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 ...

  • 1 Pages

    Homework Assignment 3

    Minnesota, CHEM 4101

    Excerpt: ... e applied. (1) e) In tandem MS/MS, we can use the first mass analyzer as a selective filter for poly-gamma-D- glutamic acid precursor ions, separating L- glutamic acid . Because these structures are so similar, more information will be investigated on whether a method such as tandem MS/MS can separate such closely related molecules. In all realistic nature, the experiment might have to be designed for a set length of poly-D- glutamic acid , such that we assume a string of equal length poly-L- glutamic acid is highly unlikely. Therefore, the product ions can be seen as different length peptides of poly-D- glutamic acid . References (1) Schneerson, R.; Kubler-Kielb, J.; Liu, T. Y.; Dai, Z. D.; Leppla, S. H.; Yergey, A.; Backlund, P.; Shiloach, J.; Majadly, F.; Robbins, J. B. Proc. Natl. Acad. Sci. U. S. A. 2003, 100, 8945-8950. ...

  • 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) ...

  • 1 Pages

    Amino acid names

    N. Arizona, BIO 350

    Excerpt: ... The One-Letter Symbols One-letter symbol A B C D E F G H I K L M N P Q R S T V W X * Y Z Three-letter symbol Ala Asx Cys Asp Glu Phe Gly His Ile Lys Leu Met Asn Pro Gln Arg Ser Thr Val Trp Xaa Tyr Glx Amino acid alanine aspartic acid or asparagine cysteine aspartic acid glutamic acid phenylalanine glycine histidine isoleucine lysine leucine methionine asparagine proline glutamine arginine serine threonine valine tryptophan unknown or 'other' amino acid tyrosine glutamic acid or glutamine (or substances such as 4-carboxy glutamic acid and 5-oxoproline that yield glutamic acid on acid hydrolysis of peptides) Note on the Choice of Symbols Initial letters of the names of the amino acids were chosen where there was no ambiguity. There are six such cases: cysteine, histidine. isoleucine, methionine, serine and valine. All the other amino acids share the initial letters A, G, L, P or T, so arbitrary assignments were made. These letters were assigned to the most frequently occurring and structurally most simple of t ...

  • 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 ...

  • 3 Pages

    HW10_key

    Columbia, C 3444

    Excerpt: ... C3444Organic Chemistry II Nuckolls section Aminoacids and Peptides, Problem Set #10 Not due Read Chapter 26 Excercises: v McMurry 5th Ed Problems Ch.26: 26.35, 26.36, 26.37, 26.38, 26.39, 26.48, 26.51, v Additional Problems: 1. How many stereoisomers are there of threonine? 4 How about serine? 2 2. Would it be better to synthesize valine from an amidomalonate synthesis or a Strecker synthesis? Why? Valine should be synthesized by a Strecker to avoid elimination of from alkylation of the secondary halide. 3.Show how you would synthesize glutamic acid from the starting material below. O EtO EtO O O H O N O OEt 1. KOEt Glutamic acid 2. H2 O/ 3. H30 +/ D OH- 4. Show how you would synthesize aspartic acid from the starting material below. O EtO EtO O H O N H EtO O Br 1. KOEt 2. H3 0+ / D Aspartic Acid 5. Show how you would synthesize the following tri-peptide with unprotected aminoacids as the starting material. 1 O H 2N CHC OH CH2 CHCH3 CH3 O H 2N CHC OH CH2 CH2 S CH3 H+ MeOH O H 2N CHC OMe CH2 CH2 S CH3 ...

  • 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

    361_Vitamin K

    Idaho, FCS 361

    Excerpt: ... ms. 2. These proteins, specified as vitamin K dependent proteins, contain glutamic acid residues a. Ten to twelve of these glutamic acid residues must be carboxylated for the proteins to be functional. 3. A polypeptide glutamic acid residue can be converted into a calcium binding gamma carboxy glutamic acid (Gla) through the action of carboxylase and its vitamin K coenzyme. 4. Gla residues are able to bind calcium a. This mediates phospholipid adsorption of the GLA containing proteins. b. The adsorption of these specific proteins on phospholipid surfaces is essential in hemostasis. 5. Vitamin K dependent proteins a. osteocalcin: bone Gla protein (BGP) secreted by osteoblasts Notes Courtesy of Dr. Kathe Gabel, PhD, RD, LD b. matrix Gla protein (MGP): bone, dentine, cartilage c. kidney Gla protein (KGP): found in the cortex of the kidney 6. Warfarin sodium crystalline (Coumadin): anticoagulant: Interferes with the main route for reducing oxidized vitamin K to its active coenzyme form (disulfide catalyzed s ...

  • 5 Pages

    361_Vitamin K

    Idaho, FCS 361

    Excerpt: ... These proteins, specified as vitamin K dependent proteins, contain glutamic acid residues a. Ten to twelve of these glutamic acid residues must be carboxylated for the proteins to be functional. 3. A polypeptide glutamic acid residue can be converted into a calcium binding gamma carboxy glutamic acid (Gla) through the action of carboxylase and its vitamin K coenzyme. 4. Gla residues are able to bind calcium a. This mediates phospholipid adsorption of the GLA containing proteins. b. The adsorption of these specific proteins on phospholipid surfaces is essential in hemostasis. 5. Vitamin K dependent proteins a. osteocalcin: bone Gla protein (BGP) secreted by osteoblasts Notes Courtesy of Dr. Kathe Gabel, PhD, RD, LD b. matrix Gla protein (MGP): bone, dentine, cartilage c. kidney Gla protein (KGP): found in the cortex of the kidney 6. Warfarin sodium crystalline (Coumadin): anticoagulant: Interferes with the main route for reducing oxidized vitamin K to its active coenzyme form (disulfide catalyzed system). ...

  • 6 Pages

    sample_exam_sample-exam-final

    Washington, CHEM 239

    Excerpt: ... hest isoelectric point, glutamine, glutamic acid or lysine? R H 2N CO 2H glutamine : glutamic acid lysine R = CH : R = CH R = CH 2 CH 2 CONH 2 2 CH 2 CO 2 H 2 CH 2 CH 2 CH 2 NH 2 (b) Lysine has three ionizable groups with the following pKa values ; pKa (CO2H) = + 2.2, pKa (NH3 ) = 9.0, and pKa (side chain-NH3+) = 10.5, Sketch curves that indicate the relative concentration of different ionic species of glutamic acid . Clearly indicate the structure of ions for each curve. ...

  • 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 ...

  • 5 Pages

    Lecture 2_Asim

    University of Medicine and Dentistry of New Jersey, BINF 5513

    Excerpt: ... Lecture2:AnswerstoHomeAssignments Q1 1. Hemoglobin>bindsO2insideredbloodcells 2. Lipase>breaksdownlipids(fat) Q2 One-letter symbol A B C D E F G H I K L M N P Q R S T U* V W X* Y Z Three-letter symbol Ala Asx Cys Asp Glu Phe Gly His Ile Lys Leu Met Asn Pro Gln Arg Ser Thr Sec Val Trp Xaa Tyr Glx Amino acid alanine aspartic acid or asparagine cysteine aspartic acid glutamic acid phenylalanine glycine histidine isoleucine lysine leucine methionine asparagine proline glutamine arginine serine threonine selenocysteine valine tryptophan unknown or 'other' amino acid tyrosine glutamic acid or glutamine (or substances such as 4-carboxy glutamic acid and 5-oxoproline that yield glutamic acid on acid hydrolysis of peptides) Source:http:/www.chem.qmul.ac.uk/iupac/AminoAcid/A2021.html Q3 Priondisease,Cysticfibrosis,Sicklecell,Diabetesetc. Q4 Allaminoacidshaveeitherhydrophobicorhydrophilicresidueorboth,whicheitherattractor r ...

  • 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 ...

  • 1 Pages

    case14_sickle

    Penn State, BIOL 110

    Excerpt: ... protein's primary structure results in a change in the overall structure of the protein. Sickle-cell anemia is a genetic disease that results in the abnormal production of the protein hemoglobin which causes misshapen red blood cells. The abnormality is in the 6th position of the subunit of the molecule. Normal hemoglobin has a glutamic acid while sickle-cell hemoglobin has a valine in the 6th position. The presence of the valine causes hemoglobin molecules to aggregate together into rod formations. These rods of hemoglobin are not effective at carrying oxygen. People with sickle-cell anemia suffer episodes of "sickle-cell crises" which are painful and, left untreated, can lead to death. Refer to tutorial 16 for an image of the 20 different R groups of amino acids. Use your understanding of the chemical behavior of the R groups to predict what would happen if the glutamic acid in the 6th position was replaced with an aspartic acid (instead of valine). Would this cause more or less disruption to the functio ...

  • 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 ...