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Translation PPT
Translation PPT

... While RNA is single-stranded, it does not “combine” to make double-stranded DNA.DNA and RNA are two entirely different molecules. RNA contains ribose sugar while DNA contains deoxyribose, and RNA contains uracil (U) instead of thymine (T). ...
Station A 1. Why are polar water molecules attracted to other polar
Station A 1. Why are polar water molecules attracted to other polar

... 1. Where does an allosteric inhibitor bind onto an enzyme, and how does it affect enzyme function? ...
RNA-Unit 6 cont.
RNA-Unit 6 cont.

... with ribosome structure; function not entirely understood ...
BiochemLecture03
BiochemLecture03

... acids with respect to the conforomations that the backbone can adopt. For this reason, it is not surprising to see Alanine present in just about all non-critical protein contexts. • Role in function: The Alanine side chain is very nonreactive, and is thus rarely directly involved in protein function ...
Lecture 27
Lecture 27

... PLP can therefore be used in both transamination and decarboxylation reactions. Most aminotransferases accept only -ketoglutarate or oxaloacetate as the -keto acid substrate in the second stage of the reaction (reverse reaction). The amino groups of most amino acids are therefore incorporated in t ...
Protein
Protein

...  Globular proteins  Compact, spherical proteins with tertiary and quaternary structures  Examples: antibodies, peptide-hormones, and enzymes ...
THE MOLECULES OF LIFE
THE MOLECULES OF LIFE

...  Protein catalysts that speed up a chemical reaction  Lower the activation energy needed to start a reaction  Each enzyme only catalyzes one reaction  How enzymes work: o Substrate binds to enzyme’s active site like lock and key o In active site, substrate is converted to product o Product leave ...
MOLECULES OF LIFE
MOLECULES OF LIFE

... A. Structure  Long chains of nucleotides linked via dehydration reactions ...
Chemistry 202 Amino Acids, Peptides, and
Chemistry 202 Amino Acids, Peptides, and

... and would be named seryl-alanyl-glycine (Ser-Ala-Gly). It is clear that when 100 or more amino acids are involved and each of these may have one of 20 different structures, the number of possible proteins is huge. Some commonly occurring peptides are antibiotics, hormones, and enzymes. Besides many ...
ENGINEERING PROTEINS
ENGINEERING PROTEINS

... Ester –COOR, Acyl chloride –COCl, Amide -CONH2 Acid anhydride -(CO)2O The region in an enzyme into which the substrate binds before it reacts with it. An organic molecule that contains both an –NH2 group and a –COOH group Pairs of bases that fit neatly together thus placing groups in just the right ...
Translation Notes
Translation Notes

... between the amino acids while breaking the bond between the previous amino acid and its tRNA. The ribosome pulls the mRNA strand the length of one codon. The first tRNA exits the ribosome, and another codon is exposed. ...
Chapter 4 - Open Yale Courses
Chapter 4 - Open Yale Courses

... • There are four levels of structure for proteins. The amino acid sequence is the primary structure, the local domains are the secondary structure, the overall three-dimensional shape is the tertiary structure, and the formation of a complex with other polypeptide chains is the quaternary structure. ...
Bio572: Amino acids and proteins
Bio572: Amino acids and proteins

... This is also shown as a projection below (from Tulane Univ.). The R groups are attached to the alpha carbon, and alternate being projected out of the screen and into the screen. One important concept is that the carboxyl carbon is planar, due to the partial double-bond character of the amide group. ...
Name
Name

... 13. Find the cards with an amino group and a carboxyl group. How many amino acids do you have in your set? ________________ 14. Which of the CHNOP elements are contained in ALL amino acids?___________ There should be 9 other cards left over in your “nitrogen” pile. Set these aside, we will come back ...
4.Lect Carbon skeleton intro
4.Lect Carbon skeleton intro

... Accounts for ~ 10% of energy requirement of adults Degradation exceeds demand for new protein When: There is excess protein in diet (amino acids are not stored) and also during starvation when carbohydrates are not available. ...
Biochemistry 462a - Proteins Extra Questions
Biochemistry 462a - Proteins Extra Questions

... zero. The two structures shown for Ala each have a net charge of zero. (A) Why is the predominant form of Ala at its isoelectric point the zwitterionic and not the uncharged form? (B) Calculate the ratio of the concentration of the zwitterionic form/uncharged form at the pI. 7. Explain the following ...
Inborn Errors of Amino Acid Metabolism
Inborn Errors of Amino Acid Metabolism

...  Prenatal diagnosis is done by detecting gene mutation in fetus  Neonatal diagnosis in infants is done by measuring blood phe levels  Treatment: Life long phe-restricted diet (low)  If a pregnant mother is affected, the fetus is affected but the opposite will not affect the mother because the ...
File
File

...  The ribosome reads mRNA three bases at a time.  Three nitrogen bases (called a codon or a triplet; EX ...
Proteins
Proteins

...  The ribosome reads mRNA three bases at a time.  Three nitrogen bases (called a codon or a triplet; EX ...
Proteins and Enzymes (p
Proteins and Enzymes (p

... shape. Examples are collagen, which plays a role in the connective tissue of humans and actin. Globular proteins are more three dimensional in their shape. Examples are haemoglobin and insulin. Use the worksheet to add to these notes, as to the differences ...
File
File

... Hemoglobin in red blood cells acts as a buffer by preventing a drop in pH of the blood. It is a tertiary protein that bonds to iron, which gives it its red hue when carrying oxygen. ...
Slide 1
Slide 1

...  Cofactors and Enzyme Function  Cofactor  An ion or molecule that binds to an enzyme before substrates can bind ...
structure of organic molecules
structure of organic molecules

... central carbon atom bonded to a single hydrogen atom and three characteristic “groups.” Reexamine the glycine and alanine molecules shown below. a. An amino group (NH2) is found in every amino acid. Put a square around the amino group (NH2) in glycine and alanine. b. A carboxylic acid group (COOH) i ...
Chapter 3
Chapter 3

... – Functional units within a larger structure – Most proteins made of multiple domains that perform different parts of the protein’s function ...
Macromoleucles Notes
Macromoleucles Notes

< 1 ... 558 559 560 561 562 563 564 565 566 ... 622 >

Amino acid synthesis

Amino acid synthesis is the set of biochemical processes (metabolic pathways) by which the various amino acids are produced from other compounds. The substrates for these processes are various compounds in the organism's diet or growth media. Not all organisms are able to synthesise all amino acids. Humans are excellent example of this, since humans can only synthesise 11 of the 20 standard amino acids (aka non-essential amino acid), and in time of accelerated growth, arginine, can be considered an essential amino acid.A fundamental problem for biological systems is to obtain nitrogen in an easily usable form. This problem is solved by certain microorganisms capable of reducing the inert N≡N molecule (nitrogen gas) to two molecules of ammonia in one of the most remarkable reactions in biochemistry. Ammonia is the source of nitrogen for all the amino acids. The carbon backbones come from the glycolytic pathway, the pentose phosphate pathway, or the citric acid cycle.In amino acid production, one encounters an important problem in biosynthesis, namely stereochemical control. Because all amino acids except glycine are chiral, biosynthetic pathways must generate the correct isomer with high fidelity. In each of the 19 pathways for the generation of chiral amino acids, the stereochemistry at the α-carbon atom is established by a transamination reaction that involves pyridoxal phosphate. Almost all the transaminases that catalyze these reactions descend from a common ancestor, illustrating once again that effective solutions to biochemical problems are retained throughout evolution.Biosynthetic pathways are often highly regulated such that building-blocks are synthesized only when supplies are low. Very often, a high concentration of the final product of a pathway inhibits the activity of enzymes that function early in the pathway. Often present are allosteric enzymes capable of sensing and responding to concentrations of regulatory species. These enzymes are similar in functional properties to aspartate transcarbamoylase and its regulators. Feedback and allosteric mechanisms ensure that all twenty amino acids are maintained in sufficient amounts for protein synthesis and other processes.
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