Amino Acids Notes: Week 1 PDF

- Amino acids Describe the Basie structure of amino acids and categorize them based on R group & Each amino acid has a carboxyl group, a primary amino group, and a distinctive side chain (R group) bonded to the α-carbon atom...

- Amino acids Describe the Basie structure of amino acids and categorize them based on R group & Each amino acid has a carboxyl group, a primary amino group, and a distinctive side chain (R group) bonded to the α-carbon atom Polar Non-polar Acidic Basic  Amino acids. Isomers Non-polar Cannot gain or lose a proton and do not become charged- hydrophobic characteristics Chiral-α-carbon of an amino acid is attached to four different..chemical groups, it is an asymmetric D & L: = mirror images of enantioners Polar Enantiomers are optically active. If an isomer, either D or L, causes the Can create hydrogen & iconic Bonds & is hydrophilic plane of polarized light to rotate clockwise, it is designated the (+) form. Uncharged polar side chains all a.a found in body are L - for living Can all form hydrogen bonds except cystine' Acidic Able to let go of hydrogen ion in dissociation Basic Accepts hydrogen ion Acidic + basic properties Equations T Henderson hasselbach - tells as how well AMINO ACID is able to dissociates + give up its proton+ act as on acid pH = log 1/[H+] or –log [H+]. Acids = proton donors. Bases = proton acceptors. - Buffers concentration of protons ([H+]) in aqueous solution is expressed as pH Buffer = solution that resists changes pH follower the addition of an acid or base. release of a proton by a weak acid represented by HA: Max buffering capacity y= ph= to the PKA. A =ionized form of a weak acid > Larger the ka, strange the acid  peptide Bond Aneiro Acids iM ↓ NT I dipeptide) I C carbon Classifications & , / - Amine/ acidic If highlighted in blue = non-polar Non-polar. Carboxyl/ acidic Bot Alanine (negative ) (positive) ⑪ Glycine Aspartic ACID 7 Total neg charge Arginine Other Asparagine Isoleucine = -2 Amine JNST -1 Histidine Cysteine (disulfide bunds) = Glutamic ACID Leucine Must be obtained from & pH 7 4 Lysine Glutamine · the diet Methionine Hydroxyl Aromatic. Need to Live Selenocysteine · Can be synthesized by the body, can survive COO NHst Serine wout , Proline Tantot Phenylalanine Notes Pyrrolysine. Valine Threonine Tryptophan Asymmetric ~ · Center & Alpha C Allows P or DtLisomers tyrosine,. Most biological A A exist L-configuration Tyrosine ·. in 1) Learning obj. 1-describe AMINO acids and categorize them Change · in pH - changes charge A A bonds - · > peptide bonds based on r-group. · If double bond In protein nomenclature ↳ Use Sis/ Trans * same Opp. 2) - & StabilizingForces Discuss the main forces that stabilize protein Explain the 4 levels of protein structure A-bond : stabilizing secondary tertiary structures structures. & Identify common secondary structure elements Disulfide Bonds-Cordent bonds that provide additional stability tertiary structures Explain the basic concept op protein folding in Hydrophobic Interactions Non-polar side chains - Aggregate to avoid water Levels of Structure: (Protein) Contributing to folding * and factors that can lead to denaturalization donic Interactions Electrostatic attractions blween charged Primary A A Sequence peptide bonds - Side chains stabilize protein structure How Protein Structure : determined mRNA translation, begins & amine end by Denaturation Factors. , , enominates e Carboxy Secondary : Localized structures like Alpha helicest Beta sheets (L-R) Protein Folding Heat : disrupts H-bonds + ↑ molec motion Relates to funct. => Formed thrn H-BONDS Affects · hydrophobicness folding Process Proteins fold pH Changes : Alters charge tionic Interactions Affecting STABILITY Tertiary Punct. > - Overall 3D shape Stabilized by : shapes driven by energetics +interactions among AA 3-D shape directly dictates · : long-range interactions deals wi polds +turns into Specific 3-D ↳ , Detergents disrupts hydrophobic Interactions, leading to unfolding shape determines how it'll interact Chaperonins : Quaternary Assembly w/ other molec ->. Assist of multiple poly peptide chains /iP Applicable) : in proper folding by providing an environment 4 hydrophobic sequences Reducing Agents Exemplified by enzymes that catalyze : breaks disulfide bonds destabilizing the protein · : , Proteasomes Degradation to biochemica rxns or structural proteins : digopeptides of about 8A A each. Chelators : bind metal dons essential 4 structural Integrity causingdistability , that provide support Mercaptoethano/dithiothreitol- break disulfide bonds Explain the concept a post-translational Discuss the relationship between protein modifications and their significance misfolding and certain diseases Post-Translational - Chemical Changes the Modifications occur to proteins Intrinsically Disordered Proteins · S Shove regisfavoringdisdePresidue Metamorphic Proteins After their synthesis impacting , their function , · Rich in polar A A +proline · May adapt morethan / stable structure stability & Activity - , · May favor being modified Definition : PTMs refer to the covalent alteration madeto proteins following translation · Non-IDP-more involved in catalysis + transport · Lymphotactin - monomeric receptor. · IDPs b more Involved may in signaling tregulation Types : phosphorylation glycosylation Ubiquitination , , , ect. functional Regulation activate or deactivate enzymes , Alter Amyloids & Diseases : can protein Interactions t Influenc allular localization , Disease Association : Abnormalities In PMTs rlinked to various diseases Definition: Collection of Improperly folded protein Aggregates found in the human body - phosphorylated A A When misfolded thyr ansoluble t contribute to some 20 human diseases Andudy , Import Neurological Is Involving prions. ↳ Adding. or removing can Turn DNA Off Alzheimer's disease (Amyloid B) ~ S on or · · Parkinson's disease (a-synuclein) Significance: · Huntington's disease /huntingtin) ◦ Functional Regulation: PTMs can activate or deactivate enzymes, alter · Rheumatoid Arthritis /Serum Amyloid A) protein-protein interactions, and influence cellular localization. · Fatal Familial Insomnia (P PS)). ◦ Protein Stability: They contribute to the stability and lifespa nof proteins within cells. ◦ Cellular Signaling: PTMs play critical roles in signaling pathways, influencing responses to environmental stimuli. ◦ Disease Association: Abnormalities in PTMs are linked to various diseases, including cancer and neurodegenerative disorders  Nutrition Vitamins & Minerals , , Question : Fat in In regard to Macronutrients Second Does Lecture Chapter 27-29 or Micro-Vitamins MICRO-NUTRIENTS MACRONUTRIENTS Definition nutrients needed fats Fatty Acid Examples : & : in small amounts Definition : nutrients neededIn large amounts - Omega-3 Concentrated · functions : provide energy source · function: Essential 4 norm health ; DO NOT provide energy energy a building blocks ↳ PKcal/gram ↳ Cold Water fish 4 bodily functions · supply essential fatty Acids (chodutobot + fat-souble vitamins lipids Types # role structural gain in mem · ; ↳ RDA weight 65g saturated 20 gr : causes Essential : /indeis , :. · Omega-6 - , corn syrup Types proteins + Carbohydrates - - > Minerals · : linolenic And (w ↳ Effects : bplasma 6 : z -3) &Carbohydratesa - me s Vitamins phospholipido 4 miem structure · provid (22) · Excess : e (provid Obesity , heart diseas ↳ sources: Nuts Avocados Water soluble (B P Major : calc , potassium magnesium , , Olives , Soybeans Oils , fats ans , , as stored Complex : fat soluble (ADE k) Trace : dron New concept , iodine simple dairy fish leay ge as Zinc , liver liver · in , : , , , Not found in plants Sucrose ,fructose · whole grains wheat, starch lactose , pasta , Found based goods Functions: essential 4 various bodilyfunct functions Important bostructurea , · · in. ↳ Immune response , bone health tiron absorption Protein , Sparing Effect &portance Sources: Meat, Sources : Fruits Veg , dairy , meets,I fortified diary , nuts , seeds fruits Veg of Proteins ,