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For the textbook, chapter, and section you specified we found
8 Videos
7 Assessment Questions
2 Journal Articles
32 Other Resources
Videos: First 3 results
Nature of Proteins  
Effect of pH on solubility, denaturing proteins, hydrolysis in strong base, binding to coomassie blue, dying wool and cotton, gel filtration column, reaction of ninhydrin with amino acids and precipitating protein with ammonium sulfate are demonstrated.
Proteins / Peptides
Protein Reactions  
Curdling milk, decomposition of hydrogen peroxide by catalase, glucose oxidase activity, hydrolyzing of sucrose with invertase, and using an enzyme to halt the Briggs-Rauscher reaction are demonstrated. Inhibiting the enzyme HIV-1 protease may slow the spread of AIDS.
Proteins / Peptides
Denaturation of Protein by Strong Acid  John W. Moore, Jerrold J. Jacobsen, Gary Trammell, Kristin Johnson
"Strong acid denatures egg white proteins.This video contains voiceover:""The tertiary structure of egg white proteins is held together by hydrogen bonding and hydrophobic interactions. Adding strong acid to the protein disrupts the intermolecular forces, and the tertiary structure is lost. The loss in protein structure is called denaturation. The proteins precipitate, forming a white solid."""
Acids / Bases |
Proteins / Peptides
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Assessment Questions: First 3 results
Biochemistry : NameTripeptide (4 Variations)
What is the name of the tripeptide below?


Proteins / Peptides
Biochemistry : PeptideSequence (19 Variations)
Use the amino acid table below to answer the following question.

Which of the following structures corresponds to the peptide Met-Thr-Arg (methionylthreonylarginine)?


Proteins / Peptides
Biochemistry : PeptideStructure (3 Variations)
All amino acids have which pair of functional groups?
Proteins / Peptides
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Journal Articles: 2 results
Pedagogies:
Homogeneous Immunoassays: Historical Perspective and Future Promise  Edwin F. Ullman
The founding and growth of Syva Company is examined in the context of its leadership role in the development of homogeneous immunoassays. The simple mix and read protocols of these methods offer advantages in routine analytical and clinical applications.
Ullman, Edwin F. J. Chem. Educ. 1999, 76, 781.
Biotechnology |
Enzymes |
Atomic Properties / Structure |
Free Radicals |
Photochemistry |
Medicinal Chemistry |
Proteins / Peptides
An enzyme immunoassay for human transferrin  Russo, Salvatore F.; Dahlberg, Judy Utter
The field of immunology provides a powerful method for detecting specific noncatalytic proteins.
Russo, Salvatore F.; Dahlberg, Judy Utter J. Chem. Educ. 1990, 67, 175.
Enzymes |
Medicinal Chemistry |
Proteins / Peptides
Other Resources: First 3 results
Molecular Models of Natural Products  William F. Coleman
This month's issue of the Journal includes several papers discussing interesting molecules that fall into the broad category of natural products, and four of these papers serve as the source for our featured molecules this time around. Addison Ault weaves an interesting tale of the search for the true structure of eserethole and of the competition between two research groups that of Percy Julian, consisting of two people, and that of the British chemist Robert Robinson, a large group at Oxford (1). David Vosburg describes a case study approach to teaching organic synthesis and includes a number of molecules that have been the basis of student research papers (2). Jean-Michel Lavoie, Esteban Chornet, and André Pelletier have developed an experiment utilizing GCMS to separate terpenes from citrus (3), and Patty Feist, in a paper that may send readers running for their Kafka, has students synthesize a cockroach pheromone that may have wide applicability in cockroach control without the problems created by many insecticides (4).The molecules that have been added to our collection contain a wide variety of functional groups, and would serve as a good source for an exercise in having students recognize these functional groups in a number of different settings. Questions such as How many cyclic ether groups are present?, How many bridgehead carbons?, or How many chiral centers would be useful exercises in organic and introductory non-majors courses. Students could find other pheromone structures and see how they compare with that of blattellaquinone, or explore the various ways in which the steroid backbone shows up in the collection.This collection of molecules also provides a good starting point for students to use the capabilities of Jmol to further explore structural features. The focus here is on measuring bond distance and angles. Double clicking on any atom will change the cursor to a cross-hair (this may take a little practice). One end of a dashed line is now locked to that atom. Dragging the free end of the line to other atoms will show the distance between the two centers in nanometers. Double clicking on a second atom will lock a line segment between those two atoms and display the distance in black. There is now another free end of the segmented line, and dragging that to any other atom will show the angle defined by the three-atom combination. Double clicking on the third atom fixes the second line segment and gives a third segment that can be dragged and double clicked to display dihedral angles. Students could, for example, explore various ring structures in this collection to determine which rings are distorted and which are not.The files that are currently used for the collection are MDL mol files, and do not contain orbital, electrostatic potential, or vibrational data. Beginning next month we will change the file format, and that information will be available to users, either through the Jmol menu (right click on any structure) or through menu choices.Not all of the molecules from the Ault paper (1) have been included, leaving room for students to model and perform calculations on many of the non-eserethole species, and to consider how modern tools of analysis might have simplified the identification of eserethole. They might also wish to determine which pair of eserethole enantiomers are the more stable. (The eserethole structures included here have all been optimized at the 6311++G (d,p) level.)
Natural Products
Molecular Models of Rosmarinic Acid and DPPH  William F. Coleman
The paper by Canelas and da Costa (1) introduces students to the antioxidant rosmarinic acid, and its interaction with the free radical DPPH. Those two molecules are the featured species this month. The original paper shows the 2-dimensional structure of the cis isomer of rosmarinic acid, although the trans isomer exhibits very similar antioxidant properties. Calculations at the DFT/B3LYP 631-G(d) level show that the trans isomer is more stable than the cis isomer in the gas phase, a situation that is expected to carry over into solution. Many antioxidants are phenols, and rosmarinic acid has four such groups available for radical formation. A DFT study by Cao et al. (2) examines the relative stabilities of the radicals formed from loss of each of the phenolic hydrogens. That paper focuses on the trans isomer, and a useful student project would be to repeat the calculations with the cis isomer. An HPLC separation of the isomers of rosmarinic acid has been published (3), and might well lead to an extension of the experiment described in ref 1 in which relative antioxidant efficiencies of the two isomers could be evaluated. DPPH has been used extensively as a standard for determining antioxidant activity. An examination of the molecular orbital occupied by the lone electron shows significant delocalization, providing a partial explanation for the stability of the neutral radical. Our gas phase structure for DPPH, also at the DFT/B3LYP 631-G(d) level, is quite consistent with several crystal structures on DPPH and DPPH in the presence of another species (4).
Natural Products
Umami and Proteins  Robert Hetue
A section of ChemPrime, the Chemical Educations Digital Library's free General Chemistry textbook.
Proteins / Peptides
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