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The Nutritional Value of Milk Proteins
The Nutritional Value of Milk Proteins

... Milk is an excellent source of high quality protein. The proteins in milk have balanced amino acid profiles and good digestibility. In addition, they contain high levels of the amino acids which are deficient in vegetable proteins. Because of this, milk proteins are excellent “complementary” protein ...
Polymers and Amino Acids
Polymers and Amino Acids

... Examples of globular proteins include enzymes and some hormones. 11 of 13 ...
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... proteins can assist proper protein folding as a protein matures, but once protein aggregates form generally they cannot be renatured to their individual, correct structure. Disulfide bond forming (DBF) enzyme is a chaperone protein related to the class of Sso7d proteins from the hyperthermophilic ba ...
Amino acids, peptides and proteins
Amino acids, peptides and proteins

... Twenty different residues are involved in protein synthesis. These residues might be modified after the synthesis of the polypeptide chain. The other components of proteins are called prosthetic groups. The structure of the amino acids and their characteristic property as amphoteric molecules is des ...
Bio1A Unit 1-3 The Cell Notes File
Bio1A Unit 1-3 The Cell Notes File

... pH 4-5 (required for enzyme function) Lysosomal enzymes can hydrolyze proteins, fats, polysaccharides, and nucleic acids ...
Building Materials of Life
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... Compounds may be organic or inorganic. Water is the most abundant inorganic compound in living things. Carbon dioxide is an inorganic compound that supplies carbon for living things. (CO is also inorganic) ...
Ch. 5 Pppt
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... of organic compounds and hydrolysis in the digestion of organic compounds. How to recognize the 4 biologically important organic compounds (carbs, lipids, proteins, nucleic acids) by their structural formulas. The cellular functions of all four organic compounds. The 4 structural levels of proteins ...
lab.2 Precipitation of Proteins at isoelectric Point
lab.2 Precipitation of Proteins at isoelectric Point

... • Are substance of high molecular weight from 5000 to1000,000 daltons. • All protein Contain C, H, O, N, and most contain sulfur, some contain phosphorus and a few have mineral elements such as Fe, Mg and Cu. • Serve as structural components of animals ...
Proteins…
Proteins…

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Protein Synthesis
Protein Synthesis

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proteins
proteins

... • Even a slight change in primary structure can affect a protein’s conformation and ability to function. • In individuals with sickle cell disease, abnormal hemoglobins, oxygen-carrying proteins, develop because of a single amino acid substitution. • These abnormal hemoglobins crystallize, deformin ...
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Biochemistry - mrmitchellbiowiki

Anatomy I - Unit 3: Basic Biochemistry
Anatomy I - Unit 3: Basic Biochemistry

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... •Proteins are synthesized on ribosomes as linear chains of amino acids. •In order to be biologically active, they must fold into a unique threedimensional structure. •The tunnel that leads from the peptidyl transferase site to the exterior of the ribosome is ~100A long, enough to shelter 30 residues ...
Anatomy I - Unit 3: Basic Biochemistry
Anatomy I - Unit 3: Basic Biochemistry

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Molecules of Life Review Topics
Molecules of Life Review Topics

...  functions: structure, transport, defense, movement, messengers, catalysts  monomer – amino acid: carbon, amino, carboxyl, H and variable (R group)  R group – how many – 20; important – cross links hold 3-D shape of protein  Peptide bond- covalent, between amino acids  Dipeptide, polypeptide – ...
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... The motor: how does it change direction? The direction of the rotation results in the direction of the cell (North, south…) and this is related to CheY-P which are chemotactic proteins and binds FliM. ...
THE CELL MEMBRANE - Mrs. Guida's AP Biology Class
THE CELL MEMBRANE - Mrs. Guida's AP Biology Class

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Name: Cell Biology Test #1: 50 points

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Chapter 4
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... • Simple – composed only of amino acid residues • Conjugated – contain prosthetic groups (metal ions, co-factors, lipids, carbohydrates) Example: Hemoglobin – Heme ...
Proteins perform most functions in the cell [1].
Proteins perform most functions in the cell [1].

... 5. If a chain of amino acids is actually a polypeptide and not a protein as was first mentioned in this section. Explain the relationship between amino acids, polypeptides, and proteins. [1] ...
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Protein in meats and how it helps your body
Protein in meats and how it helps your body

... Meats • Protein is an important sours for our body but you can get protein in several foods and shacks steak, squirrel, eggs and other meats. All foods contain some protein but many foods like those of plant origin lack certain amino acids but that’s why ...
Biomolecules
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Classification of Amino Acids
Classification of Amino Acids

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< 1 ... 613 614 615 616 617 618 619 620 621 ... 656 >

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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