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Macromolecular Crystallography in India, IUCr, 2017
Macromolecular Crystallography in India, IUCr, 2017

... 'Chiral  Proofreading'  task,  a  term  they  have  introduced  to  the  biological  text  (5-­‐8).  The  study   provides  deeper  insights  into  how  a  single  DTD  deals  with  the  incredible  challenge  of  being   an   absolute ...
Become Hot Spot Healthy
Become Hot Spot Healthy

... and is often made from GM soy. • Soy milk is slightly less indigestible but may still cause problems, especially if used in excess. • Studies have also shown that soy supplements and processed soy products promote breast tumor growth in laboratory animals. • Soy is one of the top eight allergenic fo ...
Free amino acids and proteins dynamics in somatic embryogenesis
Free amino acids and proteins dynamics in somatic embryogenesis

... development (Sallandrouze et al., 2002). These substances whose levels vary during different stages of development of cell cultures are involved in some transduction signals or are used as substrates or regulators of growth and morphogenesis (Lulsdorf, 1992; Jimenez, 2001). The variations of ionical ...
Chapter 17 (Oct 23, 27, 28)
Chapter 17 (Oct 23, 27, 28)

... CH2 NH3+ -O C CH2 Ionic bond ...
Phospholipids: Membrane Components Steroids: Four Fused Rings
Phospholipids: Membrane Components Steroids: Four Fused Rings

... Metabolism Enzymes bring reactants together and thereby speed chemical reactions in cells. They are specific for one particular type of reaction and can function at body temperature. Support Some proteins have a structural function. For example, keratin makes up hair and nails, while collagen lends ...
Student Exploration: Digestive System
Student Exploration: Digestive System

... Fat molecules can be difficult to break down because large fat droplets do not mix well with water-based enzymes such as lipase. For lipase to work, it helps if the fat is emulsified into tiny droplets. This is done with the help of bile, which is stored in the gallbladder. 5. Observe: Now look at t ...
Amino Acids and Peptides
Amino Acids and Peptides

... Amino acids are the basic structural building units of proteins. They form short polymer chains called peptides or polypeptides which in turn form structures called proteins. The process of such formation from an mRNA template is known as translation, which is part of protein synthesis.  Phenylalan ...
Super secondary structure (Motif)
Super secondary structure (Motif)

... 5. EF hand is two helices connected by a loop that contains residues to coordinate calcium ion (Ca2+) Name refers to the helices E and F in parvalbumin Loop contains 12 amino acids, 5 bind Ca++ ...
Multiple linear regression for protein secondary structure prediction
Multiple linear regression for protein secondary structure prediction

... Here ␣(1,2…19兩␻) is a coefficient vector of 19 amino acids (one left out) for state ␻. Rj is a 19-D vector with the component for residue in position j as 1 and the others as 0 for prediction using single sequence and with aligned compositions of 19 amino acids in position j for prediction using mul ...
The Effects of Whey Supplementation and Natural Diet on Protein
The Effects of Whey Supplementation and Natural Diet on Protein

... depends on a few factors: athletic status of the individual, their weight, intensity of exercise, and the nature of their sport or activity. The FDA suggests that elite endurance athletes consume 1.21.4 g/kg body weight daily to ensure proper muscle rebuilding and structural maintenance of tissues. ...
Detailed proteome analysis of growing cells of the planctomycete
Detailed proteome analysis of growing cells of the planctomycete

... Rhodopirellula baltica SH1T, which was isolated from the water column of the Kieler Bight, a bay in the southwestern Baltic Sea, is a marine aerobic, heterotrophic representative of the ubiquitous bacterial phylum Planctomycetes. We analyzed the R. baltica proteome by applying different preanalytica ...
Ch16b: Peptides
Ch16b: Peptides

... fold over or run straight… ‣ The way a protein string packs on itself 
 with the intramolecular hydrogen bonds 
 is it’s secondary structure. ‣ Secondary structure considers only 
 amide-carbonyl intramolecular hydrogen bonds. ...
Solid state NMR of isotope labelled murine fur: A powerful tool to
Solid state NMR of isotope labelled murine fur: A powerful tool to

Amino acid catabolism I
Amino acid catabolism I

... transdeamination (transamination+GDH) minor patways 2. deamination of other compounds N-containing side chains of nucleotides neurotransmitters 3. ammonia production in the large intestine by bacteria portal vein, direct transport of ammonia. Urea cycle Function: 1. prevents ammonia levels from risi ...
Characterization of Tbc2, a nucleus
Characterization of Tbc2, a nucleus

... quired for the splicing of several plastid group II introns, is related to peptidyl-tRNA hydrolase enzymes (Jenkins and Barkan, 2001). Another splicing factor Raa3, which is involved in the splicing of the first psaA intron of C. reinhardtii, contains a short region of homology with pyridoxamine 5 ...
Make:targeting signals
Make:targeting signals

... MW ~ 17 kDa ...
Enzymes -2.Properties, claasification and theories of action (1)
Enzymes -2.Properties, claasification and theories of action (1)

... • Turnover number is the maximum no: of substrates converted into products/ active site/ unit time • Turn over no: of Carbonic Anhydrase is 36million/active site/minute ...
enzyme - Clayton State University
enzyme - Clayton State University

... • Provides a reaction surface (the active site) • Provides a suitable environment (hydrophobic) • Brings reactants together • Positions reactants correctly for reaction • Weakens bonds in the reactants • Provides acid / base catalysis • Provides nucleophilic groups ...
THIAMINE DEPRIVATION DISTURBS CHOLINERGIC SYSTEM AND OXIDATIVE STRESS IN Original Article
THIAMINE DEPRIVATION DISTURBS CHOLINERGIC SYSTEM AND OXIDATIVE STRESS IN Original Article

... by mammals and thus thiamine can be obtained only from diet [1,2]. It plays a role in the synthesis of AChE, via the synthesis of acetyl CoA. As thiamine plays a role in the synthesis of AChE, it is likely that deficiency of thiamine will lead to alter the level of AChE. BChE has a synergistic relat ...
Full-Text PDF
Full-Text PDF

Isolation, Properties and a Possible Function of a Water
Isolation, Properties and a Possible Function of a Water

... The rapeseed and radish proteins were postulated to function as an inhibitor of proteases since their amino acid sequences contain the signature motif of the Kiinitz family of protease inhibitors (Reviron et al. 1992, Lopez et al. 1994). This possibility could not be examined, however, because the p ...
PROTEOLYSIS is the breakdown of protein to free amino acids
PROTEOLYSIS is the breakdown of protein to free amino acids

... b. Activation of lysosomes increases the rate of intracellular proteolysis. c. Glucocorticoids increase protein degradation in muscle tissue. d. Excessive thyroid hormones increase protein turnover. e. Insulin reduces proteolysis and increases protein synthesis. 2. Purpose a. Abnormal, defective, an ...
The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase
The Crystal Structure of Arabidopsis thaliana Allene Oxide Cyclase

... 12,13(S)-epoxylinolenic acid but not 12,13(S)-epoxylinoleic acid as a substrate (Ziegler et al., 1999). This is in contrast with AOS, which produces both allene oxides from the respective 13(S)hydroperoxy fatty acids (18:3 and 18:2, respectively). It thus appears that AOC confers additional specific ...
Chapter 9 – Catalytic Strategies (So we`ve talked about enzymes
Chapter 9 – Catalytic Strategies (So we`ve talked about enzymes

... - Involved in the degradation of flesh iv. Protease Inh used as drugs (As you can imagine, proteases shut down a very important property of cells, that is the ability for cell to break down proteins whether it be a wide range of proteins like in ones gut for digestion, or specific protein like in th ...
Protein Interactions Techniques and Challenges
Protein Interactions Techniques and Challenges

... Tertiary Structure Quaternary Structure ...
< 1 ... 195 196 197 198 199 200 201 202 203 ... 656 >

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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