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Biochemistry And Molecular Biology

  • Binding pocket diagram The image suggests that by providing appropriate non-covalent interactions at sites A, B and C, students can create a binding pocket selective for the neurotransmitter molecule serotonin.

    Serotonin in the Pocket: Non-covalent interactions and neurotransmitter binding

    Learning Objectives
    • Students will design a binding site for the neurotransmitter serotonin.
    • Students will be able to determine the effect of a change in molecular orientation on the affinity of the molecule for the binding site.
    • Students will be able to determine the effect of a change in molecular charge on the affinity of the molecule for the binding site.
    • Students will be able to better differentiate between hydrogen bond donors and acceptors.
    • Students can use this knowledge to design binding sites for other metabolites.
  • Multiple sequence alignment of homologous cytochrome C protein sequences using Jalview viewer.

    Sequence Similarity: An inquiry based and "under the hood" approach for incorporating molecular sequence...

    Learning Objectives
    At the end of this lesson, students will be able to:
    • Define similarity in a non-biological and biological sense when provided with two strings of letters.
    • Quantify the similarity between two gene/protein sequences.
    • Explain how a substitution matrix is used to quantify similarity.
    • Calculate amino acid similarity scores using a scoring matrix.
    • Demonstrate how to access genomic data (e.g., from NCBI nucleotide and protein databases).
    • Demonstrate how to use bioinformatics tools to analyze genomic data (e.g., BLASTP), explain a simplified BLAST search algorithm including how similarity is used to perform a BLAST search, and how to evaluate the results of a BLAST search.
    • Create a nearest-neighbor distance matrix.
    • Create a multiple sequence alignment using a nearest-neighbor distance matrix and a phylogram based on similarity of amino acid sequences.
    • Use appropriate bioinformatics sequence alignment tools to investigate a biological question.
  • Students using the Understanding Eukaryotic Genes curriculum to construct a gene model. Students are working as a pair to complete each Module using classroom computers.

    An undergraduate bioinformatics curriculum that teaches eukaryotic gene structure

    Learning Objectives
    Module 1
    • Demonstrate basic skills in using the UCSC Genome Browser to navigate to a genomic region and to control the display settings for different evidence tracks.
    • Explain the relationships among DNA, pre-mRNA, mRNA, and protein.
    Module 2
    • Describe how a primary transcript (pre-mRNA) can be synthesized using a DNA molecule as the template.
    • Explain the importance of the 5' and 3' regions of the gene for initiation and termination of transcription by RNA polymerase II.
    • Identify the beginning and the end of a transcript using the capabilities of the genome browser.
    Module 3
    • Explain how the primary transcript generated by RNA polymerase II is processed to become a mature mRNA, using the sequence signals identified in Module 2.
    • Use the genome browser to analyze the relationships among:
    • pre-mRNA
    • 5' capping
    • 3' polyadenylation
    • splicing
    • mRNA
    Module 4
    • Identify splice donor and acceptor sites that are best supported by RNA-Seq data and TopHat splice junction predictions.
    • Utilize the canonical splice donor and splice acceptor sequences to identify intron-exon boundaries.
    Module 5
    • Determine the codons for specific amino acids and identify reading frames by examining the Base Position track in the genome browser.
    • Assemble exons to maintain the open reading frame (ORF) for a given gene.
    • Define the phases of the splice donor and acceptor sites and describe how they impact the maintenance of the ORF.
    • Identify the start and stop codons of an assembled ORF.
    Module 6
    • Demonstrate how alternative splicing of a gene can lead to different mRNAs.
    • Show how alternative splicing can lead to the production of different polypeptides and result in drastic changes in phenotype.
  • Students engaged in building the PCR model

    A Close-Up Look at PCR

    Learning Objectives
    At the end of this lesson students will be able to...
    • Describe the role of a primer in PCR
    • Predict sequence and length of PCR product based on primer sequences
    • Recognize that primers are incorporated into the final PCR products and explain why
    • Identify covalent and hydrogen bonds formed and broken during PCR
    • Predict the structure of PCR products after each cycle of the reaction
    • Explain why amplification proceeds exponentially
  • Sodium-Potassium pump

    Lights, Camera, Acting Transport! Using role-play to teach membrane transport

    Learning Objectives
    At the end of this activity, students should be able to:
    • Compare and contrast the mechanisms of simple diffusion, facilitated diffusion, and active transport (both primary and secondary).
    • Identify, and provide a rationale for, the mechanism(s) by which various substances cross the plasma membrane.
    • Describe the steps involved in the transport of ions by the Na+/K+ pump, and explain the importance of electrogenic pumps to the generation and maintenance of membrane potentials.
    • Explain the function of electrochemical gradients as potential energy sources specifically used in secondary active transport.
    • Relate each molecule or ion transported by the Na+/glucose cotransporter (SGLT1) to its own concentration or electrochemical gradient, and describe which molecules travel with and against these gradients.
  • Structure of protein ADA2

    Understanding Protein Domains: A Modular Approach

    Learning Objectives
    • Students will be able to compare protein sequences and identify conserved regions and putative domains.
    • Students will be able to obtain, examine, and compare structural models of protein domains.
    • Students will be able to interpret data on protein interactions (in vitro pull-down and in vitro and in vivo functional assays)
    • Students will be able to propose experiments to test protein interactions.
  • This is the question when working with pH and pKa. This is original artwork by the author and no copyright is violated.

    Taking the Hassle out of Hasselbalch

    Learning Objectives
    Students will be able to:
    1. Characterize an aqueous environment as acidic or basic.
    2. Explain that pKa is a measure of how easy it is to remove a proton from a molecule.
    3. Predict ionization state of a molecule at a particular pH based on its pKa (qualitative use of the Henderson-Hasselbalch equation).
    4. Calculate the ratio of protonated/unprotonated forms of ionizable groups depending on chemical characteristics and /or environment pH (quantitative use of the Henderson-Hasselbalch equation).
    5. Apply this knowledge in a medical context.