Cellular Metabolism and Nutrition notes
... Enzyme Catalysis • Speed of the enzyme action depends on the concentration of the enzyme and substrate. – As enzyme concentration increases, enzyme activity will increase to a point. – As substrate concentration increases, enzyme activity will increase to a point. ...
... Enzyme Catalysis • Speed of the enzyme action depends on the concentration of the enzyme and substrate. – As enzyme concentration increases, enzyme activity will increase to a point. – As substrate concentration increases, enzyme activity will increase to a point. ...
DESI - plaza
... Advantages of DESI Ambient condition Large range of molecules from small to proteins Sample can be moved in space during analysis (Imaging) No need for Matrix unlike MALDI Multiple charge ions is an advantage to extend mass range (proteins) Variable distance and angel allows different energy ...
... Advantages of DESI Ambient condition Large range of molecules from small to proteins Sample can be moved in space during analysis (Imaging) No need for Matrix unlike MALDI Multiple charge ions is an advantage to extend mass range (proteins) Variable distance and angel allows different energy ...
3-D STRUCTURE PREDICTION OF AQUAPORIN-2, VIRTUAL SCREENING AND IN-SILICO
... water channel protein or water channel aquaporin-2 or more. The antidiuretic hormone Vasopressin secreted by the pituitary gland regulate the expression of this aquaporin 2 protein. Upon vasopressin stimulation, AQP2 translocate from sub apical storage vesicles to the apical plasma membrane, renderi ...
... water channel protein or water channel aquaporin-2 or more. The antidiuretic hormone Vasopressin secreted by the pituitary gland regulate the expression of this aquaporin 2 protein. Upon vasopressin stimulation, AQP2 translocate from sub apical storage vesicles to the apical plasma membrane, renderi ...
Some application of d block metal in biology
... The main biological functions of lipids include energy storage, acting as structural components of cell membranes, and participating as important signaling molecules. ...
... The main biological functions of lipids include energy storage, acting as structural components of cell membranes, and participating as important signaling molecules. ...
Basic Principle in Plant Physiology
... •NAD+, FAD, and Coenzyme A are formed from ATP. •Disruptions in nucleotide metabolism can cause pathological conditions. ...
... •NAD+, FAD, and Coenzyme A are formed from ATP. •Disruptions in nucleotide metabolism can cause pathological conditions. ...
The K-Segment of Maize DHN1 Mediates Binding
... S-segment (a tract of Ser residues), and the f-segment (Close, 1996). Because of high hydrophilicity, high content of Gly (.20%), and the lack of a defined threedimensional structure in the pure form (Lisse et al., 1996), DHNs have been categorized as “intrinsically disordered/unstructured proteins” ...
... S-segment (a tract of Ser residues), and the f-segment (Close, 1996). Because of high hydrophilicity, high content of Gly (.20%), and the lack of a defined threedimensional structure in the pure form (Lisse et al., 1996), DHNs have been categorized as “intrinsically disordered/unstructured proteins” ...
Mechanisms of mitochondrial protein import
... Mitochondria are the organelles that mediate respiration and ATP synthesis in eukaryotic cells. They also participate in numerous indispensable metabolic pathways (e.g. synthesis of haem, nucleotides, lipids and amino acids) and they mediate intracellular homoeostasis of inorganic ions. Mitochondria ...
... Mitochondria are the organelles that mediate respiration and ATP synthesis in eukaryotic cells. They also participate in numerous indispensable metabolic pathways (e.g. synthesis of haem, nucleotides, lipids and amino acids) and they mediate intracellular homoeostasis of inorganic ions. Mitochondria ...
BE.342/442 Tuesday, October 25, 2005 Topic: Biomineralization
... Dentinogenesis involves a stacked structure containing: a cell-rich zone, a cell-free zone, and an osteoblast layer. The odontoblasts manufacture predentin, which mineralizes into teritubules of dentin. The odontoblast process fills the tubules of predentin produced by odontoblasts, and has relative ...
... Dentinogenesis involves a stacked structure containing: a cell-rich zone, a cell-free zone, and an osteoblast layer. The odontoblasts manufacture predentin, which mineralizes into teritubules of dentin. The odontoblast process fills the tubules of predentin produced by odontoblasts, and has relative ...
Biochemistry Biochemistry is the science concerned the chemical
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
Biochemistry Biochemistry is the science concerned the chemical
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
Biochemistry Biochemistry is the science concerned the chemical
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
... properties of amino acids, zwitterions. The structure of some modified amino acids (as selenocysteine, 4-hydroxyproline, 5-hydroxylysine). The structure of some physiologically important nonprotein amino acids. The formation, structure and properties of the peptide bond. Some important peptides in t ...
Proteins and Albumin
... respectively. Amino acid chains containing more than a dozen or so residues are often referred to as oligopeptides (from the Greek oligos, meaning “few”). Proteins are typically defined as polypeptides with a molecular weight of greater than 5000 Daltons (ie, > 5 kDa). Proteins adopt stable conforma ...
... respectively. Amino acid chains containing more than a dozen or so residues are often referred to as oligopeptides (from the Greek oligos, meaning “few”). Proteins are typically defined as polypeptides with a molecular weight of greater than 5000 Daltons (ie, > 5 kDa). Proteins adopt stable conforma ...
Differentially Expressed Proteins in Sugarcane Leaves
... to identify proteins that were differentially expressed in sugarcane leaves in response to a water deficit treatment to describe the sugarcane responses at the cellular and molecular levels. Drought-tolerant sugarcane cultivar Khon Kaen 3 stalk cuttings were grown under a controlled environment in a ...
... to identify proteins that were differentially expressed in sugarcane leaves in response to a water deficit treatment to describe the sugarcane responses at the cellular and molecular levels. Drought-tolerant sugarcane cultivar Khon Kaen 3 stalk cuttings were grown under a controlled environment in a ...
Document
... and van der Waals forces between tightly packed aliphatic side chains inside peptide. ...
... and van der Waals forces between tightly packed aliphatic side chains inside peptide. ...
Extinction Coefficients - Thermo Fisher Scientific
... the concentration of a purified sample. Amino acids containing aromatic side chains (i.e., tyrosine, tryptophan and phenylalanine) exhibit strong UV-light absorption. Consequently, proteins and peptides absorb UV-light in proportion to their aromatic amino acid content and total concentration. Once ...
... the concentration of a purified sample. Amino acids containing aromatic side chains (i.e., tyrosine, tryptophan and phenylalanine) exhibit strong UV-light absorption. Consequently, proteins and peptides absorb UV-light in proportion to their aromatic amino acid content and total concentration. Once ...
mnw2yr_lec16_2004
... collecting the N- and C- termini of local alignments we can identify domain boundaries. By finding domains we can significantly improve database search methods SnapDRAGON is more sensitive than DOMAINATION but at high computational cost ...
... collecting the N- and C- termini of local alignments we can identify domain boundaries. By finding domains we can significantly improve database search methods SnapDRAGON is more sensitive than DOMAINATION but at high computational cost ...
Exam questions used in the past
... 10. Mention two types of mutations (i.e. Phe -> Asp or Trp -> Ala) that generally make proteins more stable (perhaps this question can only be answered in two weeks...) ...
... 10. Mention two types of mutations (i.e. Phe -> Asp or Trp -> Ala) that generally make proteins more stable (perhaps this question can only be answered in two weeks...) ...
Unique Protein Reporter Assays: Green Fluorescent Proteins (GFP
... Single and Dual Luciferase assays, using Purple Cypridina, Blue Gaussia, Green Renilla and Red Firefly Luciferases The Gaussia, Gaussia-Dura (a mutant form of the Gaussia luciferase gene that confers better bioluminescent signal stability than native luciferase) and Cypridina luciferase proteins ar ...
... Single and Dual Luciferase assays, using Purple Cypridina, Blue Gaussia, Green Renilla and Red Firefly Luciferases The Gaussia, Gaussia-Dura (a mutant form of the Gaussia luciferase gene that confers better bioluminescent signal stability than native luciferase) and Cypridina luciferase proteins ar ...
handout nucleic acids and DNA replication
... in proteins. The precise number and sequence of amino acids makes up the primary structure of a polypeptide chain. A functional protein may consist of a single, or several polypeptide chains. DNA must therefore carry a coded message that determines not only the number and types of amino acids that a ...
... in proteins. The precise number and sequence of amino acids makes up the primary structure of a polypeptide chain. A functional protein may consist of a single, or several polypeptide chains. DNA must therefore carry a coded message that determines not only the number and types of amino acids that a ...
Pathways of Pyrimidine and Purine Metabolism in E.coli
... Because mammals lack these enzymes, a better understanding of these molecules may make them attractive targets for drug therapy. This study attempted to characterize the active site of the inosine-uridine hydrolase of E. coli, encoded by rihC. Methods: Specific amino acid residues of the rihC gene o ...
... Because mammals lack these enzymes, a better understanding of these molecules may make them attractive targets for drug therapy. This study attempted to characterize the active site of the inosine-uridine hydrolase of E. coli, encoded by rihC. Methods: Specific amino acid residues of the rihC gene o ...
Lab Session 9
... What if not using a stacking gel? • In the absence of a stacking gel, your sample would sit on top of the running gel, as a band of up to 1cm deep. • Rather than being lined up together and hitting the running gel together, the proteins in the sample would all enter the running gel at different tim ...
... What if not using a stacking gel? • In the absence of a stacking gel, your sample would sit on top of the running gel, as a band of up to 1cm deep. • Rather than being lined up together and hitting the running gel together, the proteins in the sample would all enter the running gel at different tim ...
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.