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AIM: What are Macromolecules?
AIM: What are Macromolecules?

... 3 main chemical elements: carbon, oxygen, and hydrogen (plus lots of other elements) • An organic molecule is any molecule containing Carbon (C) and Hydrogen (H) elements combined with any other chemical elements. Examples : Glucose (C6H12O6 ) is organic, H2O is not organic , CO2 (carbon dioxide) is ...
No Slide Title
No Slide Title

... - Plane support (filter) is derivatised by a spacer (for on support screening) - Subsequently, covalent attachment of a linker unit (attachment of growing molecules and for further cleavage) ...
pro amino crème
pro amino crème

... pro amino crème has the ability to boost the skin’s natural moisture levels, restoring free water levels and natural lipids to enhance barrier function and maintain a balanced, youthful complexion. pro amino is a crème that is formulated with the eight essential amino acids, proteins and vitamin C; ...
Which DNA sequence is most likely to form a hairpin structure? x
Which DNA sequence is most likely to form a hairpin structure? x

... A. RNA can base pair with another RNA molecule. B. RNA can base pair with a DNA molecule. C. RNA is commonly found in a double helix structure. D. RNA molecules can form a wide variety of three-dimensional structures. E. RNA contains the nucleotides adenylate, guanylate, cytidylate, and uridylate. C ...
NNI086 - Nestlé Nutrition Institute
NNI086 - Nestlé Nutrition Institute

... Proteins are the main building blocks of the body. They are polymers composed of 30 or more amino acids. Twenty different standard amino acids combine to form the proteins. Some amino acids are essential dietary components, since they are not synthetized by human metabolic processes. Proteins are pr ...
Chapter 2
Chapter 2

... • Isotopes are atoms of an element that have the same number of protons, but a different number of neutrons • Why do we care as biologists? They make very good identification markers for certain biological molecules like proteins and DNA ...
ADAM
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... Function of disintegrin domain ...
6. Protein Hydrolysis and Denaturation
6. Protein Hydrolysis and Denaturation

...  occurs in the digestion of proteins  occurs in cells when amino acids are needed to synthesize new proteins and repair tissues ...
rev4 - Adams State University
rev4 - Adams State University

... are attached via disulfide bonds. Giving hair a perm involves these bonds. 13. Collagen, the most abundant protein in vertebrate animals, has a unique collagen helix due to a preponderance of proline and hydroxyproline in the structure. 3 collagen helixes coil around one another and held together by ...
ppt - UCLA Chemistry and Biochemistry
ppt - UCLA Chemistry and Biochemistry

... insert into/span the membrane bilayer; or covalently linked to membrane lipids. (Interact with the hydrophobic part of the membrane) 2. Peripheral proteins: interact with integral protein through noncovalent interaction; or interact with polar head groups of the membrane lipids. (charge interaction ...
Enzymes are specific? - The BioUpdate Foundation
Enzymes are specific? - The BioUpdate Foundation

... chloramphenicol acetyltransferase (CAT), a bacterial enzyme which detoxifies chloramphenicol and known since the 1960s. This enzyme was present in the organism before chloramphenicol was used as an antibiotic and no-one suggests that the natural function of this enzyme is to detoxify antibiotics. It ...
Sports Nutrition Advertisement Assignment
Sports Nutrition Advertisement Assignment

... 10lbs (210 Servings) 90% PROTEIN-Pure WPI is nature's purest and most effective protein Undenatured Whey Protein , High in BCAAs for lean muscle growth. Supports the body's immune system. High levels of essential amino acids. No Ace K or aspartame. Natural appetite suppressant. Pure WPI is nature's ...
Functional genomics: assigning functions to genome sequences
Functional genomics: assigning functions to genome sequences

... Functional Linkages Among Cytochrome Oxidase Genes ...
essential nutrition - Ortho Molecular Products
essential nutrition - Ortho Molecular Products

... Solathin™ brand potato protein is a chosen ingredient in LifeCORE Complete because it is a compilation of low molecular weight amino acids, including a potent satiety inducing factor called proteinase inhibitor II (PI2). Proteinase inhibitor II, is a heat –stable protein derived from potatoes that i ...
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... Fats are large molecules made from smaller molecules linked together by dehydration reactions. Neutral fats are made of glycerol and three fatty acids. Glycerol is a 3-carbon alcohol. Fatty acids are long unbranched hydrocarbon chain with a carboxyl group (COOH) at one end. The carbon skeleton of th ...
Preview Sample 1 - Test Bank, Manual Solution, Solution Manual
Preview Sample 1 - Test Bank, Manual Solution, Solution Manual

... If both starch and cellulose contain the monosaccharide glucose, why can't most animals, including humans, digest cellulose? ...
Lecture: Biochemistry
Lecture: Biochemistry

WHAT IS PROTEIN?
WHAT IS PROTEIN?

... the essential amino acids our bodies cannot make and are therefore vital in our diets in small amounts. By contrast, incomplete proteins, which come from mainly plant sources, can be combined to make a complete protein. WHY IS PROTEIN IMPORTANT IN YOUR DIET? Protein makes up the largest percentage o ...
Signal transmission with cell surface and intracellular receptors.
Signal transmission with cell surface and intracellular receptors.

Gene Duplication in the Mo-Fe Protein of Nitrogenase
Gene Duplication in the Mo-Fe Protein of Nitrogenase

... • Constructed a phylogenetic tree of the Mo-Fe protein of nitrogenase from published nucleic acid data. • Tried to get a more coherent tree by eliminating some of the sequences. • Tree still not revealing. • Mistake: using nucleotides, switched to amino acid sequences for the alpha and beta chains. ...
Signal transmission with cell surface and intracellular receptors Prof.Dr.Gönül Kanıgür
Signal transmission with cell surface and intracellular receptors Prof.Dr.Gönül Kanıgür

... • Can exert their specific effects in three ways • By influencing the rate of synthesis of enzymes and other proteins • By effecting the rate of enzymatic catalysis • By altering the permeability of cell ...
Gail`s powerpoint
Gail`s powerpoint

... • All 3 glycosylation Asn replaced with Glu on b-subunit – Proper assembly and trafficking to PM with wild-type a-subunit – Catalytically active, but increased susceptibility to degradation ...
Extracellular Macromolecules
Extracellular Macromolecules

... one kind of post-translational modification others: phosphorylation carboxylation ...
ab initio
ab initio

2401-Ch3.pdf
2401-Ch3.pdf

... It codes for the amino acid methionine, so every proteins starts with this amino acid ...
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Protein



Proteins (/ˈproʊˌtiːnz/ or /ˈproʊti.ɨnz/) are large biomolecules, or macromolecules, consisting of one or more long chains of amino acid residues. Proteins perform a vast array of functions within living organisms, including catalyzing metabolic reactions, DNA replication, responding to stimuli, and transporting molecules from one location to another. Proteins differ from one another primarily in their sequence of amino acids, which is dictated by the nucleotide sequence of their genes, and which usually results in protein folding into a specific three-dimensional structure that determines its activity.A linear chain of amino acid residues is called a polypeptide. A protein contains at least one long polypeptide. Short polypeptides, containing less than about 20-30 residues, are rarely considered to be proteins and are commonly called peptides, or sometimes oligopeptides. The individual amino acid residues are bonded together by peptide bonds and adjacent amino acid residues. The sequence of amino acid residues in a protein is defined by the sequence of a gene, which is encoded in the genetic code. In general, the genetic code specifies 20 standard amino acids; however, in certain organisms the genetic code can include selenocysteine and—in certain archaea—pyrrolysine. Shortly after or even during synthesis, the residues in a protein are often chemically modified by posttranslational modification, which alters the physical and chemical properties, folding, stability, activity, and ultimately, the function of the proteins. Sometimes proteins have non-peptide groups attached, which can be called prosthetic groups or cofactors. Proteins can also work together to achieve a particular function, and they often associate to form stable protein complexes.Once formed, proteins only exist for a certain period of time and are then degraded and recycled by the cell's machinery through the process of protein turnover. A protein's lifespan is measured in terms of its half-life and covers a wide range. They can exist for minutes or years with an average lifespan of 1–2 days in mammalian cells. Abnormal and or misfolded proteins are degraded more rapidly either due to being targeted for destruction or due to being unstable.Like other biological macromolecules such as polysaccharides and nucleic acids, proteins are essential parts of organisms and participate in virtually every process within cells. Many proteins are enzymes that catalyze biochemical reactions and are vital to metabolism. Proteins also have structural or mechanical functions, such as actin and myosin in muscle and the proteins in the cytoskeleton, which form a system of scaffolding that maintains cell shape. Other proteins are important in cell signaling, immune responses, cell adhesion, and the cell cycle. Proteins are also necessary in animals' diets, since animals cannot synthesize all the amino acids they need and must obtain essential amino acids from food. Through the process of digestion, animals break down ingested protein into free amino acids that are then used in metabolism.Proteins may be purified from other cellular components using a variety of techniques such as ultracentrifugation, precipitation, electrophoresis, and chromatography; the advent of genetic engineering has made possible a number of methods to facilitate purification. Methods commonly used to study protein structure and function include immunohistochemistry, site-directed mutagenesis, X-ray crystallography, nuclear magnetic resonance and mass spectrometry.
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