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Supplementary Methods (a) Chemically
Supplementary Methods (a) Chemically

... #1150-1157 (Repl. 2), 1158-1165 (Repl 3). To reduce false positive identifications, proteins ...
Organic Molecule Marshmallow Lab
Organic Molecule Marshmallow Lab

... Gathered Information: Organic molecules all contain carbon. There are four different groups of organic molecules. Each group can be identified by the elements that comprise it and the functional groups that are present within it. The four groups of organic molecules are carbohydrates, lipids, protei ...
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The Origin of Life: What We Do and Don`t Know

... For small amino acids (C≤ 4), biology uses a good sampling of the possible “chemical space”. For larger amino acids, this relationship falls off rapidly. ...
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Addition of the keto functional group to the genetic
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... by oxidizing N-terminal serine or threonine with periodate. The aldehyde group was coupled to biotin and fluorescent reporters (8) or protein fragments containing a COOH-terminal hydrazide through a hydrazone linkage (25). The carbonyl group introduced by this method is restricted to the N terminus, ...
Section 2 - Introduction to Molecular Biology
Section 2 - Introduction to Molecular Biology

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Full Text
Full Text

... it is performed by attached myristic acid in proteins. Myristoylation can affect conformational stability of proteins by interaction with membranes or the hydrophobic domains of other proteins (Podell & Gribskov, 2004; Zheng et al., 1993; Olsen & Kaarsholm, 2000). Also, myristoylation was identified ...
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lausanne_poster2010.v2
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... De novo prediction of protein tertiary structure on the basis of amino acid sequence remains one of the outstanding problems in biophysical chemistry. Protein structure prediction using homology modeling has been one of the most popular technique to construct atomic resolution model of the target pr ...
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Carlson, Scott M.: Sequence Motifs are Necessary but not Sufficient for Predicting Post-translational Modifications
Carlson, Scott M.: Sequence Motifs are Necessary but not Sufficient for Predicting Post-translational Modifications

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Sample Preparation Methods for MS Based Proteomics
Sample Preparation Methods for MS Based Proteomics

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English 
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... III. Proteins make up more that 50% of the dry weight of animals. A. Proteins perform many important functions in living organisms. Have students create a “protein pamphlet” by folding 2 pieces of paper in half. Use this to take notes about the function of proteins in animals. 1. Hair and fingernail ...
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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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