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Final Exam: Multiple Choice Portion Biochem Block Spring 2016
Final Exam: Multiple Choice Portion Biochem Block Spring 2016

... d) fairly small (<< 1 M) because this acid is a weak acid 12. (3 pts) The distance between stacked bases of DNA is: a) 3 m b) 3 x 108 m/s c) 3 D d) 3 x 10-9 m e) 3.4 D f) 34 D 13. (3 pts) Cytochrome c peroxidase has an isoelectric point (pI) of 5.2. A reasonable value for the charge on this protein ...
Protein Structure Predictions 2
Protein Structure Predictions 2

AMINO ACIDS COMPLEX Factsheet
AMINO ACIDS COMPLEX Factsheet

... contain approximately 16% nitrogen, which differentiates them from the other two primary nutrients, sugars and fatty acids, which do not contain nitrogen. Proteins are chains of amino acids linked by peptide bonds. Proteins are not obtained directly from human diet, instead they are broken down from ...
protein translocation.
protein translocation.

... functions in the cytosol. • The ribosomes on which these proteins are synthesized are sometimes called "free ribosomes". • The "default" for a protein released from "free" ribosomes is to remain in the cytosol. • To be targeted to a specific location requires an appropriate signal, typically a seque ...
Notes - Part 1.
Notes - Part 1.

... amino acid residues in the common secondary structures. R corresponds to the helix (also known as the 3.613 helix), This has 3.6 residues per turn. It is a righthanded helix, with the carbonyls pointing towards the C-terminus of the helix, and the sidechains and NH groups towards the N-terminus (s ...
Cube Biotech
Cube Biotech

... One advantage of the system is the high specificity of the antibody-epitope interaction. Epitope sequence and chain length are critical for binding. For example, replacing the third alanine with glycine which removes a single methyl group, eliminates binding. Likewise, the full 9-amino acid tag bind ...
Critical Reading: Organic Compounds
Critical Reading: Organic Compounds

... in organic compounds, so carbon is essential to life on Earth. Without carbon, life as we know it could not exist. Why is carbon so basic to life? The reason is carbon’s ability to form stable bonds with many elements, including itself. This property allows carbon to form a huge variety of very larg ...
Collapse of Homochirality of Amino Acids in Proteins from Various
Collapse of Homochirality of Amino Acids in Proteins from Various

... chains of the following amino acids of the Asp residues are small, and a chiral reaction field exists in the vicinity of the Asp residues. This indicates that d-b-Asp-containing proteins may be much more widespread in various tissues than previously thought. Therefore, to detect d-b-Asp-containing p ...
AMINO ACIDS, POLYPEPTIDES, AND PROTEINS
AMINO ACIDS, POLYPEPTIDES, AND PROTEINS

... Quaternary structure. The three-dimensional shape formed by an aggregate of protein subunits found in some complex proteins. ...
Protein Structure
Protein Structure

... 3-dimensional arrangement of all atoms in a single polypeptide chain The entire protein molecule coils into an overall threedimensional shape-Functional property to the protein Spatial arrangement of amino acid residues that are far apart in a linear sequence Superfolding brings functional groups th ...
Document
Document

... prevents folding Guides it to SecA, which drives it through SecYEG into periplasm using ATP In periplasm signal peptide is removed and protein folds ...
Proteins, Proteomics, and Post
Proteins, Proteomics, and Post

... ...
3.2 Carbohydrates, Lipids, and Proteins
3.2 Carbohydrates, Lipids, and Proteins

... • All organic molecules contain Carbon, but not everything with C is organic Ex: carbon dioxide not organic ...
Protein Building Blocks (PBBs): Toys for teaching the principles of
Protein Building Blocks (PBBs): Toys for teaching the principles of

... like beads on a string. These beads interact in different ways to cause the beads on a string to fold up into specific threedimensional structures. The shapes of these structures allow the protein machinery to carry out functions as diverse as muscle contraction (actin and myosin) and transporting o ...
Protein_hierarchy
Protein_hierarchy

... • (c) describe, with the aid of diagrams, the formation and breakage of peptide bonds in the synthesis and hydrolysis of dipeptides and polypeptides; • (d) explain, with the aid of diagrams, the term primary structure; • (e) explain, with the aid of diagrams, the term secondary structure with refere ...
Organic Molecules: The Molecules of Life
Organic Molecules: The Molecules of Life

... fats in animal bodies function as a long term energy storage fatty tissue also covers our organs and protects them from injury lipids do not dissolve in water It is possible for us to digest fats because we emulsify them. Bile from our gall bladder is secreted into our digestive tract and causes fat ...
Proteins
Proteins

... Eating enough fiber reduces the risk of heart disease. ...
Slide 1 - MisterSyracuse.com
Slide 1 - MisterSyracuse.com

... 26. An artificial cell is created by placing a plastic bag in a beaker of water (figure1). The key below shows what chemicals are in the bag and in the beaker. Predict what would happen over time by showing the location of molecules I, G, and S in diagram B of figure 2. ...
Physicists Identify Factors Governing Protein Aggregation, a
Physicists Identify Factors Governing Protein Aggregation, a

... protein aggregation. For example, Alzheimer's disease is thought to be related to the aggregation of Aβ 40 (a protein made up of 40 amino acids) and Aβ 42 (a protein made up of 42 amino acids), while Huntington's disease and spinocerebellar atrophy are related to aggregation of PolyQ (a protein with ...
Nutrients note
Nutrients note

... - a process by which the peptide bonds between the amino acids are reconfigured which causes a loss of the protein’s biological properties - can be caused by heat, radiation, pH changes or salty environments - once the physical or chemical factor is removed, the protein may assume its original shape ...
Module 1: Review of General and Organic Chemistry
Module 1: Review of General and Organic Chemistry

A Guided Reading on Macromolecules
A Guided Reading on Macromolecules

... 28. _________________ makes up cell membranes. 29. Name a waxy lipid covering plants. 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 __________ _________ c ...
File
File

Protein Biosynthesis at Three Levels of Modifications
Protein Biosynthesis at Three Levels of Modifications

carbohydrate, protein and fat.
carbohydrate, protein and fat.

... Fats coat the flour particles and prevent them from absorbing water. This reduces the formation of gluten development, which would cause the dough to become elastic. Fats such as pure vegetable fats or lard are suitable for shortening because of their low water content. There are distinctive colours ...
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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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