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Plasma proteins
Plasma proteins

... • Transport Iron • 2.2- 4 g/L • Synthesized in liver but affected by iron concentration in the blood • Low level leads to rise in transferrin level • Raised in anemia ...
Give a brief account of drug protein binding and outline its
Give a brief account of drug protein binding and outline its

... General: Drug protein binding refers to the interaction a drug has with proteins. - Can be intravascular, interstitial, or intracellular proteins o Plasma proteins binding is most significant - Interaction is usually reversible - Ionic or electrostatic - Obeys the law of mass action [drug] + [protei ...
FlexWeb
FlexWeb

... Proteins • The ability of proteins to change their conformation is important to their function as biological machines. ...
Essential Cell Biology
Essential Cell Biology

... • Secretory Proteins Are Released from the Cell by Exocytosis ...
PROJECT PROPOSAL for applicants for ITC fellowships
PROJECT PROPOSAL for applicants for ITC fellowships

... phosphatases has been linked to various cellular processes, including DNA repair and cell division. Not surprisingly, the dysfunction of these enzymes has already been associated with the progression of human diseases, including cancer. They all function as a heterotrimeric complex consisting of one ...
Proteins - Cook Biology
Proteins - Cook Biology

... Proteins have many structures, resulting in a wide range of functions • Proteins account for more than 50% of the dry mass of most cells. • Protein functions include structural support, storage, transport, cellular communications, movement, defense against foreign substances, and organic catalysts ...
Lecture 5
Lecture 5

... easily make the sharp turns and bends needed in a b-turn. Proline is special because it is so rigid; you could say that it is pre-bend for the b-turn. Aspartic acid, asparagine, and serine have in common that they have short side chains that can form hydrogen bonds with the own backbone. These hydro ...
Biological membranes, cell compartments
Biological membranes, cell compartments

... • DNA replication • Transcription, synthesis of mRNA, tRNA, rRNA, ribosomes • Surrounded by double membrane connected to ER • Transport of cytosolic compounds (active and passive) only via nuclear pores • Specialized subcompartments (nucleolus – ribosomes formation, DNA replication is localized etc. ...
bchm628_lect5_15
bchm628_lect5_15

... matches to other domains.  Increased size of protein databases  Number related sequences rises and less related ...
Biology 12 – Lesson 3 - Biological Molecules 1 http://nhscience
Biology 12 – Lesson 3 - Biological Molecules 1 http://nhscience

...  The single most important molecule in our steroid chemistry is cholesterol  We ingest cholesterol in animal products such as eggs, meat, and cheese, and our liver produces a certain amount  Main Functions of Cholesterol: 1. Cholesterol is a key component to plasma membranes in animal cells - pla ...
Plasma Membrane
Plasma Membrane

... the membrane and act as pathways for ions and molecules. Some of the ion movement may not require work (passive transport), but other processes require lot of energy and pumping action (active transport). When you look at the whole membrane, there are very few integral proteins when compared to the ...
Leukaemia Section t(1;9)(p34;q34)  Atlas of Genetics and Cytogenetics
Leukaemia Section t(1;9)(p34;q34) Atlas of Genetics and Cytogenetics

... and the coiled-coil domain (dimerization domain), fused to the SH2 domain of ABL1; the fusion protein also includes the SH1 domain (tyrosine kinase activity), the nuclear localization domain, and the actin binding domain of ABL1. ...
BB 450/550 Exam 1 - Oregon State University
BB 450/550 Exam 1 - Oregon State University

... 2. Name and describe the structure of proteins that gives rise to alpha-helices, folding, and subunit interactions. 3. What are the primary forces stabilizing alpha helices? 4. Using a diagram, clearly illustrate the arrangement of hydrophobic and hydrophilic amino acids in a membrane protein like p ...
Cell signalling
Cell signalling

Gene Section LASP1 (LIM and SH3 protein) Atlas of Genetics and Cytogenetics
Gene Section LASP1 (LIM and SH3 protein) Atlas of Genetics and Cytogenetics

... to those in LASP1 are also present in other nebulinrelated proteins such as NEBL (nebulette, 107 kD actin-binding Z-disk protein) and NRAP (nebulinrelated anchoring protein); NRAP also contains an Nterminal LIM domain and NEB (nebulin) a C-terminal SH3 domain, both of which are highly homologous to ...
biological process
biological process

... 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 a dictionary of motifs (there are currently 1600 entries). In PROSITE, a pattern is a qualitative motif description (a protein eit ...
PPT File
PPT File

... common structural patterns 1. The three-dimensional structure of a typical globular protein can be considered an assemblage of polypeptide segments in the a-helix and b-sheet conformations. 2. Supersecondary structures: motifs, folds Stable arrangements of several elements of secondary structure and ...
Chapter 5 Notes Bio AP
Chapter 5 Notes Bio AP

... ○ When a bond forms between two monomers, each monomer contributes part of the water molecule that is lost. One monomer provides a hydroxyl group (—OH), while the other provides a ...
Additional file 1, Table S1. Summary of yeast two
Additional file 1, Table S1. Summary of yeast two

... Oryzias latipes, Gg: Gallus gallus, Hs: Homo sapiens, Xt: Xenopus tropicalis). Protein domains are color-coded: green: basic domain, purple: HLH domain, orange: orange domain. Note the signature of the Hes6-like subfamily: the loops of Her13 and Hes6 contain 5 less amino acids when compared with oth ...
Amino Acid Metabolism
Amino Acid Metabolism

... Metabolic Pool of Amino Acids • Metabolic pool AA has no storage form in mammals (as with other life forms) as free AA or as specialized storage form (such as glycogen for glucose, TG for FA) but a certain percentage of muscle & structural proteins are “expendable”. • AA are used for proteins, N co ...
1 Amino Acid Metabolism
1 Amino Acid Metabolism

... Metabolic Pool of Amino Acids • Metabolic pool AA has no storage form in mammals (as with other life forms) as free AA or as specialized storage form (such as glycogen for glucose, TG for FA) but a certain percentage of muscle & structural proteins are “expendable”. • AA are used for proteins, N co ...
Protein Synthesis
Protein Synthesis

... 1. Your instructor will assign you a sequence of 63 nucleotides forming 21 DNA code words. Beginning at the left and proceeding to the right, transcribe (by writing the sequence on paper) the DNA code words into mRNA codons using the following key to transcription:  A (adenine) in DNA transcribes t ...
Biological Membranes and Transport
Biological Membranes and Transport

... Structure of Integral membrane proteins X-ray crystallography - very difficult Hydropathy plot - easier if know amino acid sequence of protein An α-helical sequence of 20-25 amino acids is just long enough to span the thickness (30 A) of the lipid bilayer (length of an α helix is 1.5 A per amino aci ...
Do Now: Wednesday, March 19
Do Now: Wednesday, March 19

... for the protein that is needed is unwound  Step 2: RNA polymerase (enzyme) uses the DNA to make a complementary strand of mRNA ...
Membranes and transport - part 1
Membranes and transport - part 1

... Biological Membranes and Transport Structure of Integral membrane proteins X-ray crystallography - very difficult Hydropathy plot - easier if know amino acid sequence of protein An -helical sequence of 20-25 amino acids is just long enough to span the thickness (30 A) of the lipid bilayer (length ...
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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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