<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-biomolecules---tertiary-structure-primary"><primary style="font-size:24px"> Biomolecules - Tertiary Structure </primary></h3> <hr> <main> <ul> <li>The tertiary structure is the three-dimensional arrangement of atoms in a biomolecule.</li> <li>It is formed by interactions between R groups of amino acids.</li> <li>Tertiary structure determines the overall shape and function of proteins.</li> <li>Various forces contribute to the stability of the tertiary structure.</li> <li>Examples of proteins with tertiary structure include enzymes, antibodies, and hemoglobin.</li> </ul> </main> <hr> <footer style = "font-size: 18px"> $\rightarrow$ $\rightarrow$ <span style = "color:blue"> Biomolecules - Tertiary Structure </span> $\rightarrow$ Tertiary Structure - Forces and Interactions $\rightarrow$ Tertiary Structure - Folding </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-1"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---forces-and-interactions-primary"><primary style="font-size:24px"> Tertiary Structure - Forces and Interactions </primary></h3> <hr> <main> <ul> <li><strong>Hydrophobic interactions</strong>: Nonpolar amino acids tend to cluster together to minimize contact with water.</li> <li><strong>Hydrogen bonds</strong>: Formed between polar amino acids or between polar amino acids and water molecules.</li> <li><strong>Disulfide bonds</strong>: Covalent bonds between sulfur atoms of two cysteine residues.</li> <li><strong>Ionic interactions</strong>: Attraction between positively and negatively charged amino acids.</li> <li><strong>Van der Waals forces</strong>: Weak forces of attraction between nonpolar amino acids.</li> </ul> </main> <hr> <footer style = "font-size: 18px"> $\rightarrow$ Biomolecules - Tertiary Structure $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Forces and Interactions </span> $\rightarrow$ Tertiary Structure - Folding $\rightarrow$ Tertiary Structure - Protein Domains </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-2"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---folding-primary"><primary style="font-size:24px"> Tertiary Structure - Folding </primary></h3> <hr> <main> <ul> <li>Protein folding is the process by which a protein adopts its functional tertiary structure.</li> <li>It is guided by the hydrophobic effect and other intermolecular forces.</li> <li>Proteins can fold spontaneously, driven by the energetically favorable state.</li> <li>Incorrect folding can lead to nonfunctional or misfolded proteins.</li> <li>Chaperone proteins help in proper folding and prevent protein aggregation.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Biomolecules - Tertiary Structure $\rightarrow$ Tertiary Structure - Forces and Interactions $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Folding </span> $\rightarrow$ Tertiary Structure - Protein Domains $\rightarrow$ Tertiary Structure - Protein Folding Pathways </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-3"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---protein-domains-primary"><primary style="font-size:24px"> Tertiary Structure - Protein Domains </primary></h3> <hr> <main> <ul> <li>Protein domains are distinct structural and functional units within a larger protein.</li> <li>They can fold independently and perform specific functions.</li> <li>Domains often have conserved sequences and are found in multiple proteins.</li> <li>Examples of protein domains include the DNA-binding domain and kinase domain.</li> <li>Domains play a crucial role in protein-protein interactions and overall protein function.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Forces and Interactions $\rightarrow$ Tertiary Structure - Folding $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Protein Domains </span> $\rightarrow$ Tertiary Structure - Protein Folding Pathways $\rightarrow$ Tertiary Structure - Denaturation </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-4"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---protein-folding-pathways-primary"><primary style="font-size:24px"> Tertiary Structure - Protein Folding Pathways </primary></h3> <hr> <main> <ul> <li>Protein folding follows a specific pathway.</li> <li>Folding intermediates form along the pathway before reaching the native state.</li> <li>The folding pathway can involve multiple folding and unfolding events.</li> <li>Cooperative folding occurs when different parts of the protein fold simultaneously.</li> <li>Misfolded intermediates can lead to protein aggregation and disease.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Folding $\rightarrow$ Tertiary Structure - Protein Domains $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Protein Folding Pathways </span> $\rightarrow$ Tertiary Structure - Denaturation $\rightarrow$ Tertiary Structure - Folding Algorithms </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-5"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---denaturation-primary"><primary style="font-size:24px"> Tertiary Structure - Denaturation </primary></h3> <hr> <main> <ul> <li>Denaturation is the disruption of the tertiary structure of a protein.</li> <li>It can be caused by heat, pH extremes, chemicals, or mechanical stress.</li> <li>Denaturation leads to loss of protein function.</li> <li>Some proteins can regain their native conformation upon removal of denaturing agents.</li> <li>Denatured proteins can aggregate and form amyloid fibrils in certain diseases.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Protein Domains $\rightarrow$ Tertiary Structure - Protein Folding Pathways $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Denaturation </span> $\rightarrow$ Tertiary Structure - Folding Algorithms $\rightarrow$ Tertiary Structure - Protein Misfolding Diseases </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-6"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---folding-algorithms-primary"><primary style="font-size:24px"> Tertiary Structure - Folding Algorithms </primary></h3> <hr> <main> <ul> <li>Folding algorithms are computational methods for predicting protein folding.</li> <li>They use known protein structures to predict the structure of a target protein.</li> <li>The accuracy of folding algorithms varies depending on the complexity of the protein.</li> <li>Algorithms often utilize energy minimization and molecular dynamics simulations.</li> <li>Folding algorithms have applications in drug design and understanding protein function.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Protein Folding Pathways $\rightarrow$ Tertiary Structure - Denaturation $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Folding Algorithms </span> $\rightarrow$ Tertiary Structure - Protein Misfolding Diseases $\rightarrow$ Tertiary Structure - Protein Engineering </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-7"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---protein-misfolding-diseases-primary"><primary style="font-size:24px"> Tertiary Structure - Protein Misfolding Diseases </primary></h3> <hr> <main> <ul> <li>Misfolding of proteins can lead to various diseases.</li> <li>Examples include Alzheimer’s disease, Parkinson’s disease, and prion diseases.</li> <li>Misfolded proteins can aggregate and form plaques or amyloid fibrils.</li> <li>The exact mechanisms underlying protein misfolding diseases are still being studied.</li> <li>Developing therapeutics targeting protein misfolding is an active area of research.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Denaturation $\rightarrow$ Tertiary Structure - Folding Algorithms $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Protein Misfolding Diseases </span> $\rightarrow$ Tertiary Structure - Protein Engineering $\rightarrow$ Tertiary Structure - Protein Structure Determination Methods </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-8"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---protein-engineering-primary"><primary style="font-size:24px"> Tertiary Structure - Protein Engineering </primary></h3> <hr> <main> <ul> <li>Protein engineering involves modifying or designing proteins for specific purposes.</li> <li>Rational design uses knowledge of protein structure and function to make modifications.</li> <li>Directed evolution applies random mutations and selection to generate desired proteins.</li> <li>Protein engineering has applications in medicine, industry, and biotechnology.</li> <li>Examples include creating enzymes with improved catalytic properties or engineering antibodies for targeted therapies.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Folding Algorithms $\rightarrow$ Tertiary Structure - Protein Misfolding Diseases $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Protein Engineering </span> $\rightarrow$ Tertiary Structure - Protein Structure Determination Methods $\rightarrow$ Protein Folding - Energy Landscapes </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-9"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-tertiary-structure---protein-structure-determination-methods-primary"><primary style="font-size:24px"> Tertiary Structure - Protein Structure Determination Methods </primary></h3> <hr> <main> <ul> <li><strong>X-ray crystallography</strong>: Determines protein structure based on diffraction patterns from a crystallized protein.</li> <li><strong>Nuclear Magnetic Resonance (NMR) spectroscopy</strong>: Provides structural information by measuring interactions between atomic nuclei.</li> <li><strong>Cryo-electron microscopy (cryo-EM)</strong>: Uses electron microscopy to determine the 3D structure of proteins in their native state.</li> <li><strong>Mass spectrometry</strong>: Determines the mass and amino acid sequence of proteins, which can help infer their tertiary structure.</li> <li><strong>Bioinformatics methods</strong>: Analyze protein sequences and predict their tertiary structure based on known structures.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Protein Misfolding Diseases $\rightarrow$ Tertiary Structure - Protein Engineering $\rightarrow$ <span style = "color:blue"> Tertiary Structure - Protein Structure Determination Methods </span> $\rightarrow$ Protein Folding - Energy Landscapes $\rightarrow$ Protein Misfolding Diseases - Alzheimer's Disease </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-10"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-folding---energy-landscapes-primary"><primary style="font-size:24px"> Protein Folding - Energy Landscapes </primary></h3> <hr> <main> <ul> <li>Protein folding occurs along an energy landscape.</li> <li>Folding begins in the unfolded state where the protein has high potential energy.</li> <li>The folded state represents the lowest energy state for the protein.</li> <li>Folding intermediates are states with lower energy than the unfolded state but higher than the folded state.</li> <li>The energy landscape is rugged, with multiple pathways leading to the native structure.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Protein Engineering $\rightarrow$ Tertiary Structure - Protein Structure Determination Methods $\rightarrow$ <span style = "color:blue"> Protein Folding - Energy Landscapes </span> $\rightarrow$ Protein Misfolding Diseases - Alzheimer's Disease $\rightarrow$ Protein Misfolding Diseases - Parkinson's Disease </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-11"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-misfolding-diseases---alzheimers-disease-primary"><primary style="font-size:24px"> Protein Misfolding Diseases - Alzheimer’s Disease </primary></h3> <hr> <main> <ul> <li>Alzheimer’s disease is characterized by the accumulation of amyloid-beta plaques in the brain.</li> <li>Amyloid-beta is derived from the misfolding of the amyloid precursor protein (APP).</li> <li>Misfolded proteins aggregate to form insoluble plaques, leading to neuron dysfunction and cognitive decline.</li> <li>The exact mechanism of amyloid-beta aggregation and its role in Alzheimer’s disease is still under investigation.</li> <li>Therapies targeting amyloid-beta aggregation are being developed as potential treatments for Alzheimer’s disease.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Tertiary Structure - Protein Structure Determination Methods $\rightarrow$ Protein Folding - Energy Landscapes $\rightarrow$ <span style = "color:blue"> Protein Misfolding Diseases - Alzheimer's Disease </span> $\rightarrow$ Protein Misfolding Diseases - Parkinson's Disease $\rightarrow$ Protein Misfolding Diseases - Prion Diseases </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-12"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-misfolding-diseases---parkinsons-disease-primary"><primary style="font-size:24px"> Protein Misfolding Diseases - Parkinson’s Disease </primary></h3> <hr> <main> <ul> <li>Parkinson’s disease is associated with the misfolding and aggregation of alpha-synuclein protein.</li> <li>Misfolded alpha-synuclein forms Lewy bodies, which are pathological protein aggregates.</li> <li>Lewy bodies disrupt normal cellular processes, leading to the death of dopamine-producing neurons.</li> <li>The exact causes of alpha-synuclein misfolding and aggregation in Parkinson’s disease are not fully understood.</li> <li>Developing therapies to prevent or reduce alpha-synuclein aggregation is an active area of research.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Folding - Energy Landscapes $\rightarrow$ Protein Misfolding Diseases - Alzheimer's Disease $\rightarrow$ <span style = "color:blue"> Protein Misfolding Diseases - Parkinson's Disease </span> $\rightarrow$ Protein Misfolding Diseases - Prion Diseases $\rightarrow$ Protein Engineering - Introduction </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-13"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-misfolding-diseases---prion-diseases-primary"><primary style="font-size:24px"> Protein Misfolding Diseases - Prion Diseases </primary></h3> <hr> <main> <ul> <li>Prion diseases are caused by the misfolding of normal prion protein (PrPC) into an infectious, disease-causing form (PrPSc).</li> <li>PrPSc acts as a template and induces the conversion of PrPC into the disease-causing form.</li> <li>Prion diseases can be inherited, acquired through exposure to infected tissues, or sporadic.</li> <li>Examples of prion diseases include Creutzfeldt-Jakob disease and mad cow disease (bovine spongiform encephalopathy).</li> <li>Understanding the structural changes during prion conversion is crucial for developing therapies.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Misfolding Diseases - Alzheimer's Disease $\rightarrow$ Protein Misfolding Diseases - Parkinson's Disease $\rightarrow$ <span style = "color:blue"> Protein Misfolding Diseases - Prion Diseases </span> $\rightarrow$ Protein Engineering - Introduction $\rightarrow$ Protein Engineering - Directed Evolution </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-14"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-engineering---introduction-primary"><primary style="font-size:24px"> Protein Engineering - Introduction </primary></h3> <hr> <main> <ul> <li>Protein engineering involves modifying or designing proteins to improve their properties or create new functionalities.</li> <li>Rational protein engineering uses knowledge of protein structure and function to guide modifications.</li> <li>Directed evolution employs iterative cycles of mutation and selection to generate desired proteins.</li> <li>Protein engineering has wide applications, including biocatalysis, biotechnology, and medicine.</li> <li>Examples of engineered proteins include enzymes with enhanced activity, therapeutics with improved efficacy, and biosensors.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Misfolding Diseases - Parkinson's Disease $\rightarrow$ Protein Misfolding Diseases - Prion Diseases $\rightarrow$ <span style = "color:blue"> Protein Engineering - Introduction </span> $\rightarrow$ Protein Engineering - Directed Evolution $\rightarrow$ Protein Engineering - Rational Design </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-15"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-engineering---directed-evolution-primary"><primary style="font-size:24px"> Protein Engineering - Directed Evolution </primary></h3> <hr> <main> <ul> <li>Directed evolution involves creating diverse libraries of protein variants through mutagenesis.</li> <li>The variants are subjected to a selection process to identify those with desired traits.</li> <li>Selection methods can be based on functional activity, affinity, stability, or other desired properties.</li> <li>The selected proteins are then subjected to iterative cycles of mutation and selection to further improve desired traits.</li> <li>Directed evolution has been successfully used to generate enzymes with altered substrate specificities and improved stability.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Misfolding Diseases - Prion Diseases $\rightarrow$ Protein Engineering - Introduction $\rightarrow$ <span style = "color:blue"> Protein Engineering - Directed Evolution </span> $\rightarrow$ Protein Engineering - Rational Design $\rightarrow$ Protein Engineering - Applications </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-16"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-engineering---rational-design-primary"><primary style="font-size:24px"> Protein Engineering - Rational Design </primary></h3> <hr> <main> <ul> <li>Rational protein engineering uses computational methods to guide modifications based on structural and functional information.</li> <li>Protein structure prediction techniques help identify regions that can be modified without disrupting overall structure.</li> <li>Protein modeling and molecular dynamics simulations can predict the effects of mutations or modifications on protein function and stability.</li> <li>Rational design can be used to engineer binding sites, alter enzymatic activities, or introduce novel functions.</li> <li>Combining rational design with experimental validation allows for the development of improved protein variants.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Engineering - Introduction $\rightarrow$ Protein Engineering - Directed Evolution $\rightarrow$ <span style = "color:blue"> Protein Engineering - Rational Design </span> $\rightarrow$ Protein Engineering - Applications $\rightarrow$ Protein Engineering - Examples </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-17"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-engineering---applications-primary"><primary style="font-size:24px"> Protein Engineering - Applications </primary></h3> <hr> <main> <ul> <li>Protein engineering has diverse applications in various fields.</li> <li>In biocatalysis, engineered enzymes are used to carry out specific chemical reactions efficiently.</li> <li>In biotechnology, proteins are engineered for use in industrial processes, such as manufacturing biofuels or pharmaceuticals.</li> <li>In medicine, engineered proteins can serve as therapeutics, diagnostics, or targets for drug development.</li> <li>Protein engineering is also essential for creating biosensors, biomaterials, and nanodevices with tailored properties.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Engineering - Directed Evolution $\rightarrow$ Protein Engineering - Rational Design $\rightarrow$ <span style = "color:blue"> Protein Engineering - Applications </span> $\rightarrow$ Protein Engineering - Examples $\rightarrow$ Protein Structure - Quaternary Structure </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-18"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-engineering---examples-primary"><primary style="font-size:24px"> Protein Engineering - Examples </primary></h3> <hr> <main> <ul> <li><strong>Engineering antibody therapeutics</strong>: Antibodies can be engineered for improved affinity, specificity, or stability.</li> <li><strong>Enzyme engineering</strong>: Enzymes can be engineered to catalyze reactions not found in nature or to increase their activity.</li> <li><strong>Protein-based materials</strong>: Proteins can be engineered to assemble into nanostructures with specific properties for drug delivery or tissue engineering applications.</li> <li><strong>Cell targeting and imaging</strong>: Proteins can be engineered to specifically bind to target cells or used as imaging agents in diagnostics.</li> <li><strong>Synthetic biology</strong>: Proteins can be designed and engineered to perform new functions, such as generating renewable materials or producing biofuels.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Engineering - Rational Design $\rightarrow$ Protein Engineering - Applications $\rightarrow$ <span style = "color:blue"> Protein Engineering - Examples </span> $\rightarrow$ Protein Structure - Quaternary Structure $\rightarrow$ Protein Structure - Post-translational Modifications </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-19"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-structure---quaternary-structure-primary"><primary style="font-size:24px"> Protein Structure - Quaternary Structure </primary></h3> <hr> <main> <ul> <li>Quaternary structure refers to the arrangement of multiple protein subunits to form a functional protein complex.</li> <li>Protein complexes can be formed by identical or different subunits.</li> <li>Non-covalent interactions between subunits stabilize the quaternary structure.</li> <li>Examples of proteins with quaternary structure include hemoglobin and DNA polymerase.</li> <li>Quaternary structure is essential for the function and regulation of many proteins.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Engineering - Applications $\rightarrow$ Protein Engineering - Examples $\rightarrow$ <span style = "color:blue"> Protein Structure - Quaternary Structure </span> $\rightarrow$ Protein Structure - Post-translational Modifications $\rightarrow$ Carbohydrates - Structure and Function </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-20"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-protein-structure---post-translational-modifications-primary"><primary style="font-size:24px"> Protein Structure - Post-translational Modifications </primary></h3> <hr> <main> <ul> <li>Post-translational modifications (PTMs) are chemical modifications that occur after protein synthesis.</li> <li>PTMs can affect protein structure, stability, activity, and localization.</li> <li>Common PTMs include phosphorylation, glycosylation, acetylation, and ubiquitination.</li> <li>PTMs can regulate protein function, signal transduction, and protein-protein interactions.</li> <li>Dysregulation of PTMs is associated with various diseases, including cancer and neurodegenerative disorders.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Engineering - Examples $\rightarrow$ Protein Structure - Quaternary Structure $\rightarrow$ <span style = "color:blue"> Protein Structure - Post-translational Modifications </span> $\rightarrow$ Carbohydrates - Structure and Function $\rightarrow$ Lipids - Structure and Function </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-21"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-carbohydrates---structure-and-function-primary"><primary style="font-size:24px"> Carbohydrates - Structure and Function </primary></h3> <hr> <main> <ul> <li>Carbohydrates are organic compounds composed of carbon, hydrogen, and oxygen.</li> <li>They are classified as monosaccharides, disaccharides, or polysaccharides.</li> <li>Monosaccharides are the basic building blocks of carbohydrates.</li> <li>Disaccharides are formed by the joining of two monosaccharide units.</li> <li>Polysaccharides are long chains of monosaccharides and serve as storage or structural molecules.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Structure - Quaternary Structure $\rightarrow$ Protein Structure - Post-translational Modifications $\rightarrow$ <span style = "color:blue"> Carbohydrates - Structure and Function </span> $\rightarrow$ Lipids - Structure and Function $\rightarrow$ Nucleic Acids - Structure and Function </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-22"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-lipids---structure-and-function-primary"><primary style="font-size:24px"> Lipids - Structure and Function </primary></h3> <hr> <main> <ul> <li>Lipids are a diverse group of hydrophobic molecules.</li> <li>They include fats, oils, phospholipids, and steroids.</li> <li>Fats and oils are triglycerides, composed of glycerol and fatty acids.</li> <li>Phospholipids are major components of cell membranes.</li> <li>Steroids, such as cholesterol, serve as signaling molecules and are precursors of hormones.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Protein Structure - Post-translational Modifications $\rightarrow$ Carbohydrates - Structure and Function $\rightarrow$ <span style = "color:blue"> Lipids - Structure and Function </span> $\rightarrow$ Nucleic Acids - Structure and Function $\rightarrow$ Monosaccharides - Structure and Classification </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-23"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-nucleic-acids---structure-and-function-primary"><primary style="font-size:24px"> Nucleic Acids - Structure and Function </primary></h3> <hr> <main> <ul> <li>Nucleic acids are macromolecules that store and transmit genetic information.</li> <li>They include DNA (deoxyribonucleic acid) and RNA (ribonucleic acid).</li> <li>Nucleic acids are composed of nucleotide monomers.</li> <li>Each nucleotide consists of a sugar (deoxyribose or ribose), a phosphate group, and a nitrogenous base.</li> <li>DNA carries the genetic code, while RNA plays various roles in gene expression and protein synthesis.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Carbohydrates - Structure and Function $\rightarrow$ Lipids - Structure and Function $\rightarrow$ <span style = "color:blue"> Nucleic Acids - Structure and Function </span> $\rightarrow$ Monosaccharides - Structure and Classification $\rightarrow$ Monosaccharides - Glycosidic Linkage </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-24"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-monosaccharides---structure-and-classification-primary"><primary style="font-size:24px"> Monosaccharides - Structure and Classification </primary></h3> <hr> <main> <ul> <li>Monosaccharides are simple sugars with the formula (CH2O)n.</li> <li>They are classified based on the number of carbon atoms in the molecule.</li> <li>Example monosaccharides include glucose (6 carbons), fructose (6 carbons), and ribose (5 carbons).</li> <li>Monosaccharides can exist in linear or cyclic forms due to the presence of an aldehyde or ketone functional group.</li> <li>Monosaccharides can also differ in their stereochemistry, giving rise to different sugar isomers.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Lipids - Structure and Function $\rightarrow$ Nucleic Acids - Structure and Function $\rightarrow$ <span style = "color:blue"> Monosaccharides - Structure and Classification </span> $\rightarrow$ Monosaccharides - Glycosidic Linkage $\rightarrow$ Polysaccharides - Starch and Glycogen </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-25"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-monosaccharides---glycosidic-linkage-primary"><primary style="font-size:24px"> Monosaccharides - Glycosidic Linkage </primary></h3> <hr> <main> <ul> <li>Monosaccharides can combine to form disaccharides or polysaccharides through glycosidic linkages.</li> <li>A glycosidic linkage is formed when the hydroxyl group of one sugar reacts with the anomeric carbon of another sugar.</li> <li>Disaccharides, such as sucrose and lactose, are formed by the joining of two monosaccharides.</li> <li>Polysaccharides, such as starch and cellulose, are long chains of monosaccharides linked by glycosidic bonds.</li> <li>The type of glycosidic linkage determines the stability and function of the resulting disaccharide or polysaccharide.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Nucleic Acids - Structure and Function $\rightarrow$ Monosaccharides - Structure and Classification $\rightarrow$ <span style = "color:blue"> Monosaccharides - Glycosidic Linkage </span> $\rightarrow$ Polysaccharides - Starch and Glycogen $\rightarrow$ Polysaccharides - Cellulose and Chitin </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-26"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-polysaccharides---starch-and-glycogen-primary"><primary style="font-size:24px"> Polysaccharides - Starch and Glycogen </primary></h3> <hr> <main> <ul> <li>Starch and glycogen are storage polysaccharides found in plants and animals, respectively.</li> <li><strong>Starch consists of two components</strong>: amylose (a linear polymer) and amylopectin (a branched polymer).</li> <li>Glycogen is highly branched, allowing for efficient storage of glucose units.</li> <li>Both starch and glycogen can be hydrolyzed to release glucose for energy production.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Monosaccharides - Structure and Classification $\rightarrow$ Monosaccharides - Glycosidic Linkage $\rightarrow$ <span style = "color:blue"> Polysaccharides - Starch and Glycogen </span> $\rightarrow$ Polysaccharides - Cellulose and Chitin $\rightarrow$ Lipids - Fatty Acids </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-27"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-polysaccharides---cellulose-and-chitin-primary"><primary style="font-size:24px"> Polysaccharides - Cellulose and Chitin </primary></h3> <hr> <main> <ul> <li>Cellulose is a structural polysaccharide found in the cell walls of plants.</li> <li>It is composed of long chains of glucose units linked by beta-1,4 glycosidic bonds.</li> <li>Cellulose provides rigidity and strength to plant cell walls.</li> <li>Chitin is a structural polysaccharide found in the exoskeletons of arthropods and the cell walls of fungi.</li> <li>It is composed of N-acetylglucosamine units linked by beta-1,4 glycosidic bonds.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Monosaccharides - Glycosidic Linkage $\rightarrow$ Polysaccharides - Starch and Glycogen $\rightarrow$ <span style = "color:blue"> Polysaccharides - Cellulose and Chitin </span> $\rightarrow$ Lipids - Fatty Acids $\rightarrow$ </footer>

<h3 id="success-stylefont-size25px-biomolecules-tertiary-structure-success-28"><Success style="font-size:25px"> Biomolecules Tertiary Structure </Success></h3> <h3 id="primary-stylefont-size24px-lipids---fatty-acids-primary"><primary style="font-size:24px"> Lipids - Fatty Acids </primary></h3> <hr> <main> <ul> <li>Fatty acids are the building blocks of lipids.</li> <li>They consist of a carboxylic acid group attached to a hydrocarbon chain.</li> <li>Fatty acids can be saturated (no double bonds) or unsaturated (one or more double bonds).</li> <li>The length and degree of saturation of fatty acids determine their physical properties.</li> <li>Fatty acids serve as energy storage molecules and are important components of cell membranes.</li> </ul> </main> <hr> <footer style = "font-size: 18px">Polysaccharides - Starch and Glycogen $\rightarrow$ Polysaccharides - Cellulose and Chitin $\rightarrow$ <span style = "color:blue"> Lipids - Fatty Acids </span> $\rightarrow$ $\rightarrow$ </footer>