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An Introduction to Protein Structure Databases
An Introduction to Protein Structure Databases

... and orientation (no connectivities between the secondary structures)‫‏‬ Topology (FOLD family): overall shape and connectivities. Homologous superfamily: proteins are thought to share common ancestor. Similarities by sequence alignment and then by structure comparison using the SSAP structural align ...
Exam 1
Exam 1

... A group of organisms of the same species is a(n): A) system C) population D) genus E) none of the above ...
Two Rules on Protein-Ligand Interactions Xiaodong Pang1, 2
Two Rules on Protein-Ligand Interactions Xiaodong Pang1, 2

... Understanding the ruling principles of interaction between a target protein and a ligand is of paramount importance in drug discovery efforts. So far, in finding a real ligand for a given target protein, we are limited to experimental screening from a large number of small molecules, or through free ...
Proteiinianalyysi 5
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... The energy score for a contact between secondary structures is summed using database statistics. ...
99( I )生技所分生考題,林富邦老師部分
99( I )生技所分生考題,林富邦老師部分

... pre-proteins are maintained in a loosely folded, translocation-competent conformation through interaction with molecular chaperones. membranes involved in translocation have specific protein receptors exposed on their cytosolic faces. translocons catalyze movement of the proteins across the membrane ...
Annexure `CD-01` L T P/S SW/FW TOTAL CREDIT UNITS 3 0 0 0 3
Annexure `CD-01` L T P/S SW/FW TOTAL CREDIT UNITS 3 0 0 0 3

... fundamental concepts in biochemistry. This will also help the students to enumerate the molecular motif of a living cell, structural and functional hierarchy of biomolecules besides emphasis on the various aspects of metabolism and interrelationship of metabolic events. Prerequisites: Basic concept ...
The Synthesis and Expression of Peptide CbnY Thomas Doerksen
The Synthesis and Expression of Peptide CbnY Thomas Doerksen

... The King’s University ORAL Collaboration Bacteriocins are small antimicrobial peptides produced by bacteria, and have great potential in the food industry as an alternative to antibiotics. The two-component bacteriocins, produced by various strains of lactic acid bacteria, display optimal activity w ...
The Nature of Matter
The Nature of Matter

...  Some control the rate of reactions and regulate cell processes (Enzymes are proteins).  Some are used to form bone and muscles.  Some transport substances into or out of cells or help fight diseases. ...
Macromolecule Summary Chart
Macromolecule Summary Chart

... Glycosidic linkage ...
3-3 notes answers
3-3 notes answers

... Organelle – specialized structures within the cell The following organelles are found in both plant and animal cells: Nucleus – controls most of the cell functions Nuclear envelope / nuclear membrane – double layer (2 lipid bilayers) Nuclear pores – small channels scattered over/through membrane Sub ...
Chapter 3: The Chemistry of Life: Organic Compounds
Chapter 3: The Chemistry of Life: Organic Compounds

... 3. Essential amino acids are those that must be ingested in the diet of an animal B. Peptide bonds join amino acids 1. 2 amino acids form a dipeptide 2. Polypeptides are formed from more than 2 amino acids C. Proteins have 4 levels of organization 1. Primary structure is the amino acid sequence 2. S ...
Ubiquitin-proteosome protein degradation ppt
Ubiquitin-proteosome protein degradation ppt

... Decrease steady-state levels of aggregate prone proteins in the absence of Usp14 ...
food proteins
food proteins

... phase but also strengthen the interface. ...
Preparation and transformation of competent bacteria: Calcium
Preparation and transformation of competent bacteria: Calcium

... (use information from these databases or the Berg reading material, note that you may need to clink on links). Please indicate which source each answer comes from. a. What metabolic pathway does this protein belong to? ...
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Carbohydrates

... • The 20 different amino acids can be joined by peptide bonds with an almost infinite number of combinations • Proteins vary greatly in size – some are as small as 3 amino acids in length – some are as large as 34350 amino acids in length • 4 levels of structural complexity in proteins • Primary str ...
Simulating Protein Synthesis and RNA Interference in the
Simulating Protein Synthesis and RNA Interference in the

... The students represent the active portions of the protein synthesis pathway, whether it be proteins or RNA. The paper represents information carried either in the DNA or the mRNA and contains the instructions for the creation of specific proteins. The teacher represents the RNA silencing protein com ...
Lecture 10 - Columbus Labs
Lecture 10 - Columbus Labs

... Structural basis of the collagen triple helix • Every third residue faces the crowded center of the helix - only Gly fits here • Pro and HyP suit the constraints of phi and psi • Interchain H-bonds involving HyP stabilize helix • Fibrils are further strengthened by intrachain lysine-lysine and inte ...
republique française - Laboratoire Léon Brillouin (LLB)
republique française - Laboratoire Léon Brillouin (LLB)

... investigate solution organization or solvation dynamics give highly averaged information over all different kinds of molecular interactions, with a variety of time scales and length scales. To address these limitations, we have developed a well-defined model system based on amino acid monomers in so ...
File
File

... DNA into a complementary sequence of mRNA • Requires enzyme, RNA polymerase • Binds to and separates DNA strands • Uses strand of DNA as template to assemble mRNA • RNA polymerase binds to promoters, sequences of DNA that signal where to begin transcription ...
8. DNA,RNA Membranes, Cytoskeleton
8. DNA,RNA Membranes, Cytoskeleton

... • a double stranded helix • two polynucleotide chains that run in opposite directions (anti-parallel) • one purine pairing with its complementary pyrimidine base • the helix is the only shape that accommodates the purinepyrimidine base pair and maintains stable hydrogen bonds ...
Moving Cellular Material
Moving Cellular Material

... 6. What is only used in active transport? 7. How do substances move in active transport? 8. Which proteins are used in active and passive transport? 9. What does a cell do to a substance in endocytosis? 10. What does a cell use to eliminate a substance that is too large to leave by diffusion? 11. Wh ...
Week 5 Assignment 1. Reverse Phase Arrays (RPA) involve printing
Week 5 Assignment 1. Reverse Phase Arrays (RPA) involve printing

... Once a master clone is sequence verified, is it necessary to re-sequence the recombinant expression clone generated through gateway-cloning? ...
1 - contentextra
1 - contentextra

... Optimum temperature maximum rate. ...
CHEM131 Quiz 5_AA
CHEM131 Quiz 5_AA

... b. Circle the acidic R group in the tirpeptide you drew in question part a and draw an arrow pointing out each peptide bond. 4. Answer questions a-c about the Fisher projection of the amino acid shown on the right. (3 pts) a) Briefly explain what is wrong with this Fisher projection. ...
Steps of Translation
Steps of Translation

... 3. The Anticodon on the tRNA pairs with codon 4. The tRNA drops off it’s amino acid 5. An enzyme forms a peptide bond between amino acids 6. This process continues to form a protein until a STOP codon is reached and then the new protein is released. ...
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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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