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Homology between the DNA-binding domain of the GCN4
Homology between the DNA-binding domain of the GCN4

... domains of the protein: DNA binding and transcriptional activation (13). The DNA-binding function depends on the integrity of the carboxyl-terminal segment of 60 amino acids (13). This highly basic region is also the domain showing homology to jun protein. Transcriptional activation by GCN4 requires ...
Outer dense fibre protein 2 (ODF2) is a self
Outer dense fibre protein 2 (ODF2) is a self

... amino acids with a deduced molecular mass of about 70 kDa (Brohmann et al., 1997; Hoyer-Fender et al., 1998; Petersen et al., 1999). In the C-terminal region (at amino acid positions 392-413 and 530-551 of rat ODF2) two leucine zipper motifs are present which are responsible for interaction with the ...
Biochemistry and the Cell - Tanque Verde Unified District
Biochemistry and the Cell - Tanque Verde Unified District

... Protein Structure Proteins are complex molecules with 4 levels of structure (1) Primary structure the order of amino acids in the polymer (2) Secondary structure weak hydrogen bonds bend the chain into a helix or pleated sheet (3) Tertiary structure the 3D shape of the protein (polypeptide) chain ( ...
I Periodic table
I Periodic table

... the addition of one of these groups in the R group? What effects do mutations have on the structure and function of proteins? An amino acid sequence is the primary sequence of a protein. Draw the following amino acids structures and connect them by a peptide bonds by dehydration synthesis to form a ...
Master course KEMM03 Principles of Mass Spectrometric Protein
Master course KEMM03 Principles of Mass Spectrometric Protein

... e. Lysine-terminated peptides f. mgf-file g. 1672.92 Da h. Database ...
lec39_2013 - Andrew.cmu.edu
lec39_2013 - Andrew.cmu.edu

... c) rRNA – ribosomal RNA is found in the ribosome and is responsible for most of the function in protein synthesis. ...
The Proteins of the Keratin Component of Bird`s Beaks
The Proteins of the Keratin Component of Bird`s Beaks

... these proteins show an overall similarity in composition. This is particularly evident in their contents of glycine (about 30 residues %), tyrosine, serine and proline which together account for 55-60 % of the total residues. Their content of half-cystine, determined as S-carboxymethyl cysteine, is ...
The WHy domain mediates the response to
The WHy domain mediates the response to

... query for standalone PSI-Blast (Altschul et al., 1997) against the protein nr-database. After three iterations, which retrieved only homologs of the Hin1 family in several plants, the first protein from the bacterium Ralstonia metallidurans was detected (ZP_00273651, E = 0.0003). This is an uncharac ...
Lecture_1_Dr_Manar_1
Lecture_1_Dr_Manar_1

... 2-Polysaccharides are polymers with few hundred to few thousand monosaccharides joined by peptide bond. ...
Central Dogma of Genetics
Central Dogma of Genetics

... – and allows bacteria to grow in Trp free medium. ...
26.5 Cotobolism of smino ocids
26.5 Cotobolism of smino ocids

A plant has stunted growth and yellowing leaves because it is
A plant has stunted growth and yellowing leaves because it is

... This answer suggests the student understands that this is a dehydration synthesis reaction because a hydrogen atom is removed from one amino acid and a hydroxyl group is removed from the other, and that the hydrogen and hydroxyl group form a water molecule, which is released to the environment. ...
Fluorescence Detection of Tryptophan and Tyrosine Residues for
Fluorescence Detection of Tryptophan and Tyrosine Residues for

... Native fluorescence of tryptophan (Trp) and tyrosine (Tyr) can be a useful additional LC detection mode for peptide mapping of proteins when used in-series with ultraviolet (UV) detection and mass spectrometry. Methods Excitation and emission wavelengths were chosen in order to obtain tyrosine-selec ...
Mapping functional regions of the segment
Mapping functional regions of the segment

... which recognize identical or very closely related GC-rich sequences. So far, three other members have been identified: Krox-24 (also known as Egr-1, Zif268, NGFI-A and TIS8 (8-12)), EGR-3 (13) and NGFI-C (14). Although these proteins are very closely related within their putative DNA-binding domains ...
Mitochondrial Uncoupling Proteins in Mammals and Plants
Mitochondrial Uncoupling Proteins in Mammals and Plants

... Looking for other sequences, specific for mammal and plant uncoupling proteins, we employed the pattern prediction program package MEME-MAST (http:兾兾 www.sdsc.edu兾MEME, Refs. 57, 58). MEME motifs are represented by letter-probability matrices that specify the probability of each possible letter (of ...
Modification and Inactivation of Human Cu,Zn
Modification and Inactivation of Human Cu,Zn

Fatty acid - St John Brebeuf
Fatty acid - St John Brebeuf

... • All living things are made up of four classes of large biological molecules: carbohydrates, lipids, proteins, and nucleic acids • Macromolecules are large molecules composed of thousands of covalently ...
CHAPTER 4: CELLULAR METABOLISM
CHAPTER 4: CELLULAR METABOLISM

... A. Definition: Enzymes are biological, protein catalysts that increase the rate of a chemical (metabolic) reaction without being consumed by the reaction. B. Enzymes are typically globular proteins (review protein structure in chapter 2). C. Enzymes are specific for the substance they act upon (call ...
Simple Models of Protein Folding
Simple Models of Protein Folding

... Otherwise, the value of < ρ > may approach 1, but the value for ρ∗ may approach 1 through one or two steps, corresponding to a first-order folding transition or transition through a folding intermediate respectively. Now, specifically for the ten monomer chain, there are 1024 possible sequences. Of ...


... correct ionization state for a pH of 6.0. If you do not know the structure of the sidechains for these amino acids, draw those that you do know, label them, and give the sequence of your modified peptide. Please do not use Glu, Phe, or Ile, as these are given elsewhere on the exam. Label the followi ...
Protein
Protein

... Binding of insulin to its receptor activates the protein tyrosine kinase activity of the receptor, leading to the phosphorylation of insulin-receptor substrates (IRSs). The phosphorylated IRSs interact with the phosphotidylinositide 3-kinase (PI kinase) at the plasma membrane, where the enzyme catal ...
UTM EatWell  Are Protein Powders Right For You?
UTM EatWell Are Protein Powders Right For You?

... advantage of being relatively convenient (e.g. you don’t have to cook, or even refrigerate them). However, this convenience is a costly one - upwards of $2500 a year! ...
Chapter 4 Outline
Chapter 4 Outline

... 3. The portion of a DNA molecule that contains the genetic information for making one kind of protein is called a gene. 4. All of the DNA in a cell constitutes the genome. a. Over the last decade, researchers have deciphered most of the human genome (see chapter 24, The Human Genome Project). 5. In ...
Enzyme Properties - Illinois Institute of Technology
Enzyme Properties - Illinois Institute of Technology

... Segments with secondary structure are usually short: 2-30 residues Some globular proteins are almost all helical, but even then there are bends between short helices Other proteins: mostly beta Others: regular alternation of ,  Still others: irregular , , “coil” ...
CHAPTER 4: CELLULAR METABOLISM
CHAPTER 4: CELLULAR METABOLISM

... 3. The portion of a DNA molecule that contains the genetic information for making one kind of protein is called a gene. 4. All of the DNA in a cell constitutes the genome. a. Over the last decade, researchers have deciphered most of the human genome (see chapter 24, The Human Genome Project). 5. In ...
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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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