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Lecture 5: Major Nutrient Groups
Lecture 5: Major Nutrient Groups

... group of one to the carboxyl group of another  this bond is known as the peptide linkage  AA found in protein are known as residues  protein chains of AA have typically 100200 residues  many proteins have more than one chain ...
lesson_1_model3D_4
lesson_1_model3D_4

... Click on the 'Features' tab (bottom of the window) Double click on the feature lane titled “Modified residue” (posttranslational modification). This will highlight the residues in the structure. Then you can click on the residues to see their position and amino acid. Which two amino acid modificatio ...
Document
Document

... • Use a table of mRNA codons and their corresponding amino acids to deduce the sequence of amino acids coded by a short mRNA strand of known base sequence ...
Organic Molecules
Organic Molecules

... – Active site: location where substrate binds to enzyme – Enzymes are unique: • Never change shape or form! • Only fit one substrate! • Can be reused! ...
3.2-Cell Membrane
3.2-Cell Membrane

... • It is present in ALL living things o animals, plants, fungi, protists and bacteria ...
Cell Organelles
Cell Organelles

... tight packing of phospholipids ...
Chapter 3
Chapter 3

... interior out of contact with water (Fig. 3.7). The structures of hundreds of proteins have been determined by techniques such as x-ray crystallography and NMR. Different methods of representing structures are shown in Fig. 3.8. Keep in mind that most proteins are somewhat flexible and undergo subtle ...
Document
Document

... MA A G Y AV L S ...
Introduction to the Digestive System Notes
Introduction to the Digestive System Notes

... Liver, Pancreas and Gallbladder • Liver: The center of metabolic activity in the body provides bile salts to the small intestine, which are critical for digestion and absorption of fats. • Pancreas: provides a potent mixture of digestive enzymes to the small intestine which are critical for digesti ...
Final Examination
Final Examination

... common inability to interact with water  hydrophobic interactions always involve organic solvents, such as hexane  hydrophobic interactions can be disrupted at higher temperatures  hydrophobic interactions can involve only a part of a molecule, rather than the whole molecule 10. Nucleolin is a eu ...
Proteins
Proteins

... Signal transduction Transcription regulation Immune response Other vital cellular actions ...
Proteomics
Proteomics

... Proteomics • The proteome is larger than the genome due to alternative ...
An overview of biochemistry for bioCHEM480
An overview of biochemistry for bioCHEM480

... in the CFTR protein that results in misfolding than leads to a change in membrane permeability, (V9) and (2) phenylketonuria (PKU) caused by mutations in the PAH gene and thus diminished enzyme activity cause a buildup of Phe (and some of its catabolites) that has a deleterious physiological effect ...
Ch. 4-5 - Carbon and Organic Chem
Ch. 4-5 - Carbon and Organic Chem

... Enzymes work by a physical fit (Lock and Key) between the enzyme molecule and its SUBSTRATE, the reactant being catalyzed. Enzymes reduces the activation energy for the chemical reaction to ...
Tisdag 17 jan
Tisdag 17 jan

... asthma, low grade metabolic inflammation, etc.), furthermore it is used as an indicator of well being in farmed fish. Permeability, the flow of substances across a porous wall, in the intestine can mainly be divided in two fundamentally different parts; transcellular (through cells, across both apic ...
Protein Structure - Laboratory of Molecular Modelling
Protein Structure - Laboratory of Molecular Modelling

... elements of separate polymer chains • may be promoted by chaperones, membrane proteins, cytosolic and extracellular elements as well as the proteins’ own propensities • E decreases further due to further desolvation and reduction of surface area • globular proteins, e.g. hemoglobin, largely involve ...
Protein Structure
Protein Structure

... elements of separate polymer chains • may be promoted by chaperones, membrane proteins, cytosolic and extracellular elements as well as the proteins’ own propensities • E decreases further due to further desolvation and reduction of surface area • globular proteins, e.g. hemoglobin, largely involve ...
Most common elements in living things are carbon, hydrogen
Most common elements in living things are carbon, hydrogen

... 30. Plant pigments like ______________ are also __________. 31. Lipids have more ___________ and _______ than they do oxygen atoms. 32. Fats are made of an alcohol called __________ and three __________ _________ chains. This is known as a ____________. 33. If there are all SINGLE bonds between ___ ...
Introduction to Macromolecular Structures
Introduction to Macromolecular Structures

... The sulfur or Se-methionines are the perfect starting point for the sequence fitting if the map is from sulfur SAS or Se-MAD phases. Tryptophan is so much larger than all the other amino acids it can often be recognized. Hydrophilic side chains are often disordered. A correct fitting should be eas ...
Structure determination by X
Structure determination by X

... The sulfur or Se-methionines are the perfect starting point for the sequence fitting if the map is from sulfur SAS or Se-MAD phases. Tryptophan is so much larger than all the other amino acids it can often be recognized. Hydrophilic side chains are often disordered. A correct fitting should be eas ...
Carbon-based molecules are life`s building blocks.
Carbon-based molecules are life`s building blocks.

... Nucleic acids (noo-KLEE-ihk AS-ihdz) are huge, complex carbonbased molecules that contain the information that cells use to make proteins. These macromolecules are made of carbon, hydrogen, and oxygen, as well as nitrogen and phosphorus. Each of the cells in your body contains a complete set of nucl ...
Protein Synthesis
Protein Synthesis

... • Clover-leaf shape • Single stranded molecule with attachment site at one end for an amino acid • Found out in the cytoplasm • Brings amino acid to ribosome ...
Topic 2 Molecular Biology
Topic 2 Molecular Biology

... illustrate the functions of proteins is not needed. • Egg white or albumin solutions can be used in denaturation experiments. • Students should know that most organisms use the same 20 amino acids in the same genetic code although there are some exceptions. Specific examples could be used for illust ...
Slide 1
Slide 1

... the muscles serves as the main gluconeogenic precursor for both liver and kidney. ...
chapter 7 membranes
chapter 7 membranes

...  Selective permeability – some substances cross more easily than others ...
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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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