The trans-Golgi network GRIP-domain proteins form α
... On the basis of their high content of coiled coils, these molecules are predicted to adopt a rod-like or extended fibrous structure. Members of the family of coiled-coil proteins specifically located on the Golgi (termed golgins), such as p115 and GM130, have been shown to be important as tethering ...
... On the basis of their high content of coiled coils, these molecules are predicted to adopt a rod-like or extended fibrous structure. Members of the family of coiled-coil proteins specifically located on the Golgi (termed golgins), such as p115 and GM130, have been shown to be important as tethering ...
AP Biology Summer Homework Macromolecules WebQuest
... page, click “continue”, and then “play” to watch the animation. 1. What are the two types of nucleic acids? ____________________ and ____________________ 2. What do nucleic acids have the ability to do within the cell? 3. When two strands of DNA pair by hydrogen bonding, the base ___________________ ...
... page, click “continue”, and then “play” to watch the animation. 1. What are the two types of nucleic acids? ____________________ and ____________________ 2. What do nucleic acids have the ability to do within the cell? 3. When two strands of DNA pair by hydrogen bonding, the base ___________________ ...
lecture 15
... A Simplified Schematic of Possible Hsp90 Function Substrate is represented as a green circle to mark the expected position of contacts, but not as a direct indication of substrate size or structural details. The bulk of the substrate may, in fact, be variously extended outside of the Hsp90 clamp wit ...
... A Simplified Schematic of Possible Hsp90 Function Substrate is represented as a green circle to mark the expected position of contacts, but not as a direct indication of substrate size or structural details. The bulk of the substrate may, in fact, be variously extended outside of the Hsp90 clamp wit ...
intact-protein based sample preparation strategies for
... National Cancer Institute (Emmert-Buck et al., 1996). It has been successfully used to isolate single cells within a tissue section (Emmert-Buck et al., 1996). Cells can be selected according to their phenotypic and functional characteristics. The major limitation of the LCM approach for proteomics ...
... National Cancer Institute (Emmert-Buck et al., 1996). It has been successfully used to isolate single cells within a tissue section (Emmert-Buck et al., 1996). Cells can be selected according to their phenotypic and functional characteristics. The major limitation of the LCM approach for proteomics ...
Protein Motif Recognition I Introduction
... the structure or fold of a protein provides the key to understanding its biological function, and proteins play a variety of important roles in the body (e.g., as enzymes, antibodies, etc.). Proteins may also be associated with particular human diseases, and thus, understanding protein structure may ...
... the structure or fold of a protein provides the key to understanding its biological function, and proteins play a variety of important roles in the body (e.g., as enzymes, antibodies, etc.). Proteins may also be associated with particular human diseases, and thus, understanding protein structure may ...
Full Text
... use of multiple sequence alignment methods to create families of related proteins (1,2). The conservation information contained in a multiple sequence alignment is often condensed into a sequence motif to provide a tool for easily assigning new sequences to the family. These motifs are compact repre ...
... use of multiple sequence alignment methods to create families of related proteins (1,2). The conservation information contained in a multiple sequence alignment is often condensed into a sequence motif to provide a tool for easily assigning new sequences to the family. These motifs are compact repre ...
pam&blosum
... then calculated by subtracting the position in the first sequence from that in the second. Words that have the same offset position reveal a region of alignment between the two sequences. The number of comparisons increases linearly in proportion to average sequence length. In contrast, the time tak ...
... then calculated by subtracting the position in the first sequence from that in the second. Words that have the same offset position reveal a region of alignment between the two sequences. The number of comparisons increases linearly in proportion to average sequence length. In contrast, the time tak ...
Lecture Protein Metabolism
... Sources of Amino Acids for Host Animal 1. Microbial proteins Quantity determined by: a) Fermentability of the feed b) Quantity of feed consumed c) Nitrogen available to microorganisms 2. Undegraded feed proteins (UIP) Quantity will vary in relation to: a) Degradability of feed proteins b) Quantity ...
... Sources of Amino Acids for Host Animal 1. Microbial proteins Quantity determined by: a) Fermentability of the feed b) Quantity of feed consumed c) Nitrogen available to microorganisms 2. Undegraded feed proteins (UIP) Quantity will vary in relation to: a) Degradability of feed proteins b) Quantity ...
Molecular cloning, expression, and bioactivity of dove B lymphocyte
... B cell activating factor (BAFF) belonging to the tumor necrosis factor (TNF) family is a novel member of the tumor necrosis factor ligand family and plays an important role in B lymphocyte maturation and survival. cDNA of dove B lymphocyte stimulator (doBAFF) was amplified from total RNA of dove sple ...
... B cell activating factor (BAFF) belonging to the tumor necrosis factor (TNF) family is a novel member of the tumor necrosis factor ligand family and plays an important role in B lymphocyte maturation and survival. cDNA of dove B lymphocyte stimulator (doBAFF) was amplified from total RNA of dove sple ...
Document
... called monomer. It can be a molecule, a molecule fragment or just an atom. Each such monomer has an at most three letter long code, called monomer id, eg. ALA for alanine, MG for magnesium ion, ACE for acethyl group, or HOH for water. A protein chain consists of many amino acid monomers, each having ...
... called monomer. It can be a molecule, a molecule fragment or just an atom. Each such monomer has an at most three letter long code, called monomer id, eg. ALA for alanine, MG for magnesium ion, ACE for acethyl group, or HOH for water. A protein chain consists of many amino acid monomers, each having ...
12-3 RNA and Protein Synthesis
... separates the DNA strands. RNA Polymerase then uses one strand of DNA as a template to assemble nucleotides into RNA Foothill High School Science Department ...
... separates the DNA strands. RNA Polymerase then uses one strand of DNA as a template to assemble nucleotides into RNA Foothill High School Science Department ...
Both DRIs and RDAs refer to long-term average daily nutrient intake
... • Proteins consumed in excess of the body's needs is deaminated and the resulting carbon skeleton metabolized to provide: 1- energy or 2- acetyl CoA for fatty acid synthesis If carbohydrates intake is less than 130 g/day ,, Therefore, carbohydrate is considered to be protein-sparing,as it allows ami ...
... • Proteins consumed in excess of the body's needs is deaminated and the resulting carbon skeleton metabolized to provide: 1- energy or 2- acetyl CoA for fatty acid synthesis If carbohydrates intake is less than 130 g/day ,, Therefore, carbohydrate is considered to be protein-sparing,as it allows ami ...
Protein folding
... Partially folded states are problematic - they tend to aggregate in concentrationdependent manner. Aggregation primarily results in amorphous structures. Alternatively, fibrillar aggregates called amyloid may form. Formation of these aggregates in vivo is strongly restricted by the chaperone machine ...
... Partially folded states are problematic - they tend to aggregate in concentrationdependent manner. Aggregation primarily results in amorphous structures. Alternatively, fibrillar aggregates called amyloid may form. Formation of these aggregates in vivo is strongly restricted by the chaperone machine ...
File
... similar magnitude of energy difference driving their diffusion across a pure lipid bilayer. If ranked in order from fastest to slowest, which of the following items would likely be second in terms of how much of it crosses the bilayer in a given time? a) molecular oxygen b) sucrose c) insulin d) glu ...
... similar magnitude of energy difference driving their diffusion across a pure lipid bilayer. If ranked in order from fastest to slowest, which of the following items would likely be second in terms of how much of it crosses the bilayer in a given time? a) molecular oxygen b) sucrose c) insulin d) glu ...
Slide 1
... 6.13 Fermentation enables cells to produce ATP without oxygen Fermentation is a way of harvesting chemical energy that does not require oxygen. Fermentation – takes advantage of glycolysis, – produces 2 ATP molecules per glucose, and – oxidizes NADH back to NAD+ ...
... 6.13 Fermentation enables cells to produce ATP without oxygen Fermentation is a way of harvesting chemical energy that does not require oxygen. Fermentation – takes advantage of glycolysis, – produces 2 ATP molecules per glucose, and – oxidizes NADH back to NAD+ ...
f212 biological molecules
... • Final molecules maybe 1000’s of monosaccharides, the size of these molecules make them insoluble. • Polysaccharides are NOT sugars • The most important polysaccharides are built up entirely of glucose molecules. • These are starch, glycogen and cellulose. ...
... • Final molecules maybe 1000’s of monosaccharides, the size of these molecules make them insoluble. • Polysaccharides are NOT sugars • The most important polysaccharides are built up entirely of glucose molecules. • These are starch, glycogen and cellulose. ...
Presentation
... domains offer an interesting look into the flexing of the protein’s tertiary structure Monitoring exactly how this conformational change takes place would offer some insight into how the amino acid backbone shifts and contracts to allow proper binding to pERK. ...
... domains offer an interesting look into the flexing of the protein’s tertiary structure Monitoring exactly how this conformational change takes place would offer some insight into how the amino acid backbone shifts and contracts to allow proper binding to pERK. ...
Transmembrane domains control exclusion of membrane proteins
... membrane proteins. We used CD1b as a reporter protein because this protein normally traffics through endocytic compartments (Jackman et al., 1998) and thus should not be sensitive to proteases found in endosomal compartments. Indeed, we have observed that both CD1b and its specific monoclonal antibo ...
... membrane proteins. We used CD1b as a reporter protein because this protein normally traffics through endocytic compartments (Jackman et al., 1998) and thus should not be sensitive to proteases found in endosomal compartments. Indeed, we have observed that both CD1b and its specific monoclonal antibo ...
Identification of Surface Residues Involved in Protein
... metabolic and signal transduction pathways. The results reported here demonstrate that an SVM classifier can reliably predict interface residues and recognize protein-protein interaction surfaces in proteins of antibody-antigen and proteaseinhibitor complexes. In this study, interface and non-interf ...
... metabolic and signal transduction pathways. The results reported here demonstrate that an SVM classifier can reliably predict interface residues and recognize protein-protein interaction surfaces in proteins of antibody-antigen and proteaseinhibitor complexes. In this study, interface and non-interf ...
CHAPTER 4: CELLULAR METABOLISM OBJECTIVES: 1. Compare
... metabolic processes!). The portion of a DNA molecule that contains the genetic information for making one kind of protein is called a gene. In order to understand how DNA (confined to the nucleus) can direct the synthesis of proteins (which occurs in the cytoplasm), we must first look at the structu ...
... metabolic processes!). The portion of a DNA molecule that contains the genetic information for making one kind of protein is called a gene. In order to understand how DNA (confined to the nucleus) can direct the synthesis of proteins (which occurs in the cytoplasm), we must first look at the structu ...
Protein Prenylation: Genes, Enzymes, Targets, and Functions
... Annu. Rev. Genet. 1992.26:209-237. Downloaded from arjournals.annualreviews.org by Medical Research Council-Cambridge UK on 11/21/06. For personal use only. ...
... Annu. Rev. Genet. 1992.26:209-237. Downloaded from arjournals.annualreviews.org by Medical Research Council-Cambridge UK on 11/21/06. For personal use only. ...
Protein quality measures - essential amino acids (EAAs
... trans/cis linoleic acids (CLAs) at right are cardioprotective and anticancer in experimental ...
... trans/cis linoleic acids (CLAs) at right are cardioprotective and anticancer in experimental ...
Transcription and Translation
... Transcription Review • What is transcription? • Name 3 things that are different between DNA and RNA. • What does uracil pair with? • What is the function of mRNA? ...
... Transcription Review • What is transcription? • Name 3 things that are different between DNA and RNA. • What does uracil pair with? • What is the function of mRNA? ...
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.