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Macromolecules of the Human Body
Macromolecules of the Human Body

REGULAR BIOCHEMISTRY UNIT GUIDE Due Thurs, 9/10 Monday
REGULAR BIOCHEMISTRY UNIT GUIDE Due Thurs, 9/10 Monday

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Protein Structure and Function

... If the transition state can be bound more tightly than the substrate, activation energy will be reduced The differential binding of enzyme for these two state Is the driving force of reactions ...
Microbial Metabolism
Microbial Metabolism

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Molecules of Life – Part 2

... 4. A variety of bonds (covalentcovalent, ionic, hydrogen) between distant amino acids causes large folds in the protein. These help provide stability to the folded protein. 5. Quaternary Structure (4’ ) “Quarter” means “fourth” a. This is when two or more polypeptides are woven together. b. Hemoglob ...
Catalytic Mechanisms Acid-Base Catalysis Covalent Catalysis Metal
Catalytic Mechanisms Acid-Base Catalysis Covalent Catalysis Metal

... Tetrahedral intermediate decomposes to acyl-enzyme intermediate by His57 (general acid) Acyl-enzyme intermediate is deacylated by reverse of above steps, release of carboxylate product, H2O is nucleophile and Ser195 is leaving group Enzyme prefers binding transition state to either Michaelis complex ...
Ch. 5: Note Stems
Ch. 5: Note Stems

... carbon, circle the water molecule to be removed and then note the peptide bond formed when the two are joined. ...
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Biotechnological Tools and Techniques
Biotechnological Tools and Techniques

... Biotechnology • the use of living organisms in industrial, agricultural, medical, and other technological applications • there are many biotechnological tools and techniques used to gain knowledge of and to manipulate DNA ...
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Biomolecules Fill in the crossword puzzle by using

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Levels of Organization - Bremen High School District 228
Levels of Organization - Bremen High School District 228

... 3. Proteins are polymers of amino acids a. Amino acids are compounds with an amino group (NH₂) at one end and a carboxyl group (COOH) at the other. b. There are 20 different amino acids c. Amino acids are joined together by peptide bonds to form a dipeptide or a ...
Section 1 Workbook
Section 1 Workbook

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organic compounds
organic compounds

... C) Proteins: Complex compounds that carry out all the body’s activities. 1. Building blocks = amino acids 2. Have many different functions which are determined by the protein shape. 3. Lock and Key Model: Proteins must have the right shape to “fit” with other molecules. ...
Enzyme -3. Factors affecting enzyme activity Lecture NO: 1st MBBS
Enzyme -3. Factors affecting enzyme activity Lecture NO: 1st MBBS

... • It is an interaction B/W a molecule and enzyme that blocks the catalytic action of the enzyme in a normal way • Enzyme inhibition interferes with catalysis and slows down or stops the enzymatic reaction ...
enzyme structure
enzyme structure

... for the monomer of 4-oxalocrotonate tautomerase, to over 2,500 residues in the animal fatty acid synthase. A small number of RNA-based biological catalysts exist, with the most common being the ribosome; these are referred to as either RNA-enzymes or ribozymes. The activities of enzymes are determin ...
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Biochem Fall 2011 Sample Exam I – Protein Structure

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Chapter 3 Review Questions

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Introduction to Studying Proteins
Introduction to Studying Proteins

... This project is funded by a grant awarded under the President’s Community Based Job Training Grant as implemented by the U.S. Department of Labor’s Employment and Training Administration (CB-15-162-06-60). NCC is an equal opportunity employer and does not discriminate on the following basis: agains ...
Regulation of enzyme activity
Regulation of enzyme activity

... • Repressors are low molecular weight substances that decrease the rate of enzyme synthesis at the level of gene expression. • Repressors are usually end products of biosynthetic reaction, so repression is sometimes called feedback regulation. • For example, dietary cholesterol decreases the rate of ...
BC 367 Biochemistry of the Cell I
BC 367 Biochemistry of the Cell I

... Compartmentalization allows control, particularly of opposing pathways. Pathways are controlled at a few key steps, usually the irreversible ones. ...
Name: Cell Biology Unit Test #1
Name: Cell Biology Unit Test #1

... 26) True/ False: If one chemical reaction with a ∆G’o = - 10 occurs in the cytosol and another reaction with a ∆G’o of +3.3 occurs inside a mitochondria, the two ∆G’o values can be added and the net ∆G’o will be negative. a) True b) False 27) True/False: The Michealis-Menten constant (Km) of an enzy ...
enzymes lecture 1
enzymes lecture 1

... • It decreases the energy needed for activation (activation energy). • It decreases the energy barrier between reactants and end products. ...
Good Luck and Happy Studying!! Intro to Biochemistry
Good Luck and Happy Studying!! Intro to Biochemistry

... ___________________________________ - major sugar in milk = glucose + galactose ...
Lysosomes
Lysosomes

... subunits a small subunit and a large subunit that bind together and work as one to translate the mRNA into a polypeptide chain during protein synthesis . There are different type of ribosome;70s ribosome, 55s ribosome and 80s ribosome. ...
Unit Test: Metabolism
Unit Test: Metabolism

... 17. Alanine can enter Cellular Respiration as which of the following? 18. In terms of direct ATP production, what is the advantage of a cell having mitochondria? 19. In terms of the spectrum of white light, which of the following is the least effective for photosynthesis? 20. What is the function of ...
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Enzyme



Enzymes /ˈɛnzaɪmz/ are macromolecular biological catalysts. Enzymes accelerate, or catalyze, chemical reactions. The molecules at the beginning of the process are called substrates and the enzyme converts these into different molecules, called products. Almost all metabolic processes in the cell need enzymes in order to occur at rates fast enough to sustain life. The set of enzymes made in a cell determines which metabolic pathways occur in that cell. The study of enzymes is called enzymology.Enzymes are known to catalyze more than 5,000 biochemical reaction types. Most enzymes are proteins, although a few are catalytic RNA molecules. Enzymes' specificity comes from their unique three-dimensional structures.Like all catalysts, enzymes increase the rate of a reaction by lowering its activation energy. Some enzymes can make their conversion of substrate to product occur many millions of times faster. An extreme example is orotidine 5'-phosphate decarboxylase, which allows a reaction that would otherwise take millions of years to occur in milliseconds. Chemically, enzymes are like any catalyst and are not consumed in chemical reactions, nor do they alter the equilibrium of a reaction. Enzymes differ from most other catalysts by being much more specific. Enzyme activity can be affected by other molecules: inhibitors are molecules that decrease enzyme activity, and activators are molecules that increase activity. Many drugs and poisons are enzyme inhibitors. An enzyme's activity decreases markedly outside its optimal temperature and pH.Some enzymes are used commercially, for example, in the synthesis of antibiotics. Some household products use enzymes to speed up chemical reactions: enzymes in biological washing powders break down protein, starch or fat stains on clothes, and enzymes in meat tenderizer break down proteins into smaller molecules, making the meat easier to chew.
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