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79 Cards in this Set
- Front
- Back
Name?
Abbreviation(s)? Additional Information? |
Alanine
Ala A Nonpolar, Hydrophobic |
|
Name?
Abbreviation(s)? Additional Information? |
Phenylalanine
Phe F Nonpolar, Hydrophobic |
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Name?
Abbreviation(s)? Additional Information? |
Tryptophan
Trp W Nonpolar, Hydrophobic |
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Name?
Abbreviation(s)? Additional Information? |
Methionine
Met M Nonpolar, Hydrophobic |
|
Name?
Abbreviation(s)? Additional Information? |
Proline
Pro P Nonpolar, Hydrophobic |
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Name?
Abbreviation(s)? Additional Information? |
Aspartic acid
Asp D Polar, Acidic |
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Name?
Abbreviation(s)? Additional Information? |
Glutamic acid
Glu E Polar, Acidic |
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Name?
Abbreviation(s)? Additional Information? |
Lysine
Lys K Polar Basic |
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Name?
Abbreviation(s)? Additional Information? |
Arginine
Arg R Polar, Basic |
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Name?
Abbreviation(s)? Additional Information? |
Histidine
His H Polar, Basic |
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Name?
Abbreviation(s)? Additional Information? |
Glycine
Gly G Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Valine
Val V Nonpolar, Hydrophobic |
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Name?
Abbreviation(s)? Additional Information? |
Serine
Ser S Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Leucine
Leu L Nonpolar, Hydrophobic |
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Name?
Abbreviation(s)? Additional Information? |
Cysteine
Cys C Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Tyrosine
Tyr Y Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Asparagine
Asn N Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Glutamine
Gln Q Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Threonine
Thr T Polar, Uncharged |
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Name?
Abbreviation(s)? Additional Information? |
Isoleucine
Iso I Nonpolar, Hydrophobic |
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Which form of amino acids are incorporated into proteins?
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L amino acids
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Which form of amino acid has the amino group on the right?
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D amino acids
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Which form of amino acids has the amino group on the left?
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L amino acids
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Which amino acid has no D or L form, has little polar character, and is the smallest of the amino acids?
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Glycine
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Name the five amino acids that are categorized as non-aromatic with hydrocarbon side chains.
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Alanine
Valine Leucine Isoleucine Proline |
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Name the three amino acids with aromatic hydrocarbon side chains.
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Phenylalanine
Tyrosine Tryptophan |
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Name the two amino acids with sulfur-containing side chains.
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Cysteine
Methionine |
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Name the four amino acids with polar uncharged side chains.
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Serine
Threonine Asparagine Glutamine |
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Name the five amino acids with polar charged side chains:
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Aspartic Acid
Glutamic Acid Lysine Arginine Histidine |
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Which amino acid has the most polar side chain?
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Arginine
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Which amino acid does not have an asymmetric carbon?
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Glycine
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Which amino acid is really an imino acid?
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Proline (has secondary amine)
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Which amino acid has an indole group?
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Tryptophan
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Which amino acid is important in redox reactions?
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Cysteine
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Name the two negatively charged amino acids at physiologic pH.
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Glutamate
Aspartate |
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At physiologic pH acidic amino acids have what charge?
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Negative
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At physiologic pH basic amino acids have what charge?
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Positive
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What kind of bond is formed between amino acids?
How are they formed? |
Peptide bonds
They're formed through condensation reactions. |
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Proteins are made of ___.
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Amino Acids
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These Amino Acids are positively charged at neutral pH.
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Lysine
Arginine Histidine (can be) |
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What are other names of Aspartic Acid and Glutamic Acid?
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Aspartate
Glutamate |
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What is the approximate Pk of a sulfhydryl of cysteine?
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8
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What is the approximate Pk of an alpha-carboxyl?
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2
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What is the approximate Pk of an alpha-amino?
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9-10
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What is the approximate Pk of the phenol of tyrosine?
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10
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What is the approximate Pk of the carboxyls of aspartic and glutamic acid?
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4
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What is the approximate Pk of the amino of Lysine?
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10
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What is the approximate Pk of the quanidinium ion of arginine?
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12
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What is the approximate Pk of an imidazole of histidine?
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6
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Molecules having both + and - functional groups.
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zwitterion
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Which 2 amino acids are common in bends and turns? why?
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proline (it is a fused ring)
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The ring structure in tryptophan is called a _______ group
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indole
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Which two amino acids have a terminal carboxamide in their side chains?
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Glutamine (Q)
Asparagine (N) |
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What end of a peptide is taken to be the beginning of a polypeptide?
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the amino (N) terminus
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Which amino acid can form disulfide bonds and are these covalent forces?
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cysteine
yes these are covalent. |
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What type of reaction forms a disulfide bridge between two cysteines?
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Redox
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Isomers that are mirror images of each other.
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Stereoisomers (Enantiomers)
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Covalent bond formed by a condensation (dehydration) reaction that links the carboxyl group of one amino acid to the amino group of the next.
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Peptide bond
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Building block molecule of a protein; most consist of an asymmetric carbon, termed the alpha carbon, which is covalently bonded to a hydrogen atom, a carboxyl group, an amino group, and a variable R group (or side chain).
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Amino acid
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What are the the functions of proteins?
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Enzymes
defense storage transport hormonal (signals) receptors (signal response) mechanical decoding structural |
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Which stereoisomer is biologically active?
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The L isomer
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Which amino acid has a pyrrolidine ring?
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Proline
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Which amino acid has a benzyl ring?
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phenylalanine
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Which amino acid has a phenol ring?
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Tyrosine
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The absorbance of proteins at 280nm is primarily due to which two amino acids?
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Tyrosine
tryptophan |
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Which amino acid does the start codon encode?
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methionine
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Histamine is a derivative of ____
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Histadine
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Epinephrine and thyroxine are derivatives of ______
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Tyrosine
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Aminobutyrate is a derivative of _______
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Glutamate
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Peptide bonds are an example of a(n) __________ linkage
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Amide
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Fractionation of protein homogenates is based on ________
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solubility
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After fractionation of a protein, ammonium sulfate is removed by _____
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dialysis
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Which type of chromatography uses small columns under pressure?
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HPLC
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Which type of chromatography separates proteins based on charge?
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Ion-exchange
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Which type of chromatography separates proteins based on molecular size?
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Gel filtration
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Which type of chromatography separates proteins based on specific protein binding?
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affinity
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During SDS-PAGE, SDS is added to make the protein _________charged so that the proteins will move through the gel toward the ________ pole.
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negatively
positive |
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Ions in mass spectrometry are separated based on differences in______ and _________.
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Size
charge |
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The protein sequencing procedure that identifies each amino acid by HPLC after it has been cleaved off of the polypeptide chain is called _____
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Edman Degradation
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