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Protein synthesis and chance
Protein synthesis and chance

... (nucleotides)  making  up  the  DNA  contains  the  information  needed  for  building  proteins.     Simplifying  the  process  greatly,  we  can  say  that  first  a  sort  of  carbon  copy  is  made  of  the   sequences  encoded  i ...
Document
Document

... 2 The amino acids are then absorbed by active transport into the absorptive cells, and move to their opposite ...
Name___________________________ Date_________________ Period_____
Name___________________________ Date_________________ Period_____

...  All of the information contained in our genes is based on the sequence of nucleotides in the DNA molecule. (B) TYPES OF RNA o RNA serves as a temporary copy of DNA and delivers the infomation on how to make proteins to the ribosomes o ...
Biomolecules Unit Review File
Biomolecules Unit Review File

... 12. Draw a single nucleotide. Draw a chain of nucleic acid. How many strands does DNA have? How many strands does RNA have? 13. What provides more energy lipids or carbohydrates? What type of energy are each of them? 14. What is glycogen? Where can you find it? What organisms utilize glycogen? 15. W ...
Slide ()
Slide ()

... COPII vesicles to the cis-Golgi (anterograde transport). Movement of proteins through the Golgi appears to be mainly by cisternal maturation. In the TGN, the exit side of the Golgi, proteins are segregated and sorted. Secretory proteins accumulate in secretory vesicles (regulated secretion), from wh ...
Slide ()
Slide ()

... COPII vesicles to the cis-Golgi (anterograde transport). Movement of proteins through the Golgi appears to be mainly by cisternal maturation. In the TGN, the exit side of the Golgi, proteins are segregated and sorted. Secretory proteins accumulate in secretory vesicles (regulated secretion), from wh ...
PowerPoint - hrsbstaff.ednet.ns.ca
PowerPoint - hrsbstaff.ednet.ns.ca

... 20 different AA’s used by ribosomes to make proteins The R group is the deciding factor as to what the AA is as all the amino and carboxyl ends are used in bonding the AA’s together There are some modifications to the AA in a polypeptide chain – proline modifies to hydroxyproline when in collagen – ...
Protein Chemistry
Protein Chemistry

... Primary structure: amino acid only. The actual amino acid sequence is specified by the DNA sequence. The primary structure is used to determine genetic relationships with other proteins - AKA homology. Amino acids that are not changed are considered invariant or conserved. Primary sequence is also u ...
Molecules of Life - Reading molecules of life
Molecules of Life - Reading molecules of life

... Carbohydrates are sugars, or long chains of sugars. An important role of carbohydrates is to store energy. Glucose (Figure below) is an important simple sugar molecule with the chemical formula C6H12O6. Simple sugars are known as monosaccharides. Carbohydrates also include long chains of connected s ...
Biology
Biology

... • Are abundant – making up 50% or more of cellular dry weight. ...
Amino Acids - Chemistry Courses: About
Amino Acids - Chemistry Courses: About

... • Zinc finger • Disulfide bond ...
Biology-Chapter2 (Biology
Biology-Chapter2 (Biology

... notes that there are now 21 types of this biomolecule instead of the old known 20. The molecule can also be combined with others in its class to produce a wide variety of proteins, some liquid and others solid. What type of biomolecule did Edgar find? A. a nucleic acid B. a monosaccharide C. an amin ...
Chemical Principles
Chemical Principles

...  Contain C, H, N, O and sometimes P and S.  Essential for structure and function of cell  Ex: enzymes, hormones, structural molecules, ...
Levels of protein structure:
Levels of protein structure:

... Levels of protein structure (let these notes and the class notes supplement each other). 1. Primary structure. This is the amino acid sequence. Amino acids (a.a.) are covalently bonded (one to the next) via dehydration synthesis, involving the carboxyl group of one a.a and the amino group of the nex ...
Lecture 3 (BY 14)
Lecture 3 (BY 14)

... • Atoms or clusters of atoms that are covalently bonded to carbon backbone • Give organic compounds their different properties ...
Proteomics
Proteomics

... Structure Prediction • Can be used for any protein whose amino acid sequence is known. • Speed – much faster than crystallography. • Understand (structure dependent) function of proteins. • Protein structure needed for drug design. ...
Chapt. 3-Proteins - University of New England
Chapt. 3-Proteins - University of New England

... • Definite 3D regions along a polypeptide with a precise function • Example: enzyme binding sites, substrate binding sites ...
Nucleic Acids - Spring Branch ISD
Nucleic Acids - Spring Branch ISD

... 50% of the dry mass of the cell. A protein monomer is called an Amino Acid. Humans require 20 amino acids, but only can produce 10 internally. The other ten are acquired through food. Structure: Amino Acid Monomer Amino Group ...
Week 2
Week 2

... - Oxidation of Cystein can be a growth factor induced signal to ramp up cell proliferation via phosphorylation of Tyrosine. It does this by catalyzing the formation of disulphide bonds… ...
Nucleic Acid Notes
Nucleic Acid Notes

Macromolecules: Proteins and Nucleic Acids
Macromolecules: Proteins and Nucleic Acids

... Proteins are the most structurally and functionally diverse of life’s molecules • Proteins are involved in – cellular structure – movement – defense – transport – Communication ...
protein
protein

... There are 20 amino acids. Some of them are nonessential because they can be made by your body, but 9 of them are essential amino acids. That means it is essential for you to ______________________ ...
protein_folding
protein_folding

... – sulphur bridges - covalent S-S bonds between two cysteine amino acids, which are strong. ...
pptx
pptx

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

... properties of organic compounds • The unique properties of an organic compound depend not only on its carbon skeleton but also on the atoms attached to the skeleton – These atoms are called functional groups ...
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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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