Biology is designed for multi-semester biology courses for science majors. It is …
Biology is designed for multi-semester biology courses for science majors. It is grounded on an evolutionary basis and includes exciting features that highlight careers in the biological sciences and everyday applications of the concepts at hand. To meet the needs of today’s instructors and students, some content has been strategically condensed while maintaining the overall scope and coverage of traditional texts for this course. Instructors can customize the book, adapting it to the approach that works best in their classroom. Biology also includes an innovative art program that incorporates critical thinking and clicker questions to help students understand—and apply—key concepts.
By the end of this section, you will be able to:Describe the …
By the end of this section, you will be able to:Describe the role of enzymes in metabolic pathwaysExplain how enzymes function as molecular catalystsDiscuss enzyme regulation by various factors
By the end of this section, you will be able to:Describe the …
By the end of this section, you will be able to:Describe the role of enzymes in metabolic pathwaysExplain how enzymes function as molecular catalystsDiscuss enzyme regulation by various factors
This resource is a video abstract of a research paper created by …
This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:
"A team of researchers based at West Virginia University has devised an innovative way to potentially monitor enzyme activity in vivo using electron paramagnetic resonance imaging. The method could provide new insights into the molecular underpinnings of many types of disease. The team specifically focused on tracking enzymatic dephosphorylation. Abnormalities in dephosphorylation have been linked to disorders ranging from cancer to Alzheimer disease. Monitoring such malfunction in vivo can provide crucial details into disease state and progression, but direct measurement of enzyme activity within a living organism remains extremely challenging. Many imaging approaches that might be used for this purpose are hampered by concerns such as low sensitivity and penetration depth. Such limitations prompted the researchers to turn to EPRI – a method with high intrinsic sensitivity and specificity..."
The rest of the transcript, along with a link to the research itself, is available on the resource itself.
This resource is a video abstract of a research paper created by …
This resource is a video abstract of a research paper created by Research Square on behalf of its authors. It provides a synopsis that's easy to understand, and can be used to introduce the topics it covers to students, researchers, and the general public. The video's transcript is also provided in full, with a portion provided below for preview:
"Calcineurin is a serine/threonine phosphatase that serves as a critical bridge between calcium signaling and the phosphorylation states of numerous important substrates. But despite being studied for approximately 40 years, exactly how calcineurin is activated in humans and other organisms is not yet fully understood. Structurally, calcineurin is a heterodimer expressed as three different isoforms: α, β, and γ each featuring a catalytic domain, a B chain binding helix, the regulatory domain, an autoinhibitory domain, and an unstructured C-terminal domain of unknown function. Disorder is a key hallmark of calcineurin’s structure. The intrinsically disordered regulatory domain could facilitate the rapid activation of calcineurin during calcium signaling. Increasing evidence suggests that calcineurin is a vital component of various signaling pathways. But even more work is needed to understand calcineurin’s versatility including how certain substrates bind to calcineurin..."
The rest of the transcript, along with a link to the research itself, is available on the resource itself.
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