • 1987: cloned the gene which coded for a 695 amino acid protein (ß-APP) which spanned the phospholipid bilayer. • ß-amyloid are fragments of the ...
FoldIndex©: a simple tool to predict whether a given protein
FoldIndex©: a simple tool to predict whether a given protein

... The web tool FoldIndex© , implementing the original Uversky algorithm, provides a single score for the entire sequence, predicting whether it is folded or not. The other methods calculate a separate fold score for each individual residue. In order to compare the various methods we obtained a fold sc ...
PROTEIN CHEMISTRY
PROTEIN CHEMISTRY

... forces that control protein folding. Attractive van der Waals forces involve the interactions among induced dipoles that arise from fluctuations in the charge densities that occur between adjacent uncharged nonbonded atoms. Repulsive van der Waals forces involve the interactions that occur when unch ...
Protein Conformation and Function
Protein Conformation and Function

... • Proteins also have isoelectric points depending on the amino acids that make them ...
Review Problems #2 (Enzyme Review, Phosphatases
Review Problems #2 (Enzyme Review, Phosphatases

... We will definitely not get through all of these, but it is useful to have them in one place. ...
AMINO ACIDS I. Function of amino acids A. Building blocks of
AMINO ACIDS I. Function of amino acids A. Building blocks of

... i. polypeptide chains side by side ii. polypeptide chains can be parallel or antiparallel iii. carbonyl oxygen hydrogen bonded to amide hydrogen iv. beta-strand is a single pass of the polypeptide c. reverse turn, beta-bend i. allows a sharp turn in polypeptide chain ii. carbonyl oxygen hydrogen bon ...
Chapter 11: Enzyme Catalysis
Chapter 11: Enzyme Catalysis

... E) the sulfur atoms in the ring can either gain or lose a proton at physiological pH. 13. Chymotrypsin, a serine protease, preferentially cleaves a peptide bond adjoining a bulky non-polar side chain. This is because chymotrypsin's specificity pocket: A) contains a sulfhydryl group that forms a disu ...
Modes of Macromolecular Classification
Modes of Macromolecular Classification

... series of nodal “connections” (if weak) between links of the amino acid chain. But this too underestimates the extent of a polypeptide’s flexibility. For one, tertiary structure depends very sensitively on folding order. While many proteins fold more or less spontaneously into their active forms (as ...
Unit 3 * Chapter 3 Biochemistry
Unit 3 * Chapter 3 Biochemistry

... ____________ – Many amino acids (can be 100’s) linked together by peptide bonds. ____________ = 1 or more polypeptides – often they bend and fold on one another to take on different 3D shapes and properties. ...
Necessary Components for Translation
Necessary Components for Translation

... Necessary Components for Translation 3. Ribosomal RNA (rRNA): • Ribosome is the site of protein synthesis. • Facilitates coupling of mRNA to tRNA. • Huge molecule: Large and small subunits must assemble for translation. • Ribosome composition: 60% rRNA and 40% protein • Transfer RNA (tRNA) Carries ...
Carbon (Organic) Chemistry
Carbon (Organic) Chemistry

... INTRODUCTION TO MACROMOLECULES ...
Proteiinianalyysi 5
Proteiinianalyysi 5

... % of yeast proteins using gene fusion information in any homologous proteins • Enright et al. (Nature 402:86-90, 1999) considered orthologs with higher signal-tonoise ratio but only 7 % coverage ...
Chapter 15 Review Questions
Chapter 15 Review Questions

... 10. Describe what an enzyme is, what it does, how it works and an example of an enzyme we discussed in class. 11. Name and describe 2 ways in which scientists can use DNA. ...
A Guided Reading on Macromolecules
A Guided Reading on Macromolecules

Lecture 3: Protein trafficking between cell compartments The cytosol
Lecture 3: Protein trafficking between cell compartments The cytosol

... • Vesicles (~ 300/cell) filled with ~ 40 acid hydrolases that has capacity to degrade more or less anything ...
Fundamentals of protein stability
Fundamentals of protein stability

... favourable AG; contribution to this type of interaction. Recent studies demonstrate a significant role of hydrogen bonds in the maintenance of the native structure of proteins. The 86 hydrogen bonds in ribonuclease T1 are reported to contribute as much as 460 kJ/(mole of enzyme) to the stability of ...
CH 3: The Molecules of Life
CH 3: The Molecules of Life

...  Can still function but very reduced rate ...
protein synthesis
protein synthesis

... GN#2: Protein Synthesis ...
Main Notes
Main Notes

... • Nucleic Acids are composed of Carbon, Hydrogen, Oxygen, and Nitrogen, Phosophorous • Nucleic Acids function in living things as the structure of DNA and RNA – The blueprint of life ...
Macromolecule Packet
Macromolecule Packet

... oxygen atoms. Fats are made of a glycerol (alcohol) and three fatty acid chains. This subunit is called a triglyceride. Color the glycerol molecule using the same colors for carbon, hydrogen, and oxygen as you did before. The fatty acid chains may be saturated (only single bonds between carbons) or ...
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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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