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CHEM501- Introduction to Biochemistry – Exam 1 w
CHEM501- Introduction to Biochemistry – Exam 1 w

... D) The problem cannot be solved without knowing the value of pKa. E) None of the above. 7. A 1.0 M solution of a compound with 2 ionizable groups (pKa’s = 6.2 and 9.5; 100 mL total) has a pH of 6.8. If a biochemist adds 60 mL of 1.0 M HCl to this solution, the solution will change to pH: A) B) C) D) ...
Macromolecules pt 3
Macromolecules pt 3

... chemical agents (2-mercaptoethanol) ...
SLIB biochemistry homework
SLIB biochemistry homework

... 16) Draw the ring structures of -glucose and -fructose. State the name of the disaccharide that can be formed from these two monosaccharides. 17) State two structural differences between maltose and lactose. 18) Compare the structural features of the two polysaccharides that are found in starch. 1 ...
sheet#30
sheet#30

... one is transamination which happens for most amino acids and the second mechanism is oxidative deamination. Now, we will describe these two mechanisms in details: Transamination: the enzymes here are called transaminases and they require pyridoxal phosphate (PLP) as cofactor (which is the active for ...
What are L-Amino Acids
What are L-Amino Acids

... Most plants can actually manufacture the amino acids they require to live. This is in contrast to many animals (including humans) that are only able to manufacture certain amino acids, and must ingest the others in order to function. All amino acids that occur in proteins are of the “L” form (as opp ...
Unit 3 Review Sheet – Biochemistry
Unit 3 Review Sheet – Biochemistry

... 5. What are the characteristics of water that make it important to life? Polar, high heat capacity, resists temperature change, ability to bond and attract other molecules (cohesion and adhesion), ice is less dense than liquid water, universal solvent, most abundant compound in living things 6. What ...
Chapter 2
Chapter 2

... by hydrogen bonds between different parts of the molecule. The same patterns of secondary structure occur in many different proteins. ...
File - Pi Beta Philes!
File - Pi Beta Philes!

... break down proteins in vital organs like heart and liver later as starvation continues b. The body breaks down it own proteins, giving no priority to tissues such as heart or liver over muscle c. There is a specific storage protein, found in the liver, which will be broken down initially before othe ...
Proteins & Nucleic Acids - St. Mary Catholic Secondary School
Proteins & Nucleic Acids - St. Mary Catholic Secondary School

... Ladder shape – Rails - A series of alternating phosphates and sugars linked by covalent bonds known as phosphodiester bonds. Rungs of the ladder are made of the nitrogenous bases and their hydrogen bonds. The nitrogenous bases involved with DNA are adenine, cytosine, guanine and thymine. The adenine ...
Life Substances
Life Substances

DNA to Protein - Seabreeze High School
DNA to Protein - Seabreeze High School

... Things to think About & Discuss 1. What if a mutation occurs in the DNA? Explain how could that affect the organism’s protein? 2. What if a mutation occurs in 3rd base of the codon? Will it always code for a different amino acid? Explain. ...
sample written evaluation
sample written evaluation

... substrates were highly correlated > 0.9. Average costs were used for subsequent analysis of correlation between cost and codon usage bias. Correlation Between Metabolic Cost and Synonymous Codon Usage Bias For each of the 3397 genes in E. coli and 3055 genes in B. subtilis, average cost per amino ac ...
2. Explain how organic polymers contribute to
2. Explain how organic polymers contribute to

... 3. What subunits come together to make a protein? Amino acids Carbohydrates Lipids ...
MBch15
MBch15

... Eukaryotic gene regulation at steps after transcription initiation ...
1. The carbon atoms of cysteine are derived from: A. Methionine B
1. The carbon atoms of cysteine are derived from: A. Methionine B

... Glutaminase generates glutamine from glutamate using free ammonia. Glutamine is the most abundant amino acid in serum. Guutamine synthetase utilizes ATP. Glutamine donates a nitrogen to aspartate to form asparagine. Glutamine can be used as a carbon source for energy by it conversion to TCA cycle in ...
Answer
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... 31. What are the 4 main elements making up proteins? How many covalent bonds does each of these elements form? Carbon-4 hydrogen-1 nitrogen-3 and oxygen-2 32. Sketch these two amino acids --- glycine & alanine. Circle the center carbon, place a triangle around the amino group, and put a box around t ...
Answers to Exam 1 multiple choice, TF and short answer questions
Answers to Exam 1 multiple choice, TF and short answer questions

... a. is another term for the primary sequence of a protein. b. refers to a subunit in a multi-subunit protein (i.e., one that has quaternary structure). c. refers to the pattern of α-helices and β-sheets in particular parts of a protein. d. is a segment of a protein that can fold independently of the ...
Calling names
Calling names

... Genetic information written in codons is translated into amino acid sequences • The “words” of the DNA “language” are triplets of bases called codons – 3 bases or nucleotides make one ...
Biological Molecules - Westgate Mennonite Collegiate
Biological Molecules - Westgate Mennonite Collegiate

... 1. Many biological molecules are polymers A. ...
Document
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... by brush border enzymes (carboxypeptidase, aminopeptidase, and dipeptidase) of mucosal cells. ...
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... sites), and T1 and T2 (the frequency of T at first and second positions). T4 varies enormously due to mutational pressure, from less than 10% to more than 90%. T1 and T2 vary almost linearly with T4, but over a narrower range. This shows that both mutation and selection influence T1 and T2. By fitti ...
DNA: Transcription & Translation
DNA: Transcription & Translation

... • mRNA: transports information from DNA from the nucleus to the cell’s cytoplasm • rRNA: (makes up ribosomes): clamps on to mRNA and reads its information to assemble amino acids in the correct order • tRNA: transports amino acids to the ribosomes to be assembled into proteins ...
TRUE or FALSE - GEOCITIES.ws
TRUE or FALSE - GEOCITIES.ws

... The histidine residue on globin can act as either an acid or a base The histidine residue on globin can act as either a proton donor or acceptor ...
Part 2 - people.iup.edu
Part 2 - people.iup.edu

... • Enzymes are probably the most important type of protein. They act as catalysts to speed up chemical reactions • Enzymes can perform their functions repeatedly, functioning as workhorses that carry out the processes of life ...
Prof. Kamakaka`s Lecture 12 Notes
Prof. Kamakaka`s Lecture 12 Notes

... 2nd step intermediate ...
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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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