Documents about Glutamic Acid

  • 9 Pages

    lec08-S-peptide Helical Folding, (cont.)

    MIT, BIOL 7.88

    Excerpt: ... ular dichroism with pH had indicated that glutamic acid 2 and histidine 12 were important in stabilizing helix in the region of peak helicity (pH5). To test this, Shoemaker et al synthesized C peptides with glutamic acid 2 > alanine, and with histidine 12 > alanine. pk of histidine = 6.7 glutamic acid = 3.8 They then measured circular dichroism as a function over Ph over a wide range. The results were as follows. [Note: Results may be found in: Baldwin, Robert L. "Seding Protein Folding." TIBS 11 (1986): 6-9.] Now in this C-peptide the only groups titrating in the range pH2-5 is the glutamic acid , and the only group titrating in the range 8>5 is the histidine. Loss of glutamic acid results in loss of stabilility. Major increase in stability occurs in range of protonation of his-12. Consistent with his 12 + contributing to helicity. In acid region, removing glutamic acid removes change with acid ph. Loss of histidine. In acid region helicity increases with ionization of glutamic acid . ...

  • 3 Pages

    Lecture 8 Notes

    SUNY Stony Brook, BIO 202

    Excerpt: ... nal unphosphorylated molecule i.e. synthesis of the amino acid glutamine from glutamic acid and ammonia ATP phosphoryates glutamic acid (Glu) Ammonica displaces the phosphate group Glutamine (Glu-NH2) is formed Overall process is exergonic, so occurs spontaneously The Regeneration of ATP Regenerated by the addition of phosphate to ADP Energy required to phosphorylate ADP comes from catabolism ATP cycle: coupled exergonic and endergonic processes ...

  • 3 Pages

    Problem Set 2

    UNC, BIOL 202

    Excerpt: ... lved by Max Perutz. Download the file "haemoglobin.pse" from Blackboard and open the file in PyMOL. Three objects are available on the right panel: Haemoglobin (cartoon format), obj01 (line format of the protein), obj02 (stick format of the cofactor Heme groups). a. Find three amino acids in the protein chain that you suspect, when mutated at the DNA level, would interfere with haemoglobin function by acting as dominant negatives, (binding wild type molecules of haemoglobin but preventing the complete formation of a homotetramer). b. Find three amino acids that you predict would effect heme binding and or the ability of heme to function properly for transport of oxygen. c. Sickle cell anemia is caused by a mutation in the haemoglobin gene that results in the substitution of Valine at position 6 instead of the usual residue: Glutamic Acid . For each of the four proteins in the tetramer, find Glutamic Acid residue 6 and convert this residue to spherical representation (right click on the residue and select: resi ...

  • 2 Pages

    Discussion_HomeworkMar10

    Wisconsin, BIO 151

    Excerpt: ... all by itself. iii. Deletion of C at position 15. This deletion would change the first 3 codons in the mRNA which might change the first 3 amino acids and would leave one base by itself. vi. Which of the mutations produces the greatest change in the amino acid sequence of the polypeptide coded for by this 21 base pair gene? The addition of T between positions 8 and 9. 3. Sickle-cell disease is caused by a single base substitution in the gene for the beta subunit of hemoglobin. This base substitution changes one of the amino acids in the hemoglobin molecule from glutamic acid to valine. Look up the structures of glutamic acid (glu) and valine (val) on page 51 of your textbook. What kinds of changes in protein structure might result from this substitution? Explain. When adding valine to the molecule you are getting rid of one carboxyl group that was present in the glutamic acid . This change might alter the peptide bond that was once present between glutamic acid and the previous amino acid, altering the over al ...

  • 2 Pages

    lecture handout 3

    UCSB, BILD 1

    Excerpt: ... Handout Lecture 2 The 20 Amino Acids Nonpolar Glycine (Gly or G) Alanine (Ala or A) Leucine (Leu or L) Valine (Val or V) Isoleucine (Ile or I) Proline (Pro or P) Methionine (Met or M) Phenylalanine (Phe or F) Trypotphan (Trp or W) Polar Serine (Ser or S) Threonine Cysteine (Thr or T) (Cys or C) Tyrosine (Tyr or Y) Asparagine (Asn or N) Glutamine (Gln or Q) Acidic Electrically charged Basic Aspartic acid (Asp or D) Glutamic acid (Glu or E) Lysine (Lys or K) Histidine (His or H) Arginine (Arg or R) ...

  • 3 Pages

    AminoFlashCards

    Brown, CHEM 33

    Excerpt: ... Alanine Arginine Asparagine Aspartic Acid Cysteine Glutamic Acid Glutamine Glycine Histidine Isoleucine Leucine Lysine Methionine Phenylalanine Proline Serine Threonine Tryptophan Tyrosine Valine ...

  • 2 Pages

    S16

    University of Texas, BIO 325

    Excerpt: ... S1.There are mutant tRNAs that act as nonsense and missense suppressors. At the molecular level, explain how you think these suppressors work. Answer: A suppressor is a second-site mutation that suppresses the phenotypic effects of a first mutation. Intergenic suppressor mutations in tRNA genes can act as nonsense or missense suppressors. For example, lets suppose a first mutation puts a stop codon into a structural gene. A second mutation in a tRNA gene can alter the anticodon region of a tRNA so that the anticodon recognizes a stop codon but inserts an amino acid at this site. A missense suppressor is a mutation in a tRNA gene that changes the anticodon so that it puts in the wrong amino acid at a normal codon that is not a stop codon. These mutant tRNAs are termed missense tRNAs. For example, a tRNA that normally recognizes glutamic acid may incur a mutation that changes its anticodon sequence so that it recognizes a glycine codon instead. Like nonsense suppressors, missense suppressors can be produced ...

  • 25 Pages

    Lecture 8 Thermodynamics

    Cincinnati, BIOL 301

    Excerpt: ... What about changes under real conditions? In a cell, standard conditions clearly do not exist Therefore, the change in free energy for a given reaction ( G) can vary with the specific conditions G for ATP in a cell Typical concentrations in a cell [ATP] = 10 mM [ADP] = 1 mM [Pi] = 20 mM Remember Keq = 2.3 x 105 Under these conditions, G = -11kcal/mol Coupling endergonic and exergonic reactions A reaction, as written may be endergonic, but may still occur One way for this to happen is to couple the endergonic reaction with an exergonic one Example Glutamic acid + NH3 glutamine G'=+3.4 kcal/mol Do this reaction in two steps 1. Glutamic acid + ATP glutamyl phosphate + ADP Here G'= - 7.3 kcal/mol (ATP was hydrolyzed) 2. Glutamyl phosphate + NH3 glutamine + Pi This part, G'= + 3.4 kcal/mol Overall reaction G'= - 3.9 kcal.mol Enzymes - Thermodynamic Considerations Enzymes cannot change the Keq for a reaction. They can speed up reactions, but they cannot change the e ...

  • 7 Pages

    Week 2 Review Sheet answers

    Cincinnati, BIOL 301

    Excerpt: ... on to this statement. Sickle cell anemia is based on a single base substitution in which a valine is inserted in place of a glutamic acid . You should recognize why this type of change could alter the tertiary structure of the protein. Domains and motifs. Quaternary structure. Only seen in proteins made up of multiple subunits, since this has to do with the interaction between subunits. The same forces that are at work in tertiary structure also connect polypeptides that associate into multimeric proteins. A "protein" may be functional as a single polypeptide chain or as a part of a "multimeric" structure. If the latter, the functional protein has several polypeptide chains, each of which plays some role in the function of the protein. Proteins may also aggregate into larger complexes, in which one may identify several separable activities. A number of such "machines" are found in cells, for example those involved in DNA replication, in which there are proteins which unfold DNA, keep it single stranded, etc., ...

  • 5 Pages

    lecture outlines for posting8

    UCLA, EE BIOL 13

    Excerpt: ... Lecture 8 EEB 13 31 January 2008 Dr. Hespenheide kinds of microevolutionary change: - affect kinds/frequencies of alleles - four: mutation, migration. natural selection, genetic drift 1. mutation - two kinds [chromosomal mutations discussed Tuesday] gene mutations - to a single gene or allele [remember, genes produce proteins by the triplet code] deletions/insertions a base pair is lost or added and alters way triplets are read afterward; for example CAT.TAG.GAT.ACT. [C-deleted] ATT.AGG.ATA.CT. called a "nonsense" mutation, creates a very damaged enzyme, usually always a "bad" mutation substitutions - change in only one base pair - example: sickle-cell anemia - mutation to Hb (146 aa's) position 6: triplet CTC (codes for glutamic acid ) CAC (valine) silent mutations - change in DNA but no change in protein, because triplet code is "redundant"; i.e., an amino acid is coded for by more than one triplet - Hb position 6, triplet CTC ( glutamic acid ) CTT ( glutamic acid ) neutral mutations - change in pro ...

  • 1 Pages

    Clicker Questions 9-26

    University of Texas, BIO 311C

    Excerpt: ... Clicker Questions M 9/22 1. a. b. c. d. 2. a. b. c. d. e. 3. a. b. c. d. The side chain of glutamic acid is _, while the side chain of valine is _. Polar & charged; polar & uncharged Polar & charged; nonpolar Polar & uncharged; polar & uncharged Polar & uncharged; nonpolar What are the four nitrogenous bases found in RNA? A, U, G, C A, T G, C A, T, G, U A, T, U, C U, T, G, C What are the complementary base pairs that form in DNA? A-U and G-C A-T and G-C A-G and T-C A-C and T-G Clicker Questions F 9/26 1. a. b. c. d. e. My biology lecture time is 11-12 12-1 1-2 2-3 3-4 2. A fat is a cell a. true b. false 3. This weekend I am 4. a. b. c. d. Which of the following types of bonds are formed at a ribosome? glycosidic linkage peptide bond ester linkage phosphodiester linkage ...

  • 2 Pages

    Quiz 6 key

    Arizona, BIO 340

    Excerpt: ... is a transversion. Transversions are the substitution of a purine for a pyrimidine or vice versa. b) this is a base substitution or a point mutation. c) this is a missense mutation where one amino acid is substituted for another, specifically alanine to glutamic acid . All point mutations at the second codon position are missense mutations. Note that about 70% of mutations at the third codon position are silent mutations, so only 30% of mutations at the third codon position are missense mutations; at the first codon position about 97% of substitutions are missense mutations, but not all are. 3. Fragile X a) Please write out a short trinucleotide repeat. b) please draw a diagram of the location where the repeat region is found for an individual with the premutation state. Please label location of and approximate number of repeats, promoter, exon one, and intron 1. a) CAGCAGCAGCAGCAG etc. b) see Figure 3 in the lecture ppt for ch 16 (slide 26). 4. Iron assimilation: the drawing below shows the ferratin mRNA ...