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Biomolecules PPT
Biomolecules PPT

... Photo by Toni Lozano ...
Chapter 6 Crossword Puzzle
Chapter 6 Crossword Puzzle

... increased excretion of the mineral _____. Amino acids can be used to make glucose if insufficient dietary _____ are consumed. What the body uses to assemble its own proteins Proteins that act to defend the body from disease Proteins that provide sufficient quantities of essential amino acids are ref ...
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Slide 1

...  Amino acid chemistries give proteins their primary, secondary, tertiary structure  Structure function relationships  Biological roles of proteins ...
Document
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... exit across the basolateral membrane via facilitated diffusion on the GLUT2 sugar transporter. ...
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... Nucleic Acid • made up of CHONP ...
(Simple) Physical Models of Protein Folding
(Simple) Physical Models of Protein Folding

... •Linear polymer chain composed of tens (peptides) to thousands (proteins) of monome •Monomers are 20 naturally occurring amino acids •Different proteins have different amino acid sequences •Structureless, extended unfolded state •Compact, ‘unique’ native folded state (with secondary and tertiary str ...
File - Somma Science
File - Somma Science

... cells that become fingernails and hair. Antibodies, also called immunoglobins, help recognize and destroy foreign pathogens in the immune system. Actin and myosin allow muscles to contract, while albumin nourishes the early development of an embryo or a seedling. ...
1.intelligentdesign
1.intelligentdesign

... Facts of the case Proteins are indispensible component of cells – therefore the first living cell had to have them. i.e. life could not have begun without proteins Proteins are composed of Amino acids. The amino acids must link in a particular order to form proteins of a particular shape and functi ...
CARBOHYDRATES, lipids and proteins handout
CARBOHYDRATES, lipids and proteins handout

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... Proteins are made of subunits called amino acids and are used to build cells and do much of the work inside organisms. They also act as enzymes helping to control metabolic reactions in organisms. Amino acids contain two functional groups, the carboxyl group (-COOH) and the amino group (-NH2). Color ...
Table of Contents
Table of Contents

Protein Synthesis (Gene Expression) Notes
Protein Synthesis (Gene Expression) Notes

Proteins2[1]
Proteins2[1]

... • Each amino acid in a chain makes two peptide bonds • The amino acids at the two ends of a chain make only one peptide bond • The aa with a free amino group is called amino terminus or N-terminus • The aa with a free carboxylic group is called carboxyl terminus or C-terminus ...
Abstract
Abstract

... Insoluble β-amyloid peptide (Aβ) deposits formed in the synaptic milieu, chronic activation of glial cells and inflammation are consistent features in Alzheimer’s disease (AD) and strong candidates for the initiation of this process. S100B is one of the numerous pro-inflammatory molecules produced b ...
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Protein Metabolism

Chapter 5
Chapter 5

LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034
LOYOLA COLLEGE (AUTONOMOUS), CHENNAI – 600 034

... Discuss the secondary structure of proteins ? Mention the forces responsible for the maintenance of structure of protein ...
Biology I SB1bc Enzymes and Macromolecules Test Study Guide
Biology I SB1bc Enzymes and Macromolecules Test Study Guide

Biology I SB1bc Enzymes and Macromolecules Test Study Guide
Biology I SB1bc Enzymes and Macromolecules Test Study Guide

... “Reusable” proteins that put together or break down substrates to form products 2. Since enzymes are proteins they are made of ……what? Amino acids joined by peptide bonds 3. The energy needed to start a chemical reaction is called? Activation Energy (EA) 4. How do enzymes increase the rate or speed ...
Structures define the functions of proteins
Structures define the functions of proteins

... - Molecular chaperone : bind to exposed hydrophobic regions and stabilize them, thereby preventing these proteins from aggregating and being degraded. (Hsp70+Hsp40, GrpE+DnaK) - Chaperonins directly facilitate the folding of proteins (TriC, GroEL) ...
Nucleic Acids and Protein Synthesis
Nucleic Acids and Protein Synthesis

... Part A is the ________________________. Part B is the ________________________. Part C is the ________________________. ...
MacromoleculeReview
MacromoleculeReview

... 14. How does the structure of an unsaturated fatty acid differ from the structure of a saturated fatty acid? Give an example of a food that contains each. ...
Protein Degradation at Lysosome
Protein Degradation at Lysosome

... • Cells are continually building proteins, using them for a single task, and then discarding them. • Signaling or controlling proteins (eg. transcription regulators and the cyclins) - lead very brief lives, carrying their messages and then being thrown away. • Specialized enzymes - built just when t ...
General Info: Proteins: • Make up 10
General Info: Proteins: • Make up 10

... 2. Secondary structure: All proteins have one of two types of this structure held together with hydrogen bonds between oxygen and hydrogen atoms. • Most commonly- a chain that coils up like a slinky • Others- several lined up side by side and pleated in a sheet. ...
What are some other organic molecules?
What are some other organic molecules?

... other quality of the environment can cause a protein to unravel and lose its normal shape Denatured proteins do not function properly! INCORRECT FORM….. NO FUNCTION! ...
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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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