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Michal Sharon received her BSc in Chemistry from the Hebrew
Michal Sharon received her BSc in Chemistry from the Hebrew

... Ph.D. studies at the Weizmann Institute of Science focused on studying the three-dimensional structure of proteins by NMR. She conducted postdoctoral research in the Department of Chemistry at the University of Cambridge, UK in the lab of Prof. Carol Robinson until 2007, when she joined the faculty ...
2. CYCLIC AMINOACIDS 2.1. Aromatic
2. CYCLIC AMINOACIDS 2.1. Aromatic

... Play important roles in all biological processes Elementary composition: C 51-55%, O 21-23%, N 15-18%, H 6-7%, S 0.3-2.5% Structure - they are – high-molecular (the mass of single-chain protein is 10-50 kilodaltons (350 dal-1000 kdal); multichain protein complexes >200 kdal. – N containing organic c ...
Montse Fabrega`s presentation
Montse Fabrega`s presentation

... From the gene to the protein Cloning the gene Expression vector: Plasmid or virus designed for protein expression in cells. The vector is used to introduce a specific gene into a target cell and take advantage of the cell’s mechanism for protein synthesis to produce the protein encoded by the gene. ...
Chapter 2 Lecture Notes
Chapter 2 Lecture Notes

Slides
Slides

... Single Motif Protein function prediction using a single motif ...
Powerpoint - Castle High School
Powerpoint - Castle High School

... The enzyme cystathionine b-synthase (CBS) catalyzes the condenation of serine and homocysteine to produce cystathionine, an important intermediate in the biosynthesis of cysteine. Deficiency of CBS activity results in toxic levels of homocysteine and is the most common cause of homocystinuria, a di ...
Defense - Gerstein Lab
Defense - Gerstein Lab

... most sequences fall into 5 ribotypes However, there were very few identical sequences, suggesting that no two cells have identical genome sequences Eugene V Koonin Nat Biotechnology, 2007 ...
Amino Acids - Abbott Nutrition
Amino Acids - Abbott Nutrition

... • Beta-pleated sheet (multiple connected rows form flat structure) ...
Tutorial Kit (Biochemistry-300 L)
Tutorial Kit (Biochemistry-300 L)

... 5. Discuss the role of amino acids in protein structure determination and function Protein structure is generated by 4 levels of structure – primary, secondary, tertiary and quartenary. The four levels are generated by interactions between constituent amino acids Primary structure is the linear seq ...
Apoptosis of Lung Epithelial Cells in Response to Meconium and
Apoptosis of Lung Epithelial Cells in Response to Meconium and

... resuspended in ice-cold buffer (20 mM HEPES, pH 7.0, 50 mM NaCl and 1 mM EDTA), and centrifuged at 21,000g (4oC ) for 15 minutes. Proteins were isolated from cell extract using acetone precipitation and then purified to homogeneity on a Sephadex G100 column (2cm x 50cm), equilibrated with 0.05M sodi ...
Nerve activates contraction
Nerve activates contraction

... pathway but may not even enter the cell. • Its information is passed on. • At each step the signal is transduced into a different form, often by a conformational change in a protein. Copyright © 2002 Pearson Education, Inc., publishing as Benjamin Cummings ...
Gene
Gene

... Genetic sleuths, Beadle and Tatum helped develop the theory that one-gene codes for one polypeptide. These two scientists were also one of the first scientists to demonstrate that changes or mutations in the sequence of nucleotides can change the shape of the resulting protein, which often changes t ...
Transcription and Translation
Transcription and Translation

... (gene) that it wants to transcribe. It attaches to the promoter region, causing DNA to unzip with the help of a Helicase. Polymerase and Helicase are enzymes (special proteins!) ...
Carbon and Biological Molecules Functional Groups Functional
Carbon and Biological Molecules Functional Groups Functional

... • Proteins are polymers of amino acids • Consist of a central carbon + amine group + carboxyl group + R group (= side chain) • Amino acids are joined by peptide bonds • Many functions: structural, enzyme, hormone, transport, contractile ...
Membrane Structure and Function
Membrane Structure and Function

... Polar heads face outward and inward Non-polar tails mingle within the membrane Cholesterol in animal membranes keeps them flexible ...
Instructions for Biochemistry
Instructions for Biochemistry

... these bases in each of our cells. DNA is a helix of two strands: Bases interact between the strands and hold them together. G bonds with C, and A bonds with T. ...
Chapter 26:Biomolecules: Amino Acids, Peptides, and Proteins
Chapter 26:Biomolecules: Amino Acids, Peptides, and Proteins

... • An enzyme is a protein that acts as a catalyst for a biological reaction. • Most enzymes are specific for substrates while enzymes involved in digestion such as papain ...
Extended information on Western blot quantification To Gassen et al
Extended information on Western blot quantification To Gassen et al

... time as the protein of interest (different size, ECL) and used for normalization. Only one Actin example is provided in the figures. Some figures show blots where sequential detection has been applied. Figure S2 provides an example of the different procedures. In panel A, Atg12 and pAktS473 are in s ...
Bioseparation Engineering, Vol 16. Progress in Biotechnology Brochure
Bioseparation Engineering, Vol 16. Progress in Biotechnology Brochure

... bioseparation (X.-L. Feng, Y.-T. Jin, Z. -G. Su). Bioseparation of natural products (C. Keim, M.R. Ladisch). Online recovery of large molecules from mixture solution using semi-continuous size exclusion chromatography (Y.-M. Kim, W. -J. Chang, Y. -M. Koo). Dye adsorption by activated carbon in centr ...
The use of isotope-coded affinity tags (ICAT)
The use of isotope-coded affinity tags (ICAT)

... gel electrophoresis (DIGE) [15,16], ICAT (isotope-coded affinity tagging) [17] and SILAC (stable isotope-labelling with amino acids in cell culture) [18]. Of these, difference gel electrophoresis is a 2D-PAGE-based technique and thus is not suitable for the quantitative comparison of membrane protei ...
PROTEIN TURNOVER AND NITROGEN ECONOMY - U
PROTEIN TURNOVER AND NITROGEN ECONOMY - U

... - caused by deficiencies of urea cycle enzymes - severity depends on proximity of defect to point of entry of ammonia in its processing to urea - CPS-1 defects or ornithine transcarbamoylase defects  severe hyperammonemia; these two defects can be distinguished by evaluating appearance of pyrimidin ...
Vibration Characteristics of Misfolded Proteins and Their
Vibration Characteristics of Misfolded Proteins and Their

... since last 200 years of biochemical studies. Biochemical studies i.e. biochemistry deals with chemical processes in living organisms. It reveals from different experimental facts that most of the chemical reaction is pertaining to cells and their structural components are mediated by Proteins. In ot ...
Protein Structure Prediction and Structural Genomics
Protein Structure Prediction and Structural Genomics

... from focusing on only novel folds to selecting all proteins in a model genome. A modelcentric view requires that targets be selected such that most of the remaining sequences can be modeled with useful accuracy by comparative modeling. Even with structural genomics, the structure of most of the prot ...
6 II. PRIMARY STRUCTURE OF PROTEINS A. Peptide bond
6 II. PRIMARY STRUCTURE OF PROTEINS A. Peptide bond

... • Several different polypeptide helices are found in nature, but the α-helix is the most common. • It is a spiral structure, consisting of a tightly packed, coiled polypeptide backbone core, with the side chains of the component amino acids extending outward from the central axis to avoid interferin ...
HMG B domain
HMG B domain

... The HMGA proteins are among the most highly phosphorylated proteins in the mammalian nucleus. Cell cycle-dependent phosphorylation pga cdc2 activity in the G2/M phase of the cycle.  Sites: T52 and T77 situated at the N-terminal ends of the 2. and 3. AT-hook. Phosphorylation significantly reduces (> ...
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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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