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Amino Acids and Dipeptides - Chemical Minds
Amino Acids and Dipeptides - Chemical Minds

... ii) Explain your answer in terms of the structure and functional groups present in the amino acids and in the dipeptide(s). ...
Spring 2012 Lecture 5
Spring 2012 Lecture 5

... products and hormones. Amino acids are the building blocks of proteins Proteins are the most abundant macromolecules in living cells. May be 0.1 million different proteins in humans. Play pivotal role in almost every biological process. Generally, proteins composed of the 20 naturally occurring amin ...
Protein Synthesis
Protein Synthesis

... G pairs with C C pairs with G • RNA to protein: every 3 bases code for an amino acid. ...
Page 1 - Biochemistry
Page 1 - Biochemistry

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Water Covalent Bonds Ionic Bonds Non

... Affinity: the tendency of two molecules to bind. (kd is used to quantify how well. Concentration at which interactions occur) Specificity: describes the selectivity of the binding. “Does protein A interact with B, and if yes, does it also interact with C? And how much C is required before it starts ...
Chirality in Chemistry
Chirality in Chemistry

... Examples of secondary structures can be found here. Why does the shape of this secondary structure matter? As enzymes, the biological catalysts which allow our cells to work, are made of proteins, the shape of the secondary structure is important in how they can function. Enzymes work through a “lo ...


... 2. Ho - Van der Waals forces. This is unfavorable for unfolding. Van der Waals interactions are more stable in the native form of the protein. ...
Amino Acid Student Handout 1
Amino Acid Student Handout 1

... watery environment of the cell. Record the amino acid sequence of your primary structure on your lab handout number 15. 3. Now you can begin to fold your 15-amino acid protein according to the chemical properties of its side chains. Remember all of these chemical properties affect the protein at the ...
and y-crystallin X - Prof. N. Srinivasan
and y-crystallin X - Prof. N. Srinivasan

... 0-crystallins, it is extended, whereas in y-crystallins, it takes a sharp turn.As a result, pairsof domains associate intramolecularly to formmonomeric proteins in y-crystallins, whereas in 0B2, the interaction is intermolecular, leading to oligomeric association (Fig. 1). Transplantation of the PB2 ...
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CARBOHYDRATES

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... in sequence? Which type of modifications are those? Change representation to ball and stick to see the side chains. Do the side chains of the modified residues look like they could ...
Slides - Department of Computer Science • NJIT
Slides - Department of Computer Science • NJIT

... • DNA can be represented as strings consisting of four letters: A, C, G, and T. They could be very long, e.g. thousands and even millions of letters • Proteins are also represented as strings of 20 letters (each letter is an amino acid). Their 3-D structure determines the function to a large extent. ...
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... In relation to this assay procedure, which one of the following statements is correct? (A)Of the two enzymes, pyruvate kinase should be in excess. (B)The reaction could be followed by measuring the increase in absorbance at 340 nm. (C)The reaction could be followed by measuring the decrease in absor ...
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...  Proteins are made by linking monomers (amino acids)  ________, _________, _________, ___________ are made mostly of proteins ...
Intragenomic Spread of Plastid-Targeting
Intragenomic Spread of Plastid-Targeting

... identified 105 additional putative plastid-targeted proteins and searched for homologs of their presequences in other regions of the genome. In no other case could homologous presequences be identified in non-homologous proteins, suggesting that this particular presequence is the only one that has e ...
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... 4. What nucleotides are found in RNA? 5. Where in the eukaryotic cell does transcription take place? 6. What are the differences between DNA and RNA (include at least 3 differences)? 7. What are the differences between replication and transcription (include at least 3 differences)? 8. Draw a picture ...
Chemical biology: Chromatin chemistry goes cellular
Chemical biology: Chromatin chemistry goes cellular

... out that they have found a temperature range (67–80 K) where the molecular building blocks have sufficient mobility on the surface to examine many different binding sites, but also note that the cooling rate of the sample is critical in optimizing the ST structures. A cooling rate of only 0.02 K per ...
Option B IB Chemistry Definitions SL
Option B IB Chemistry Definitions SL

... characteristic for each aa – the aa exists as a zwitterion, and will not move (charges balanced). When satisfactory separation is complete, the aa can be sprayed with ninhydrin, and their isoelectric points can be compared. Protein structure, paper chromatography:When a piece of chromatographic pape ...
A Survey of Recent Work on Evolutionary Approaches to the Protein
A Survey of Recent Work on Evolutionary Approaches to the Protein

... structure information from any other protein for comparison. These methods explore an energy hypersurface ( tness landscape) for a minimal energy conformation, which is believed to correspond to the native state. Unfortunately, the enormous size of the energy hypersurface complicates the search proc ...
Chemistry SL HL Assessment Statements 2009 Revised
Chemistry SL HL Assessment Statements 2009 Revised

... The aim of this option is to give students an understanding of the chemistry of important molecules found in the human body, and the need for a balanced and healthy diet. Although the role that these molecules play in the body should be appreciated, the emphasis is placed on their chemistry, and stu ...
Proteins in Beverage: Approaches, Challenges
Proteins in Beverage: Approaches, Challenges

... As demand and acceptance of protein-containing products increases, so too have the various options and sources of protein that are available. Each source, and each form of protein within a particular source, has its own taste attributes, properties, benefits and challenges. This white paper will pro ...
An overview of biochemistry for bioCHEM480
An overview of biochemistry for bioCHEM480

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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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