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Examination questions
Examination questions

... The test consists of 25 questions and is solved on computers in the computer room of Department of Biochemistry (time limit 45 min) (specific personal number /UCO/ and key-word for IS MUNI is necessary for entrance to the test): An essential knowledge ranging over all studied topics is required. Abo ...
BIOCHEMISTRY I Spring 2013 (General medicine, Dental
BIOCHEMISTRY I Spring 2013 (General medicine, Dental

... The test consists of 25 questions and is solved on computers in the computer room of Department of Biochemistry (time limit 45 min) (specific personal number /UCO/ and key-word for IS MUNI is necessary for entrance to the test): An essential knowledge ranging over all studied topics is required. Abo ...
CH 1-4 SAMPLE Questions Membrane
CH 1-4 SAMPLE Questions Membrane

... CH 1-4 SAMPLE Questions ...
Name_________________________________________
Name_________________________________________

SECTION 2 - CELL FUNCTION AND BIOCHEMICAL MEASUREMENT
SECTION 2 - CELL FUNCTION AND BIOCHEMICAL MEASUREMENT

... 11. Plasma proteins contribute to the colloid osmotic pressure of the blood, which is needed for fluid balance. Plasma proteins also serve as circulating enzymes, hormones, transport molecules, and antibodies. Although the liver is a major source of plasma proteins, these molecules can originate fro ...
Unit 05 - Lessons 1-4
Unit 05 - Lessons 1-4

... IV.  Proteins are polymers of amino acid monomers. A.  Twenty different amino acids are used to build proteins in organisms. B.  Amino acids differ in side groups, or R groups. C.  Amino acids are linked by peptide bonds. ...
投影片 1
投影片 1

... molar elliplicity are historical (deg cm2/dmol) the sample concentration (g/L), cell pathlength (cm), and the molecular weight (g/mol) must be known % alpha-helix = (-[θ]222nm +3000)/39000 Biochemistry. 39, 11657-11666, 2000 Secondary Structure Prediction needs spectra down to at least 200nm (some n ...
03-131 Genes Drugs and DiseasesProblem Set 7Due Nov 3, 2013 1
03-131 Genes Drugs and DiseasesProblem Set 7Due Nov 3, 2013 1

... 5. (5 pts) An electron density map can be viewed on the Jmol page for this problem set. The buttons on this page will trace the main-chain through this electron density as well as give you some choices regarding the sidechain of the residue. Determine the amino acid sequence that best fits the exper ...
Experimentally testing the hypothesis of a limited amino acid
Experimentally testing the hypothesis of a limited amino acid

... the present time, any change would be lethal, or at least very strongly selected against; and ii) The shape of the genetic code table was entirely a matter of chance. Theories that rationalize the evolution of the genetic code have been also proposed: e.g. Stereochemical interaction [2], Co-evolutio ...
Study Guide
Study Guide

Amino acids: fed or fasted?
Amino acids: fed or fasted?

MULTIPLE CHOICE. Choose the one alternative that best completes
MULTIPLE CHOICE. Choose the one alternative that best completes

... B) Hydrogen bonds are important forces for holding large molecules together. C) Hydrogen bonds are responsible for many of the unique properties of water. D) Hydrogen bonds are strong attractive forces between hydrogen atoms and negatively charged atoms. E) Hydrogen bonds can form between neighborin ...
CELLular biology
CELLular biology

... vector molecules and carried back into cells. Once in cells, they are transcribed and translated into proteins. The 1st genetic engineering took place in 1973 when Stanley Cohen (Stanford University), Herb Boyer (University of California) and Paul Berg (Stanford University) excised a segment of amph ...
Document
Document

... Specific binding conditions ...
Lecture 3: Introduction to Proteins
Lecture 3: Introduction to Proteins

... Explain the 4 levels of protein structure: primary, secondary, tertiary, and quaternary. Draw the structure of a typical amino acid, indicating the following features: α-carbon, α-carboxyl group, α-amino group, side chain (“R group”), and ionic forms that predominate at acidic (say, pH 1), neutral ( ...
Moving Proteins into Membranes and Organelles Moving Proteins
Moving Proteins into Membranes and Organelles Moving Proteins

... nascent secretory proteins to the ER After synthesis of secretory protein (from N to C) → signal sequence → ER → modification (glycosylation…….)→ vesicle transport to ………. A 16- to 30-residue ER signal sequence (in N-terminal): one or more positively charged adjacent to the core a continuous stretch ...
THE EFFECT OF VARIOUS ACIDS ON THE DIGESTION OF
THE EFFECT OF VARIOUS ACIDS ON THE DIGESTION OF

... rate of liberation of carmine from carmine fibrin. As has been pointed out by various authors, there is considerable doubt as to whether any of these methods actually follows the chemical changes in the structure of the protein during hydrolysis. The recent improvements in the technique of the deter ...
solving protein structures without crystals Cryo-EM gets atom
solving protein structures without crystals Cryo-EM gets atom

... There is a beautiful recent example that is not yet impacting Jane Public, but will have a major impact in due course, and right now is fueling a veritable revolution in protein structure determination. The ability to solve macromolecular structures has been key to understanding fundamental aspects ...
"Hydrophobic Interactions in Proteins". In: Encyclopedia of Life
"Hydrophobic Interactions in Proteins". In: Encyclopedia of Life

... with a smaller one. Table 3 summarizes the results of a series of experiments of this type. If we consider, for example, the leucine-to-alanine substitutions included in the table, the average loss in stability is 14.6 + 4.6 kJ mol 2 1. As can be seen, however, there is a very large spread in the in ...
A European Infrastructure of Ligand Binding
A European Infrastructure of Ligand Binding

... together  with  tools  for  their  use  and  applications  in  studying  proteome  function  and  organisation.  This  4‐year  FP6  Research  Infrastructures  Coordination  Action,  started in March 2006, is funded with 1.8 M€ and links EU and USA partners (see  overleaf),  leaders  in  the  area  o ...
Biomolecules
Biomolecules

... The characteristic pH at which the net electric charge is zero is called the Isoelectric point or “pI”. The amino acid at the isoelectric pI is called “ Zwitter Ion “ and is electrically neutral not migrating in an electric field “Zwitter in German means hybrid or hermaphrodite”. ...
Biological Polymers - McQuarrie General Chemistry
Biological Polymers - McQuarrie General Chemistry

... essential to life. Hemoglobin (Frontispiece), which transports oxygen in the blood and hydrogen carbonate ions from cells, is a protein. Other globular (or roughly spherical) proteins act as catalysts (enzymes) in living organisms. The fibrous protein collagen provides the high tensile strength of s ...
Why should we take care of our bodies?
Why should we take care of our bodies?

... Therefore, they are an immediate source of energy. Think of them like a bunch of M&Ms spilled on a table. They are all loose and can be eaten immediately. That’s how monosaccarides are like, they are an immediate source of ...
Prediction - Center for Biological Sequence Analysis
Prediction - Center for Biological Sequence Analysis

... • Calculate numbers of neighbours for each example, and remove the example with most neighbours • Repeat until there are no examples with neighbours left Alternative: Homology partitioning • keep all examples, but cluster them so that no neighbours end up in the same fold • Should be combined with w ...
The HicAB cassette, a putative novel, RNA-targeting toxin
The HicAB cassette, a putative novel, RNA-targeting toxin

... twice as many (450 sequences) HicB proteins than HicA family proteins, with the largest number, again, found in C.watsonii (33, Supplementary material). In part, this is due to the poor detection of the small hicA genes during genome sequence annotation. In several cases, we identified a hicA-like ...
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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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