Biozentrum: Research group Martin Spiess
... and lead to the disease diabetes insipidus. They produce protein aggregations similar to amyloids found in neurological diseases like Alzheimer's. We are testing the hypothesis that amyloid-like aggregation is normally involved in the formation of secretory granules for regulated hormone secretion. ...
... and lead to the disease diabetes insipidus. They produce protein aggregations similar to amyloids found in neurological diseases like Alzheimer's. We are testing the hypothesis that amyloid-like aggregation is normally involved in the formation of secretory granules for regulated hormone secretion. ...
Coevolution in protein families: a functional correlation study.
... In this study we restrict our goal to the prediction of the set of residues in physical contacts (i.e. the set of residue pairs at distance lower than 8Å in the native 3-D structure). Local correlation based analysis (e.g. mutual information) are attractive measures because they explicitly show the ...
... In this study we restrict our goal to the prediction of the set of residues in physical contacts (i.e. the set of residue pairs at distance lower than 8Å in the native 3-D structure). Local correlation based analysis (e.g. mutual information) are attractive measures because they explicitly show the ...
Control of Gene Expression
... Proteins which control the expression of other genes Link the genome with the environment Activated by signals from outside the cell (e.g. hormones, sugar, etc.) Allow RNA polymerase to bind to the promoter so that transcription can begin Gene must also be exposed –DNA must unwind in that area. ...
... Proteins which control the expression of other genes Link the genome with the environment Activated by signals from outside the cell (e.g. hormones, sugar, etc.) Allow RNA polymerase to bind to the promoter so that transcription can begin Gene must also be exposed –DNA must unwind in that area. ...
SUPPLEMENTARY DISCUSSION The applied Hi3 approach relies
... The applied Hi3 approach relies mainly on the assumption that the average intensity of the three most abundant peptides correlates with the abundance of the corresponding protein [1]. However, the ionization properties of specific peptides may influence the corresponding signal intensity during the ...
... The applied Hi3 approach relies mainly on the assumption that the average intensity of the three most abundant peptides correlates with the abundance of the corresponding protein [1]. However, the ionization properties of specific peptides may influence the corresponding signal intensity during the ...
Lecture 2
... may have multiple functions, arise differently from the same gene, and may be modified so the 25,000 figure isn't really relevant - we have a huge variety of proteins. Protein structure Proteins have a 3D structure with a great degree of flexibility that is formed through several distinct stages of ...
... may have multiple functions, arise differently from the same gene, and may be modified so the 25,000 figure isn't really relevant - we have a huge variety of proteins. Protein structure Proteins have a 3D structure with a great degree of flexibility that is formed through several distinct stages of ...
Chemistry in Biology - Welcome to teachers.olatheschools.com!
... 13---IDENTIFY/ FAMILIARIZE yourself with the four major families of biological macromolecules ...
... 13---IDENTIFY/ FAMILIARIZE yourself with the four major families of biological macromolecules ...
Bio102A organic notes (2)
... Unsaturated: at least one double bond, causes “kinks”, usually liquid ...
... Unsaturated: at least one double bond, causes “kinks”, usually liquid ...
Übung: Monte Carlo, Molecular Dynamics
... water spherical (like a football / billiards ball) or some different shape ? 5. Exam example question with many possible answers: Describe a low-resolution protein model which can ...
... water spherical (like a football / billiards ball) or some different shape ? 5. Exam example question with many possible answers: Describe a low-resolution protein model which can ...
PP-Protein Synthesis
... Identify the genetic code and explain how it is read. Summarize the process of translation. ...
... Identify the genetic code and explain how it is read. Summarize the process of translation. ...
Opening Questions - Belle Vernon Area School District
... the carbon skeleton are covalent bonds known as PEPTIDE BONDS Many peptide bonds are called POLYPEPTIDE bonds ...
... the carbon skeleton are covalent bonds known as PEPTIDE BONDS Many peptide bonds are called POLYPEPTIDE bonds ...
Determination of Amino Acid Sequence
... Chemical Synthesis of Small Peptide Developed by R. Bruce Merrifield (1962) Synthesis from C- to N- terminal on an polymer ...
... Chemical Synthesis of Small Peptide Developed by R. Bruce Merrifield (1962) Synthesis from C- to N- terminal on an polymer ...
Stabilization of Low Affinity Protein-Protein Interactions by
... approach for investigating and manipulating diverse biological processes. Among a number of different approaches, the expansion of the genetic code has emerged as an eminent tool for in vivo site-specific incorporation of unnatural amino acids (UAAs) into proteins [1]. The requirements for genetic c ...
... approach for investigating and manipulating diverse biological processes. Among a number of different approaches, the expansion of the genetic code has emerged as an eminent tool for in vivo site-specific incorporation of unnatural amino acids (UAAs) into proteins [1]. The requirements for genetic c ...
Getting things where they need to go: Protein Targeting
... Sorting places proteins in membrane and in lumen of organelles ...
... Sorting places proteins in membrane and in lumen of organelles ...
Project
... sphingolipid that is specific to invertebrates. Moreover, the genomes of some aegerolysin-producing fungi ...
... sphingolipid that is specific to invertebrates. Moreover, the genomes of some aegerolysin-producing fungi ...
Protein Structure and Bioinformatics
... • What is protein structure? • What are proteins made of? • What forces determines protein structure? • What is protein secondary structure? • What are the primary secondary structures? • How are protein structures determined experimentally? • How can structures be predicted in silico? ...
... • What is protein structure? • What are proteins made of? • What forces determines protein structure? • What is protein secondary structure? • What are the primary secondary structures? • How are protein structures determined experimentally? • How can structures be predicted in silico? ...
Teaching Notes
... 1. All proteins have specific shapes that are best suited for their function(s) 2. Strategic locations of amino acid residues, with different physical and chemical properties (side-chains), enable proteins to perform a variety of different functions in the cell. 3. Small globular proteins (made of o ...
... 1. All proteins have specific shapes that are best suited for their function(s) 2. Strategic locations of amino acid residues, with different physical and chemical properties (side-chains), enable proteins to perform a variety of different functions in the cell. 3. Small globular proteins (made of o ...
word
... Topology of compartments – from lumen of ER to Golgi to outside of cell From nucleus to where? General concepts: Consider integral membrane protein in the ER, versus a secreted protein or a nuclear protein. How are they targeted to their locations? What about a ribosomal protein? Draw structure of e ...
... Topology of compartments – from lumen of ER to Golgi to outside of cell From nucleus to where? General concepts: Consider integral membrane protein in the ER, versus a secreted protein or a nuclear protein. How are they targeted to their locations? What about a ribosomal protein? Draw structure of e ...
Chapter 5 - Richsingiser.com
... anticancer activity. Determine the sequence of the peptide from the following information. 1. One cycle fo Edman degradation of intact FP yields 2 mole of PTH-aspartate per mole of FP. 2. Treatment of a solution of FP with 2-ME followed by the addition of trypsin yields three peptides ...
... anticancer activity. Determine the sequence of the peptide from the following information. 1. One cycle fo Edman degradation of intact FP yields 2 mole of PTH-aspartate per mole of FP. 2. Treatment of a solution of FP with 2-ME followed by the addition of trypsin yields three peptides ...
Amino Acids
... • 3D folding or ‘bundling up’ of the protein • Non-polar residues are buried inside, polar residues are exposed outwards to aqueous environment • Many proteins are organized into multiple ‘domains’ • Domains are compact globular units that are connected by a flexible segment of the polypeptide • Eac ...
... • 3D folding or ‘bundling up’ of the protein • Non-polar residues are buried inside, polar residues are exposed outwards to aqueous environment • Many proteins are organized into multiple ‘domains’ • Domains are compact globular units that are connected by a flexible segment of the polypeptide • Eac ...
7.5 Proteins notes
... Immunoglobulins are otherwise known as antibodies. Produced by the plasma cells in an immune response to an infectious antigen. Great variation exists in the heavy chains which allows a response to virtually any possible antigen surface. Due to their high specificity in identifying antigen they are ...
... Immunoglobulins are otherwise known as antibodies. Produced by the plasma cells in an immune response to an infectious antigen. Great variation exists in the heavy chains which allows a response to virtually any possible antigen surface. Due to their high specificity in identifying antigen they are ...
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.