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Cell Signaling Mechanisms
Cell Signaling Mechanisms

... Cell Signaling: Responding to the outside world  Cells interact with their environment by interpreting extracellular signals via proteins that span their plasma membrane called receptors  Receptors are comprised of extracellular and intracellular domains  The extracellular domain relays informati ...
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... electrons  in  the  conjoining  covalent  bond.  These  partially  charged  atoms  can  form  weak,   non-­‐covalent  attractions  that  hold  the  two  atoms  near  one  another  in  physical  space.  If   the  weak,  non-­‐covalent  attra ...
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... Secondary Structure of Proteins • The polypeptide backbone forms regular arrangements of amino acids that are located near to each other in the linear sequence. • These arrangements are termed the secondary structure of the polypeptide . • The α-helix, β-sheet , and β-bend are examples o f secondar ...
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... β – sheets and random loops form the basis of the active site in enzymes Tertiary structure Hydrophilic R groups attract other hydrophilic R groups according to the ‘like attracts like’ rule This interaction causes the polypeptide chain to fold, coil or twist into the proteins functional shape or co ...
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BNFO 602 Lecture 1 - New Jersey Institute of Technology
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Freeman 1e: How we got there

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... Email: [email protected] Web: www.signagenlabs.com ...
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Protein Synthesis Test Review
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... Assessment Practice - This DOES NOT cover all the material you may be tested on. You need to review all your notes, homework assignments, quizzes, and classwork. 1. Fill in the chart below using the information you know about the six most abundant elements in the human body: ...
Transport and local translational regulation of mRNAs in neurons
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... LTD and produces ataxic mice. Contrasting the differences between FMRP loss and CPEB dysfunction in Purkinje neurons will highlight the differences between these two mechanisms for dendritic mRNA translation. Bassell will discuss the role of FMRP in activity-dependent mRNA transport and synaptic pro ...
macromolecules notes
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... b. Some side chains are polar (examples: glycine, alanine, serine, tyrosine) c. Some side chains are nonpolar (examples: proline, tryptophan, valine) d. Some side chains are acidic (examples: aspartic acid, glutamine acid) e. Some side chains are basic (examples: lysine, histidine) ...
Protein Synthesis
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... the binding of the enzyme to the transition state with 1 H bond. Label this curve (b). to the transition state ...
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... activated trypsin which may find its way into the ducts, by forming a complex with it Enzyme Y is also exhibiting a protective function, which is activated by traces of active trypsin degrades zymogen The alkaline pH (8.0-9.5) and low Ca2+ concentration in pancreatic secretions promote the degradati ...
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... A few chemical groups are key to the functioning of biological molecules An organic compound has unique properties that depend upon the size and shape of the molecule and groups of atoms (functional groups) attached to it. A functional group affects a biological molecule’s function in a characterist ...
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Protein Synthesis

Do Now: - South Orange
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... mRNA is transcribed Ribosome positions start codon to bind to anti-codon on tRNA Ribosome moves along mRNA, binding new tRNA and aa’s. Peptide bond binds aa’s as the chain builds and tRNA’s move along the chain Process continues until there is a stop codon in mRNA ...
m5zn_14bea598b5b7901
m5zn_14bea598b5b7901

... present in the DNA. Any defect in the genetic code leads to abnormal proteins. Eg: sickle cell anemia. • The amino acids are joined covalently by peptide bonds, which are amide linkage between the α carboxyl group of one amino acid, and α amino group of another by removing one molecule of water. ...
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Proteolysis



Proteolysis is the breakdown of proteins into smaller polypeptides or amino acids. Uncatalysed, the hydrolysis of peptide bonds is extremely slow, taking hundreds of years. Proteolysis is typically catalysed by cellular enzymes called proteases, but may also occur by intra-molecular digestion. Low pH or high temperatures can also cause proteolysis non-enzymatically.Proteolysis in organisms serves many purposes; for example, digestive enzymes break down proteins in food to provide amino acids for the organism, while proteolytic processing of a polypeptide chain after its synthesis may be necessary for the production of an active protein. It is also important in the regulation of some physiological and cellular processes, as well as preventing the accumulation of unwanted or abnormal proteins in cells. Consequently, dis-regulation of proteolysis can cause diseases, and is used in some venoms to damage their prey.Proteolysis is important as an analytical tool for studying proteins in the laboratory, as well as industrially, for example in food processing and stain removal.
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