3914476120 - Chemistry 6921 Exam 1 Fall Semester 2009 1-10...

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1 Chemistry 6921 Exam 1 Name____________________________ Fall Semester 2009 Maximum Points Score 1-10 30(3 points/question) _________ 11 8 _________ 12 10 _________ 13 12 _________ 14 12 _________ 15 16 _________ 16 12 _________ Bonus 5 _________ Total 100 ____________ 1-10 (3 points each). True or False. If the statement is false, change it to make it true. __F___ 1. In an aqueous solution, protein conformation is determined by two major factors: the formation of the maximum number of hydrogen bonds and the placement of polar amino acid residues around the exterior of the protein. the placement of nonpolar amino acid residues within the core of the protein to minimize interaction with water. ___T__ 2. The three dimensional conformation of protein may be strongly influenced by amino acid residues that are very far apart. ___F__ 3. Detergents such as sodium dodecyl sulfate (SDS) do not affect structure of the proteins that contain disulfide bonds. Detergents do not affect disulfide bonds. SDS denatures the native structure of the proteins regardless of the presence of disulfide bonds. ___F__ 4. Secondary structure of protein is the complete three-dimensional structure of a polypeptide. Secondary structure is local arrangements of polypeptide backbone, while three-dimensional structure of a polypeptide is described by the tertiary structure of protein.
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2 ___T__ 5. If the oligopeptide with the sequence ACDEFGHIKL forms an α -helix, then hydrogen from N-H group of phenylalanine is bonded with carbonyl of alanine. ___F__ 6. The positive charge on proteins in Electrospray Ionization Mass Spectrometry is the result of protonation of the side chains of aspartate and glutamate residues. basic residues - lysine and arginine ___F__ 7. In two-dimensional electrophoresis the proteins are separated based on their solubility and their charge. 2D electrophoresis separates proteins by their pI in the first dimension (isoelectric focusing) and by their size in the second dimension (SDS-PAGE) ___F__ 8. In hydrophobic interaction chromatography proteins bind to the matrix in the solution with low concentration of salt and eluted by increasing salt concentration. In hydrophobic chromatography proteins bind to matrix at high salt when hydrophobic
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3914476120 - Chemistry 6921 Exam 1 Fall Semester 2009 1-10...

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