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Chapter 3 The Molecules of Cells
Chapter 3 The Molecules of Cells

... 3.14 DNA and RNA are the two types of nucleic acids  The amino acid sequence of a polypeptide is programmed by a discrete unit of inheritance known as a gene.  Genes consist of DNA(deoxyribonucleic acid), a type of nucleic acid.  DNA is inherited from an organism’s parents.  DNA provides direct ...
Lezione 10 - Dipartimento di Informatica e Automazione
Lezione 10 - Dipartimento di Informatica e Automazione

... Chaperoned by proteins that initiate and terminate the process, and other proteins that inject the energy for each step, ribosomes walk down a strand of mRNA, align tRNA adapters alongside, and link up the amino acids they carry ...
Membrane Structure and Function
Membrane Structure and Function

... -The hydrophobic region of an integral protein consist of one or more stretches of nonpolar amino acids, usually coiled into a-helices. -The hydrophilic parts are exposed to the aqueous solutions on either side of the membrane. ...
Noppl40  Shuttles  on  Tracks
Noppl40 Shuttles on Tracks

... whether the two mRNAs originated from one or two genes. Hybridization of common probe II to rat genomic DNA resulted in single bands in the case of EcoRI- and BamHIdigested DNA, two for Hindlll, and several for Pstl and Bglll (Figure 2C). This pattern corresponded to the restriction map of probe II ...
UNIT I Biomolecules - McGraw
UNIT I Biomolecules - McGraw

... Finally, two or more separately folded protein strands may associate with each other to form the active form of a protein, which falls under the category of quaternary structure. The conventions and depictional devices for tertiary and quaternary structures are identical—the only difference is that ...
Module 3: Genes and Sequences (NCBI)
Module 3: Genes and Sequences (NCBI)

... to view results or submit a text query against the Homologene database. You can also following Links to Homologene from related records in other Entrez databases, such as Entrez Gene or UniGene. Pre-computed protein comparisons are also available for each protein in Entrez Protein in the BLink (BLAS ...
9.1 Amino Acids—A Second Look, Continued
9.1 Amino Acids—A Second Look, Continued

... • The  helix is a coiled structure, and much like the coil of a telephone cord, it is a right-handed coil. • This coil is stabilized by hydrogen bonds between the carbonyl oxygen of one amino acid and the N—H hydrogen atom of another amino acid located four amino acids from it in the primary struct ...
Amino Acid Metabolism
Amino Acid Metabolism

... • Zero or total nitrogen balance: the intake = the excretion (adult) Amount of nitrogen intake is equal to the amount of nitrogen excreted is zero or total nitrogen balance • Positive nitrogen balance: the intake > the excretion during pregnancy, infancy, childhood and recovery from severe illness o ...
(Protein Synthesis) Steps Initiation Elongation Termination
(Protein Synthesis) Steps Initiation Elongation Termination

... The eukaryote elongation steps are very similar to those in the prokaryotes. The EF-GGTP complex is EF2-GTP in eukaryotes. The protein elongation factor 1 alpha (EF-1α) is a key GTP-binding enzyme in protein synthesis which carries out the same function as the prokaryote EF-Tu. [Small groups of orga ...
The Genetic Code
The Genetic Code

... First, we have the deoxyribonucleic acid (DNA) molecule, arguably the most important molecule for life. In DNA all the information to create a living organism is encoded in its composition. DNA is a double-stranded aperiodic polymer of a base with a deoxyribose (a sugar) backbone. The base + sugar m ...
Ehlinger Assignment 2 Practical
Ehlinger Assignment 2 Practical

chapter12
chapter12

... Transcription begins when an RNA polymerase binds to a DNA sequence known as the promoter. RNA synthesis does not require a primer, but other proteins are needed. The first nucleotide at the 5’ end retains its three-phosphate group. The last nucleotide to be incorporated has an exposed 3’ –OH group ...
Slides
Slides

... combined with other one-dimensional descriptors in fold recognition methods (e.g., with simple scores for solvent accessibility of each amino acid)。 The approach is based on predicting one dimensional descriptors for a target, and identifying a similar fold by comparing these descriptors to the desc ...
Analyses for Molecular Interactions in Living Cells
Analyses for Molecular Interactions in Living Cells

... complementation of the lacZ locus of E. coli, demonstrating that fragments of b-galactosidase that have no enzyme activity can associate spontaneously to generate an active complex GFP fragments fused to peptide sequences capable of producing an antiparallel coiled coil produced flurescent complexes ...
final review
final review

... 21. Distinguish among a solute, a solvent, and a solution. 22. Distinguish between hydrophobic and hydrophilic substances. 23. Define acid, base, and pH. 24. Explain how acids and bases may directly or indirectly alter the hydrogen ion concentration of a solution. 25. Using the bicarbonate buffer s ...
General western blot protocol
General western blot protocol

... Western blotting is used to visualize proteins that have been separated by gel electrophoresis. The gel is placed next to a nitrocellulose or PVDF (polyvinylidene fluoride) membrane and an electrical current causes the proteins to migrate from the gel to the membrane. The membrane can then be probed ...
Learning Objectives
Learning Objectives

... 2. Distinguish between the “one gene-one enzyme” hypothesis and the “one geneone polypeptide” hypothesis and explain why the original hypothesis was changed. 3. Explain how RNA differs from DNA. 4. Briefly explain how information flows from gene to protein. 5. Distinguish between transcription and t ...
Amino Acids and Peptides-chap 3
Amino Acids and Peptides-chap 3

...  Determines properties of amino acids and proteins ...
Problem of Focus - Clarkson University
Problem of Focus - Clarkson University

... which contains a disulfide bond between the two cysteines. (Quian 1998). When the protein binds to the mercury the protein undergoes a conformational change which allows the protein to be recognized by a transmembrane protein, MerT which transports the mercury across the plasma membrane. The bacteri ...
Chapter 12
Chapter 12

... There should be a stop codon  And there must also be signals for termination  Terminator often contain a sequence coding for an RNA stretch that can form a hair pin with complementary base pairing  This works as a signal for RNA polymerase to stop transcription ...
Mutation of exposed hydrophobic amino acids to arginine to
Mutation of exposed hydrophobic amino acids to arginine to

... small. This is in accordance with literature, amino acid substitution usually does not significantly affect the stability [10,19], although important improvements of stability by mutagenesis of a single solvent-exposed residue have been reported [20,21]. Several mutations stabilize the protein. A po ...
Protein Synthesis PPT
Protein Synthesis PPT

... • What type of RNA molecule is responsible for taking the DNA copy from the nucleus into the cytoplasm • What parts of the cell do you find RNA in? • Can you outline the stages in transcription? ...
A1982NF37500001
A1982NF37500001

... serum albumin had the same emission properties. It turns out that albumin binds nearly everything and is more stable when cornplexed with fatty acids, certain alcohols, or N-acetyltryptophan. These or similar additives are often deliberately incorporated into commercial samples. Impurity removal req ...
AP BIOLOGY Chapter 4 - Livonia Public Schools
AP BIOLOGY Chapter 4 - Livonia Public Schools

... Molecules with both polar and nonpolar parts are called _______________ ...
haemoglobin: structure, properties and biomedical functions
haemoglobin: structure, properties and biomedical functions

... The pairing of one alpha chain and one non-alpha chain produces a hemoglobin dimer (two chains). The hemoglobin dimer does not efficiently deliver oxygen, however. Two dimers combine to form a hemoglobin tetramer, which is the functional form of hemoglobin. The heme group consists of an iron atom he ...
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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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