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BiochemLecture07
BiochemLecture07

... • RanGTP enhances binding between an exportin and its cargo but stimulates release of importin's cargo; RanGDT has the opposite effect, namely, it stimulates the release of exportin's cargo, but enhances the binding between an importin and its cargo. Therefore, the exportin and its cargo may move t ...
Protein Modification, targeting and degradation Protein modification
Protein Modification, targeting and degradation Protein modification

... Ran helps move importins and exportins and their cargo in and out of the nucleus • RanGTP enhances binding between an exportin and its cargo but stimulates release of importin's cargo; RanGDT has the opposite effect, namely, it stimulates the release of exportin's cargo, but enhances the binding be ...
Three Dimensional Protein Structures
Three Dimensional Protein Structures

... Conformation: Spatial arrangement of atoms that depend on bonds and bond rotations. Proteins can change conformation, however, most proteins have a stable “native” conformation. The native protein is folded through weak interactions: a) Hydrophobic interactions b) Hydrogen-bonds c) Ionic interaction ...
Solutions to 7.014 Quiz I
Solutions to 7.014 Quiz I

... c) LMGT is composed of four polypeptides (two γ polypeptides and two δ polypeptides). i) How many unique primary protein structures compose the LMGT protein complex? Two ii) What protein secondary structure is part of the LMGT protein complex? α-helix iii) What is the strongest type of bond that mai ...
Carbohydrates, Lipids, and proteins
Carbohydrates, Lipids, and proteins

... Both of the functional groups are covalently bonded to a central atom, called the alpha carbon Also bonded to the alpha carbon is a hydrogen atom and a chemical group symbolized by the letter R.  R group is the variable part of an amino acid.  R group structure determines the specific properties o ...
Biochemistry
Biochemistry

... •Phospholipids – makes coverings (membranes) water resistant Found in cell membranes •Steroids and Hormones – produce body changes such as puberty Found in cholesterol, testosterone, estrogen ...
Stages and mechanisms of translation, regulation of translat
Stages and mechanisms of translation, regulation of translat

... -Ribosomal subunits -mRNA template to be translated -Initiator tRNA molecule -Protein initiation factors ...
Denaturation of proteins
Denaturation of proteins

... tertiary structure and, if applicable, quaternary structure) and how those forces would be affected by the changes in temperature or pH. For example, H bonds, such as in C=O∙∙∙∙H-N, are important in 2°, 3°, and 4° structure. As the temperature of a solution containing the protein is raised, the extr ...
Protein structure
Protein structure

... Quaternary structure Some proteins can interact with each other to form dimers or multimers The individual chains are callled subunits or monomers ...
HLFinalcell
HLFinalcell

UNIT 1 review PPT
UNIT 1 review PPT

... function make sure you know at least 3 functions and be able to give examples of each function…. The next 2 slides summarize these… the following 15 or so slides expand on these functions more. ...
DNA and RNA - Mrs-Lamberts-Biology
DNA and RNA - Mrs-Lamberts-Biology

... Why are proteins important? • All enzymes are proteins. • Every chemical reaction in the body requires an enzyme to make it go. • Enzymes make some reactions go 1 million times faster than they would go without the enzyme. • Proteins regulate the rate of growth of an ...
DNA - California State University, Stanislaus
DNA - California State University, Stanislaus

... lose nucleotides from a gene are called frameshift mutations ...
d) a and b
d) a and b

... 4. Which of the following is not found in a DNA molecule? a) ribose b) sugar e) DNA does not contains any of these ...
Plasma Membrane
Plasma Membrane

... endoplasmic reticulum 4. Drops amino acid chain into the endoplasmic reticulum for folding 5. Packaged into transport vesicles 6. Moves to the Golgi complex for processing, sorting and shipping 7. Proteins bud off and are ...
Modeling Protein synthesis lab
Modeling Protein synthesis lab

... Genes are the units that determine inherited characteristics, such as hair color and blood type. Genes are lengths of DNA molecules that determine the structure of polypeptides (the building blocks of proteins) that our cells make. The sequence of nucleotides in DNA determines the sequence of amino ...
Tobacco Mosaic Virus (TMV)
Tobacco Mosaic Virus (TMV)

... • The coat of proteins, around the RNA strand, protect it from any enzymes trying to kill it. • But, in order for TMV to spread it has to release it’s coat of proteins for the RNA to enter a cell • The proteins, situated outside the cell, repel against each other. This allows the cell to release RNA ...
Macromolecules Worksheet
Macromolecules Worksheet

... ____________________ 1. This measures the hydrogen ion level of a solution. ____________________ 2. What kind of solution contains more hydrogen ions than hydroxide ions? ____________________ 3. This is the name for a compound with many sugar subunits linked together. ____________________ 4. What ar ...
Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC)
Stable Isotope Labeling with Amino Acids in Cell Culture (SILAC)

... amino acid is supplied to cells in culture instead of the natural amino acid, it is incorporated into all newly synthesized proteins. After a number of cell divisions, each instance of this particular amino acid will be replaced by its isotope-labeled analog. Since there is hardly any chemical diffe ...
Leah Cooper
Leah Cooper

... for total nitrogen is the primary determinant of total protein requirement, which includes a need for both EAA and NEAA. There is a dietary nitrogen requirement for the de novo synthesis of the NEAA. It has been suggested that some NEAA might be metabolically very important and may have a dietary re ...
Bio Chap 2 Biomolecules
Bio Chap 2 Biomolecules

... Control rates of reaction - enzymes Transport substances in & out of the cell - hormones, channel proteins ...
Chapter 4 The Three-Dimensional Structure of Proteins
Chapter 4 The Three-Dimensional Structure of Proteins

ENGINEERING PROTEINS
ENGINEERING PROTEINS

Biomolecules - Good Earth School
Biomolecules - Good Earth School

... they are subjected to heat, acid and alkali they undergo coagulation to form fibrous proteins which are insoluble in water. This results in a change of physical and biological properties of protein. The coagulated protein thus obtained is called denatured protein and the process is called denaturati ...
Notes - Organic Molecules of Life
Notes - Organic Molecules of Life

... found in cell parts: nucleoli, ribosomes, and throughout the cytoplasm General Structure: Polymers - repeating units called ____________________________ Nucleotides have three subunits: a five carbon sugar a phosphate group a nitrogenous base (a base that contains nitrogen) ...
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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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