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Nutrition
Nutrition

... 2) In the liver, the amine group from glutamic acid is removed in the form of ammonia (NH3) and combined with CO2 to form urea a) this process is known as deamination b) the urea is then excreted into the blood where it is filtered out by the kidneys and released in urine c) deaminated amino acids m ...
Document
Document

... 28. Which of the structures cannot exist as shown at any pH in aqueous solution? _________ A. ...
Bio 263/F94/T3 V2 - Millersville University
Bio 263/F94/T3 V2 - Millersville University

... 21. Integrins bind to a specific three amino acid sequence (designated RGD) in a number of proteins. A dish is coated with a protein containing the RGD sequence. Some cultured cells with integrins embedded in their membranes were added to the culture dish along with tripeptides with the RGD sequence ...
Bioinformatics and Functional Genomics, Chapter 8, Part 1
Bioinformatics and Functional Genomics, Chapter 8, Part 1

... Definition of a motif A motif (or fingerprint) is a short, conserved region of a protein. Its size is often 10 to 20 amino acids. Simple motifs include transmembrane domains and phosphorylation sites. These do not imply homology when found in a group of proteins. PROSITE (www.expasy.org/prosite) is ...
Chapter 12: Protein structure, stability and folding
Chapter 12: Protein structure, stability and folding

... books are available which beautifully depict protein structures (e.g., see (2)), including introductory textbooks in Biochemistry. It is not our intention to review all that is known about protein structure, but to highlight what is necessary to appreciate the approaches taken to understand the issu ...
Structure-Function Analysis of Mouse Interferon Alpha Species
Structure-Function Analysis of Mouse Interferon Alpha Species

... inserted into the eukaryotic expression vector pSV328A (Van Heuvel et al., 1986) which contains the origin of replication and early promoter of simian virus 40 (SV40) and the polyadenylation signal of the rabbit fl-globin gene. pSV328A was digested with PstI (partially) and HindlII. The 1.2 kb Hindl ...
Final Exam Revision Answers 2009
Final Exam Revision Answers 2009

... 28. Which of the structures cannot exist as shown at any pH in aqueous solution? A. ...
biochemistry - living environment
biochemistry - living environment

... How to build large molecules  Synthesis (dehydrationsynthesis)-take water out to make something larger ...
The HSSP database of protein structure–sequence
The HSSP database of protein structure–sequence

... vary considerably while maintaining the same overall 3-D structure. One can therefore group sequence-similar proteins into families of structural homologues. If the 3-D structure of only one family member is known, then by implication one can derive the basic 3-D structure, or fold, of all family me ...
Organic Chemistry
Organic Chemistry

... allow them to perform a variety of functions. • In living organisms, they are used for transport, structure, metabolism, communication, and even to detect stimuli such as light. • The protein hemoglobin carries oxygen in your blood, and the protein keratin helps support your skin, hair and nails. ...
18.3 Amino Acids - Haverford Alchemy
18.3 Amino Acids - Haverford Alchemy

Artificial Small-Molecule Peptide Synthesizer
Artificial Small-Molecule Peptide Synthesizer

... • Up to 4 amino acids can be attached in specific sequence to an certain 3-amino-acid peptide chain, with a rate of approximately 12h per amino acid • Although inspiring, the further development of this system faces a lot restrictions and challenges ...
Lab #8
Lab #8

... Under many food processing conditions, reducing sugars produce brown colors that are desirable and important in some foods. Other brown colors obtained upon heating or during longterm storage of foods are undesirable. Common browning of foods on heating or on storage is usually due to a chemical rea ...
Lecture 7 - CS
Lecture 7 - CS

... templates for ~400K prokaryotic proteins) (2) Large scale + metagenomic data (614/1024 -> 137 new folds; templates for ~500K uniprot and 3M metagenomic proteins) ...
The database of epoxide hydrolases and
The database of epoxide hydrolases and

... the α/β hydrolase fold are well conserved. The cap domains are also similar in shape and size, and consist of 4–5 α-helices arranged in 2 layers. The classification of EHs based on the length of NC- and cap-loop (Barth et al., 2004) was applied to 11 homologous families. Cluster I includes soluble m ...
Absorption, transport, storage of metal ions. Biomineralisation A
Absorption, transport, storage of metal ions. Biomineralisation A

... ~ 90-95 % bound to ceruloplasmin. Based on these data ceruloplasmin was considered earlier as the copper transporter, but more recent data point to the role of albumin. Albumin binds copper unusually in an oligopeptide-like manner at the N-terminus. This binding mode has high termodynamic stability ...
Lecture3
Lecture3

... glycine (pKa= 2.43) versus the carboxyl of acetic acid (pKa= 4.76) shows this point. In glycine the positively charged amino group attached to the α-carbon helps to push the departing proton of the carboxyl group out more easily - at the α-amino group the electronegative atoms of oxygens on the carb ...
proteins
proteins

... ■ If you do not have a gene to make a protein, your body cannot make that protein. – Your body has all 20 amino acids necessary to assemble almost any protein that exists. – However, the ribosomes in the cells of your body cannot make a protein unless it has the genetic instructions in its DNA. ■ Fo ...
Document
Document

... developed software which aids identification of horizontally acquired sequences in hope that this approach will enabled us to not only identify new potential virulence factors, but also gain insight into the frequency of horizontal gene transfer within the bacteria, and between the three domains of ...
Separation and analysis of amino acids
Separation and analysis of amino acids

... at all in a given type of protein; others may occur in large numbers. ...
One of the most famous examples
One of the most famous examples

... ENZYMES The ability to bind a specific small molecule is exploited by proteins when they carry out one their main functions: to act as catalysts that bring about chemical transformations of the small molecules they bind. These protein catalysts are called enzymes. Enzymes represent perhaps the singl ...
Lipid modifications of proteins – slipping in and out of membranes
Lipid modifications of proteins – slipping in and out of membranes

... employed by trans-membrane proteins. Lipid modifications facilitate the attachment of soluble proteins to biological membranes, but they also enable protein–protein interactions and, in some cases, the shuttling of proteins between the plasma membrane and the cytosol or other membrane compartments. ...
Amino acid and protein
Amino acid and protein

... Proteins consists of amino acid linked to peptide bond ...
Evolution of the Bacterial Flagellum
Evolution of the Bacterial Flagellum

... same or similar proteins across two-membrane envelopes, showing that these systems overlap structurally and functionally. T3SSs can be encoded on mobile plasmids Variation in Flagellar Structures and pathogenicity islands, both of which can Bacterial flagella are not uniform in construction. They in ...
Antibodies for Unfolded Protein Response
Antibodies for Unfolded Protein Response

... IRE1 alpha, predicted mol. wt. 109.7 kDa, is an ER resident protein which is expressed ubiquitously in all tissue types. It is a single-pass type I membrane protein which localizes to the ER lumen, and interacts with several other proteins, including GRP78, DAB2IP, TRAF2, and TAOK3. Upon UPR activat ...
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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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