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MTC15 - toddgreen
MTC15 - toddgreen

NucPred—Predicting nuclear localization of
NucPred—Predicting nuclear localization of

... Experimental determination of subcellular locations is often expensive and time-consuming. Instead, computational methods can make fast and accurate predictions. In recent years, several bioinformatics tools have been developed to identify different kinds of subcellular compartment(s) (Emanuelsson e ...
Lecture 5: The Chemistry of Life III
Lecture 5: The Chemistry of Life III

... • Steroids are lipids characterized by a carbon skeleton consisting of four fused rings • Cholesterol, an important steroid, is a component in animal cell membranes • Although cholesterol is essential in animals, high levels in the blood may contribute to cardiovascular disease ...
SURFIN` THROUGH STAAR
SURFIN` THROUGH STAAR

... group, is formed. c. Energy is released, which can be used by the cell. d. Energy is lost in the ...
8  Hershey and Chase Experiment
8 Hershey and Chase Experiment

... They used bacteriophages (viruses that invade bacteria) to discover the solution ...
Amino Acid Analysis - Donald Danforth Plant Science Center
Amino Acid Analysis - Donald Danforth Plant Science Center

... Amino acids are the basic constituents of proteins. Qualitative and quantitative analysis of the amino acid composition of hydrolyzed samples of pure proteins or peptides is used to identify the material and to directly measure its concentration. Amino acids are also intermediates in metabolic pathw ...
Lecture 16 Outline
Lecture 16 Outline

... Functions in Maintenance of Cell Shape (tension bearing elements)changes in Cell Shape, Muscle Contraction, Cell Motility (Pseudopodia), Cell Division (Cleavage Furrow Formation) Actin Filaments have polarity, bind ATP, hydrolysis reduces affinity of monomers for each other- reducing polymer stabili ...
LB145-lecture4
LB145-lecture4

... a. a plasma membrane composed of phospholipids and proteins b. chromosomes that contain genetic information c. ribosomes to synthesize proteins d. mitochondria to generate ATP ...
Edman degradation
Edman degradation

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The Four Groups of Biologically Important Compounds

... lactose=glucose+ galactose • polysaccharides - can be single long chains, repeating branched chains of m.s. ...
Mass spectrometry - Justin Benesch
Mass spectrometry - Justin Benesch

... • Many different instrument geometries to achieve this: e.g. Q-ToF, ToF-ToF ...
NATIONAL UNIVERSITY OF SINGAPORE DEPARTMENT OF BIOCHEMISTRY ADVANCED PLACEMENT TEST (SAMPLE)
NATIONAL UNIVERSITY OF SINGAPORE DEPARTMENT OF BIOCHEMISTRY ADVANCED PLACEMENT TEST (SAMPLE)

... 2. A researcher was studying the kinetic properties of β-galactosidase using an assay in which οnitrophenol-β-galactoside (ONPG), a colorless substrate, is converted to galactose and onitrophenolate, a brightly-colored, yellow compound. Upon addition of 0.25 mM substrate to a fixed amount of enzyme, ...
Protein Motif Analysis
Protein Motif Analysis

... Proteins are like machines in that different parts of the protein perform different sub-functions, and together these parts allow the entire protein to perform its overall function. These functionally distinct parts of the protein are known as functional domains. If they are conserved across taxa, t ...
Bridges
Bridges

... Results ...
Ch4Carbonand5Macromolecules
Ch4Carbonand5Macromolecules

... • Amino acids are linked together by condensation to form polypeptides. • There are 20 different amino acids in polypeptides synthesized on ribosomes. • Amino acids can be linked together in any sequence giving a huge range of possible polypeptides. • The amino acid sequence of polypeptides is coded ...
ch-3-bio-molecules
ch-3-bio-molecules

... they are essential for life ...
List of protein families currently covered by SVMProt
List of protein families currently covered by SVMProt

... Appendix S2 Method for computing the feature vector of a protein sequence A protein sequence is represented by specific feature vector assembled from encoded representations of tabulated residue properties including amino acid composition, hydrophobicity, normalized Van der Waals volume, polarity, p ...
Amino Acids - Shelton State
Amino Acids - Shelton State

... and proteins. The carboxyl group of one amino acid links to the amino group of another amino acid to form a neutral amide. This link is called a peptide bond. These peptides have two different ends. The amino end (N-terminus) is normal ly written on the left with the carboxyl end (C-terminus) on the ...
Life Sciences 1a Practice Problems 6
Life Sciences 1a Practice Problems 6

... b) It would be much longer than it actually is. 8275 amino acids (1 remaining nucleotide). c) 2664 nucleotides not including the stop codon. If they include the stop codon (2667) it is fine. It is also okay if they add three for the start codon (2670) and say this methionine is sometimes cleaved off ...
Outline - Membranes 1. Fluid Mosaic Model of Membrane Structure
Outline - Membranes 1. Fluid Mosaic Model of Membrane Structure

... Moving Molecules into or out of Cells - Overview of Types of Transport I. Passive Transport 1. Always “down” a concentration gradient 2. Always involves proteins called A. Channels B. Carriers ...
Insight into structural and bio
Insight into structural and bio

... AaRSs are enzymes that aminoacylate tRNAs with their cognate amino acids. These proteins play a crucial role in keeping the fidelity of the protein biosynthesis. In eukaryotes, protein synthesis occurs not only in the cytoplasm, but also in different organelles, such as mitochondria and chloroplasts ...
source file
source file

... the membrane, outside the cell, or in the cytoplasm Ex: If probability >0.75, then result is significant. The maximum probability is 1, so the probability that amino acids #1-#20 are “inside” is 100% ...
Electrophoretic Analysis of Native Proteins
Electrophoretic Analysis of Native Proteins

... a protein tend to cluster on the inside of the protein in order to avoid contact with the aqueous environment. Hydrophilic amino acids such as glutamic acid and lysine are readily soluble in water, and thus these amino acids arrange themselves on the surface of the protein molecule, where they can i ...
Practice Exam - mvhs
Practice Exam - mvhs

... 1. Water is one of the most abundant molecules in living organisms. It has several chemical properties that make it ideal for living organisms. a) Explain, at a molecular level, how water is a polar molecule. Include the following terms in your explanation: electronegativity, hydrogen, oxygen, elect ...
Where in the cell is your protein most likely found?
Where in the cell is your protein most likely found?

... Where Are Proteins Located? • All proteins are synthesized in the cytoplasm. • Proteins with export signals can be directed to other cellular locations: – cytoplasm, cytoplasmic membrane, outer membrane or periplasm of Gram (-) bacteria, cell wall, or as secreted products in extracellular space ...
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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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