Structure Function Relationships
Structure Function Relationships - Related Videos
09:51
Investigating Protein Sequence-structure-dynamics Relationships with Bio3D-web
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Cited by 2 •
2017
A protocol for the online investigation of protein sequence-structure-dynamics relationships using Bio3D-web is presented.
10:36
Juxtasomal Biocytin Labeling to Study the Structure-function Relationship of Individual Cortical Neurons
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Cited by 22 •
2014
To understand the structure of neuronal networks, functional and morphological characterization of individual neurons is a necessity. Here, we demonstrate juxtasomal biocytin labeling, which allows electrophysiological recordings in the extracellular configuration, yet maintaining the ability to intracellularly label the neuron for post hoc reconstruction of dendritic and axonal architecture.
08:25
Combining Volumetric Capnography And Barometric Plethysmography To Measure The Lung Structure-function Relationship
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Cited by 1 •
2019
Here, we describe two measures of pulmonary function – barometric plethysmography, which allows the measurement of lung volume, and volumetric capnography, a tool to measure the anatomic dead space and airways uniformity. These techniques may be used independently or combined to assess airways function at different lung volumes.
09:58
Mapping the Structure-Function Relationships of Disordered Oncogenic Transcription Factors Using Transcriptomic Analysis
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Cited by 30 •
2020
Intrinsically disordered domains are important for oncogenic fusion transcription factor function. To therapeutically target these proteins, a more detailed understanding of the regulatory mechanisms employed by these domains is required. Here, we use transcriptomics to map important structural features of the intrinsically disordered EWS domain in Ewing sarcoma.
01:56
Structural Protein Function
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2020
Structural proteins are a category of proteins responsible for functions ranging from cell shape and movement to providing support to major structures such as bones, cartilage, hair, and muscles. This group includes proteins such as collagen, actin, myosin, and keratin. Collagen, the most abundant protein in mammals, is found throughout the body. In connective tissue, such as skin, ligaments, and tendons, it provides tensile strength and elasticity. In bones and teeth, it mineralizes to form...
FAQs
A sequence change can modify three-dimensional folding, the placement of chemical groups, or the bonding pattern that supports molecular interactions. These structural shifts may affect binding to substrates, cofactors, membranes, or other biomolecules. Consequently, comparing sequence changes with altered activity helps researchers connect molecular variation to biochemical function and investigate possible disease mechanisms.
Chemical groups and bonding determine which interactions a biological molecule can make and how those interactions are arranged in three-dimensional space. This organization influences recognition of substrates, cofactors, membranes, and other biomolecules. Examining these features clarifies why a particular molecular structure supports a given activity and how structural changes may weaken or redirect that activity.
Environmental conditions can change a molecule’s three-dimensional organization, which may alter the position of functional chemical groups and the interactions needed for activity. Because structure and function are linked, such changes can influence enzyme catalysis, molecular recognition, or interactions with other biomolecules. Studying these effects helps explain why activity varies under different biochemical conditions.
In enzyme catalysis, structural organization determines how a molecule carries out a chemical activity, including interactions with substrates and cofactors. In molecular recognition, the same structural principles govern selective interactions with other biomolecules. The emphasis differs, but both processes depend on shape, chemical groups, bonding, and three-dimensional folding to produce the observed biochemical outcome.
Researchers can examine a molecule’s sequence, three-dimensional folding, chemical groups, and bonding, then relate those features to interactions with substrates, cofactors, membranes, or other biomolecules. They can also consider how sequence changes or environmental conditions affect activity. This approach connects molecular organization with outcomes such as enzyme catalysis, recognition, or altered biochemical function.
A disease mechanism may be investigated by linking a sequence change or environmental effect to altered folding, chemical-group placement, bonding, or molecular interactions. Researchers can then assess how the resulting structural change affects enzyme catalysis, recognition, or biochemical pathways. This provides a molecular explanation for how altered biomolecule function may contribute to disease.
Understanding which structural features control activity can guide the design of drugs or engineered proteins with specific functions. Researchers can focus on molecular shape, chemical groups, bonding, and three-dimensional folding, then consider how these features influence interactions with substrates, cofactors, membranes, or other biomolecules. The goal is to connect deliberate structural changes with desired biochemical activities.