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Macromolecules: Proteins
Macromolecules: Proteins

... Color code the amino acid on this worksheet (carbon-black, hydrogen-yellow, nitrogen-blue, and oxygen-red). Basic Structure of Amino acid H ...
A Protein Pathway
A Protein Pathway

Designer enzymes Donald Hilvert ETH Zurich, Zurich, Switzerland
Designer enzymes Donald Hilvert ETH Zurich, Zurich, Switzerland

... understand the rules of protein folding, and our knowledge of structure-function relationships in these macromolecules is at best incomplete. Nature has solved the problem of protein design through the mechanism of Darwinian evolution. From primitive precursors, recursive cycles of mutation, selecti ...
ORGANIC COMPOUNDS
ORGANIC COMPOUNDS

...  Order of bases determine what amino acids sequence is used in protein  function of individual proteins ...
Chapter01 Introduction Amino Acids, Peptides and Proteins (绪论
Chapter01 Introduction Amino Acids, Peptides and Proteins (绪论

... Gel Electrophoresis (SDS-PAGE). The hydrophobic tail of dodecylsulfate interacts strongly with polypeptide chains. Each dodecylsulfate contribute two negative charges. Thus all protein samples undergone electrophoresis are negatively charged. Sulfhydryl-reducing agents such as -mercaptoethanol is a ...
FST 123 - Enzymology Homework IS `13
FST 123 - Enzymology Homework IS `13

... c. What predictions can you make about the results of a native PAGE at pH 7.6 (State any assumptions you might need to make about the % acrylamide in the gel.) d. Sketch the elution profile of these proteins from a carboxymethyl cellulose ion exchange chromatography column, run at pH 6.25 (with a sa ...
Exam II Review: - Texas Tech University
Exam II Review: - Texas Tech University

...  RF-2: Recognizes UAA + UGA stop codons.  RF-3: Stimulates RF- 1 & 2 release via GTP hydrolysis.  RRF: Together with EF-G, induces ribosomal dissociation of small and large subunits. ...
Unit 2 Test Retake Review Sheet – Cell Biology Answer questions
Unit 2 Test Retake Review Sheet – Cell Biology Answer questions

... Why are macromolecules important components of living things? Macromolecules are polymers composed of repeating sub-units called ___________. Identify the basic monomer for each type of macromolecule. Describe the structure of carbohydrates, proteins, lipids, and nucleic acids Distinguish the functi ...
Organic Molecules
Organic Molecules

... • Made up of monomers called amino acids • 20 essential amino acids form polypeptide bonds to form protein ...
G-protein linked receptors
G-protein linked receptors

... • The addition of Pi to a protein, which activates the protein. • Usually adds Pi to Serine or Threonine. ...
Introduction, ppt file - Cheriton School of Computer Science
Introduction, ppt file - Cheriton School of Computer Science

...  It is unclear why Dform was not chosen ...
Question 2:
Question 2:

... enzymatic activity of alkaline phosphatase and beta–galactosidase in live bacteria. In contrast, D-Pyrrhocoricin, magainin 2, or buforin II, an antimicrobial peptide involved in binding to bacterial nucleic acids (see below), had only negligible effect. Example 2: Binding to DNA and inhibit DNA synt ...
BIOS 1300 SI WORKSHEET 2 (Chapter 2) SI Leader: Merrin Jeffries
BIOS 1300 SI WORKSHEET 2 (Chapter 2) SI Leader: Merrin Jeffries

... 21.List (from simplest to most complex) the four levels of structural complexity that proteins can have: ...
Cellular compartmentalization
Cellular compartmentalization

... Here is an illustration of how proteins targeted to the mitochondria are delivered. First the protein must carry the appropriate signal sequence. Then, it attaches to a receptor protein on the outer membrane. This complex diffuses until it reaches a contact site, where it is treaded through both ch ...
RNA and protein synthesis
RNA and protein synthesis

... from monomers called amino acids. Hundreds of amino acids linked together by peptide bonds and fold into a specific shape to make up a protein. There are 20 different types of amino acids. ...
02/13
02/13

... Nuclear localization sequences (NLSs) are located in interior of proteins such as DNA and RNA polymerases. They are recognized by nuclear pore proteins for transport into nucleus. ...
Lecture 4
Lecture 4

... interact with the non polar lipid bilayers, they have hydrophobic amino acid residues on the surface. These proteins do not have stable structures in aqueous solution. ...
ERT320 BIOSEPARATION ENGINEERING
ERT320 BIOSEPARATION ENGINEERING

... aggregated protein, and undissolved nutrients. Common operations for this purpose are sedimentation, centrifugation, and filtration.  Isolation and Concentration. Generally refers to the isolation of the desired product from unrelated impurities. Significant concentration is achieved in the early s ...
Proteins
Proteins

Ribosome and Endoplasmic Reticulum
Ribosome and Endoplasmic Reticulum

... What is a Ribosome? A Ribosome is a cluster of proteins and nucleic acids that constructs proteins in a cell. They are found in the cytoplasm of a cell or on the endoplasmic reticulum and in both animal and plant cells. ...
Can use more than once
Can use more than once

... Hydrophobic Tails Cell membrane Hydrophilic Head Chemical Signals Steak ...
Ch6PROTEIN
Ch6PROTEIN

... • Otherwise, the resulting conditions of acidosis or alkalosis could lead to coma or death Transport Functions • Lipoproteins • Albumin transports a variety of nutrients such as calcium, zinc, and Vitamin B6 • Transferrin transports iron (hemoglobin – a protein, contains iron, but it transports oxyg ...
Protein Structure HW Key
Protein Structure HW Key

... 1. Give three roles of proteins in an organism. nutrition, structure, motility, enzymes, regulatory, defense, recognition.... 2. What are prosthetic groups? non amino acid parts of a protein (heme in hemoglobin, for example) 3. What are glycoproteins and lipoproteins? glycoproteins are proteins with ...
Honors Biology Name Biochemistry Exam Review #1 Period _____
Honors Biology Name Biochemistry Exam Review #1 Period _____

... The pocket or groove where the substrate fits into on the enzyme is called the active site. (See diagram in enzyme notes for enzyme structure) Enzymes are named for the substrate that they work with. Names usually end in –ase (ex. Lactase, Helicase) Enzymes can be denatured (a change in shape) by a ...
Review Sheet - Phillips Scientific Methods
Review Sheet - Phillips Scientific Methods

... o Proteins can have polymers and monomers o Polypeptide is a polymer of amine o Kinks can occur where double bond is present o Some can be acidic or basic –depending on balance of functional groups o Some hydrophilic, some hydrophobic o A peptide bond is formed during dehydration synthesis  Bond be ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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