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Class Notes
Class Notes

... Many eukaryotic genes code for a set of closely related polypeptides in a process called alternative splicing. ...
A New Method to Detect Related Function Among Proteins
A New Method to Detect Related Function Among Proteins

... function is not necessarily confined to a particular fold and it is often enough not apparent at the sequence level.13 Protein function, in particular of enzymes, is often intimately connected with the recognition and chemical modification of endogenous ligands such as agonists, antagonists, effecto ...
Erlanson et al. PNAS - UCSF Macromolecular Structure Group
Erlanson et al. PNAS - UCSF Macromolecular Structure Group

... most are problematic because moderate affinity leads are difficult to obtain. Identifying and subsequently optimizing weaker binding compounds would improve the success rate, but screening at high concentrations is generally impractical because of compound insolubility and assay artifacts. Moreover, ...
CHAPTER 17 FROM GENE TO PROTEIN
CHAPTER 17 FROM GENE TO PROTEIN

... Many eukaryotic genes code for a set of closely related polypeptides in a process called alternative splicing. ...
Transient intracellular expression of chicken UCH-L3 and
Transient intracellular expression of chicken UCH-L3 and

... profile of DUBs affected by this DUB inhibitor. Anti-UCH-L5 western blotting was done to show how activity of UCH-L5 was affected by b-AP15, while anti-β actin western blot is a loading control. The inactive UCH-L5 has not been detected. The b-AP15 compound inhibited UCH-L5 even at the lower concent ...
LP - Columbia University
LP - Columbia University

... Note the central carbon atom, to which 4 different groups are attached: an amino group (drawn by convention at the left), a carboxylic acid group (put at the right side), a hydrogen, and a side chain, or R-group.  Only the R-group varies among the 20 different amino acids. This is the side chain, an ...
Relationships between amino acid sequence and backbone torsion
Relationships between amino acid sequence and backbone torsion

... Short-range interactions along with the long-range ones are responsible for the stabilization of the native structures in globular proteins. Short-range, or local, interactions refer to those taking place between near-neighbor amino acids along the main-chain. They result from both steric exclusions ...
Molecular Plant Microbe Interactions
Molecular Plant Microbe Interactions

... (Marger and Saier 1993; Paulsen and Skurray 1993) and it was suggested that the conserved sequence may be involved in common functions, such as proton translocation, while specialized functions, such as substrate binding, are encoded by the C-terminal regions (Rouch et al. 1990). The drug extrusion ...
Protein Structure Prediction
Protein Structure Prediction

... AlphaPred: A web server for prediction of -turns in proteins (http://www.imtech.res.in/raghava/alphapred/) Harpreet Kaur and G P S Raghava (2003) Prediction of -turns in proteins using PSI-BLAST profiles and secondary structure information. Proteins . ...
Kinesin
Kinesin

...  8 nm per step (spacing of tubulin dimers along the microtubule)  = 250 steps/second!  Protein head = 7.5 X 4.5 X 4.5 nm  ≈ speed and thrust of the supersonic car  60% efficiency ...
Protein oxidation and cellular homeostasis: Emphasis
Protein oxidation and cellular homeostasis: Emphasis

... singlet oxygen (1O2) and hydrogen peroxide (H2O2) [1]. Each of these ROS is highly reactive and unstable due to the fact that they contain an unpaired electron in their outer electron shell. This conformation promotes their ability to rapidly interact with cellular macromolecules such as proteins, l ...
Troponin-I Mouse Skeletal Muscle
Troponin-I Mouse Skeletal Muscle

... present for, and remain elevated, a long time Unlike CK and CK-MB, cTnT and cTnI are released for much longer with cTnI detectable in the blood for up to 5 days and cTnT for 7-10 days following MI. This allows an MI to be detected if the patient presents late. Troponin T and I are very sensitive. Th ...
4.Lect Carbon skeleton intro
4.Lect Carbon skeleton intro

... synthesize glucose and are termed glucogenic. while some are converted to acetylCoA (ketogenic amino acids) these CANNOT be used to synthesize glucose. Ketogenic amino acids can be converted to fatty acids for storage as triglyceride and later oxidation (fed state), or to ketone bodies (made in live ...
Allied Biochemistry II - E
Allied Biochemistry II - E

... 4. The components of respiratory chain are arranged in the order of (a) increasing redox potential (b) decreasing redox potential (c) independent of redox potential (d) none of the above 5. The common metabolite of carbohydrate, protein and lipid metabolism (a) acetyl CoA (b) pyruvate (c) fumarate ...
Ribosome - Mrs. J. Malito
Ribosome - Mrs. J. Malito

... strands rejoin and wind back up. ...
A Few Axonal Proteins Distinguish Ventral Spinal Cord Neurons
A Few Axonal Proteins Distinguish Ventral Spinal Cord Neurons

... only those plates without bulk flow between the compartments are used for experiments . However, even in plates where no bulk flow of medium between the compartments occurred, contamination of the axonal proteins might result from the migration ofheavily labeled non-neuronal cells from the center co ...
Lecture 12
Lecture 12

... Ribosomes are large complexes of protein and ribosomal RNA . They consist of two subunits—one large and one small—whose relative sizes are generally given in terms of their sedimentation coefficients, or S (Svedberg) values. The prokaryotic 50S and 30S ribosomal subunits together form a 70S ribosome ...
brochure  - Your Bakery and Snack Solutions
brochure - Your Bakery and Snack Solutions

... At Tate & Lyle Oat Ingredients in Sweden we extract the protein component of the oat bran using a patented process without the use of solvents – so that the protein can be used as an individual ingredient in its own right. Oat protein is rich in essential amino acids (including leucine, isoleucine a ...
ATF4 helps mitochondria pass the stress test
ATF4 helps mitochondria pass the stress test

... mitochondrial stressors, the levels of these amino acids were increased, as were several other key metabolites, such as ceramide and certain phospholipids, that are synthesized from serine. Many of the genes induced by mitochondrial stress contained a binding site for the transcription factor ATF4. ...
Full-text PDF
Full-text PDF

... and serine (1.77). Common feature of these amino acids is that they are hydrophilic and contain highly electronegative atoms located in the outermost region of their side chains. On the other hand, tryptophan showed the lowest propensity to interact with RNA (P = 0.11), followed by valine (0.12) and ...
Functional Control by Codon Bias in Magnetic Bacteria
Functional Control by Codon Bias in Magnetic Bacteria

... similar blast searches for Iron Regulatory Proteins (IRPs: IRP1 and IRP2) from mammalian18–20 as well as bacterial sources (in bacteria, IRP1 is called aconitase) in the magnetic bacterial genome. The logic behind these searches was that if IRPs are present in magnetic bacteria, then one would expec ...
Slide 1
Slide 1

... – The correct amino acid sequence is determined by the cell’s genetic information. – The slightest change in this sequence may affect the protein’s ability to function. ...
EnCor Biotechnology Inc
EnCor Biotechnology Inc

... The Immunogen: Fox3 is one of a family of mammalian homologues of Fox-1, which was originally discovered in C. elegans as a gene involved in sex determination. Fox is an acronym of "Feminizing locus on X". The mammalian genome contains three genes homologous to C. elegans Fox-1, called Fox1, Fox2 an ...
Predicted function of the vaccinia virus G5R protein
Predicted function of the vaccinia virus G5R protein

... acids are believed to comprise the active site of hFEN-1, seven of which are negatively charged and coordinate the binding of two divalent cations, two that are positively charged and are thought to contribute to the nucleophilic attack that breaks the phosphate backbone of the substrate DNA and one ...
Gift of Protein Activity
Gift of Protein Activity

... Name:_________________________ Period:____ Date:_______________ ...
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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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