"Protein folding" Essays and Research Papers

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    Proof Is in the Proteins

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    accepted the origin of all life on Earth. In the article‚ “The Proof is in the Proteins: Tests Supports Universal Common Ancestor for All Life”‚ by Katherine Harmon‚ a scientist by the name of Douglas Theobold carried out statistical analysis on 23 preserved proteins that were preserved over three major domains of life. The result of these analyses supported Darwin’s evolutionary theory‚ by demonstrating that the protein sequences of life today came from a common universal ancestor rather than separate

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    diffusion through membrane transporters (carrier protein) by means of active transport OR The type of transporter which an animo acids is transported through the epithelial membrane through depends on the R-group attacked to the particular amino acid (structure and combosition) These transporters bind amino acids only once they have bound sodium ions – this is known as coupled transport This coupled transport is through a symport transporter protein which works by transporting the amino acid across

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    a gigantic pipeline that is spread over the whole cytoplasm and is held together by a cytoplasmic skeleton‚ made up of proteins. There are two types of endoplasmic reticulum. One is smooth and the other is rough endoplasmic reticulum and both of these types are interconvertible. The rough endoplasmic reticulum has ribosomes attached to the surface‚ which are sites for protein synthesis‚ while the smooth endoplasmic reticulum is purely a transport system for the ions and steroids in particular

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    denaturation

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    Denaturation is the alteration of a protein shape through some form of external stress (for example‚ by applying heat‚ acid or alkali)‚ in such a way that it will no longer be able to carry out its cellular function. See also: Plants & Animals Cell Biology Genetics Molecular Biology Matter & Energy Biochemistry Organic Chemistry Thermodynamics Denatured proteins can exhibit a wide range of characteristics‚ from loss of solubility to communal aggregation. Proteins are very long strands of amino

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    Atkins Protein

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    major dietary sources of each. a. Proteins b. Carbohydrates c. Fats . Janine made this statement: “… if your brain doesn’t get carbs—well‚ glucose‚ anyway—you get really cranky. You have to have enough carbs.” Find out if Janine is right. How does the nervous system use glucose? . Janine also said: “If you eat way too much protein and not enough carbs you can ruin your kidneys forever because of all the nitrogen you have to process breaking down the protein.” Find out if Janine is right about

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    wingwangs

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    shape of a polypeptide or protein The way several different polypeptide chains fit together to form the final protein Ala-gly-tyr-lys-met-trp-phe Beta-pleated sheet Results from the bending and folding of a polypeptide chain that occurs due to a variety of interactions b/w the amino acid side chains Only found in proteins composed of more than one polypeptide chain Results from hydrogen bonds b/w polar groups in the polypeptide backbone Repeated pattern of coiling or folding w/in a polypeptide chain

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    Plate tectonics help us to explain the process of folding. According to the theory of plate tectonics‚ the earth’s crust is broken up into sections called plates. These plates float on the semi-molten mantle. Thermal convection currents in the mantle drag these plates in different directions resulting in tectonic activity. Folding occurs when rock layers that were originally horizontal are bent into a series of wave-like folds. As a result of this collision of the earth’s tectonic plates‚ the

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    Enzyme Summary

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    coiling and folding of a protein’s polypeptide backbone. This folding is stabilized by hydrogen bonds between peptide linkages. These sections of polypeptide chains are repeatedly coiled or folded into patterns that add to the protein’s overall conformation. There are two types of secondary structures. They are alpha helixes and beta pleated sheets. Alpha helixes are helical coils stabilized by a hydrogen bond between every fourth peptide bond. They are usually found in fibrous protein such as keratin

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    Protein Shakes

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    Protein shakes 1) Verifiable facts: the 3 common forms of protein shakes are whey‚ soy and casein protein. Protein shakes are useful when: - You’re growing - You’re starting a program - You’re amping up your workouts - You’re recovering from an injury Unverified statements or value claim: This whole part is unverified: So how can you tell if you’re already getting enough protein? Do the math. Recreational athletes need 0.5-0.75 grams of protein daily for every per pound of body weight Competitive

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    molecule. This is easier explained through an example. An example of a polymer‚ is a protein. The monomer used to make up is an amino acid. When two amino acids join together a dipeptide is formed‚ this is then made into a polypeptide chain by the joining of additional amino acids‚ it finally becomes a protein when more than one of these polypeptide chains link to one another in a condensation reaction. Proteins have a variety of functions‚ these functions are determined by their shapes. For example

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