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Amino Acids and Peptides

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Question
Answer
only source of nitrogen in our bodies   amino acids  
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a metabolic energy source   amino acids; last resource for metabolic energy  
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amino acids are classified based on   R groups  
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the carbon in the center of the amino acid; has an amine, R group,H, and acid group attached   alpha Carbon  
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contains BOTH positive and negative charges at pH 7.4   zwitterionic  
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Amino Acids are asymmetric, except for   glycine; all others have 4 different things on chiral carbon  
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CORN   L- amino acid; COOH, R group, and NH2; COUNTING CLOCKWISE. If not in this order they are "D"  
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All 20 standard amino acids are "L" true/ false?   true; the D forms are plants and bacteria  
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antibiotics derived from bacteria with D- amino acids degrade more slowly   true  
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amino acids are broken into charged and uncharged; the 5 subclasses are?   negative and positive (charged) and polar, aromatic, and non-polar (neutral)  
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negative amino acids (2)   Aspartic; Glutamic  
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Positive Amino Acids (3)   Arginine, Histidine, and Lysine  
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Polar amino acids (5) STAGC   Serine, Threonine, Asparagine, Glutamine, Cysteine  
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Aromatic Amino acids (3) PTT   Phenylalanine, Tyrosine, Tryptophan  
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Non- polar amino acids (7) V A L G I M P   Valine, Alanine, Leucine, Glycine, Isoleucine, Methionine, Proline  
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Which amino acid is neither L or D?   Glycine; R group is a Hydrogen; no chiral structure so cannot determine CORN  
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Size/ shape of R- groups determine protein topology, form hydrophobic faces   Neutral, non-polar aliphatic amino acids  
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WHent he R group of an amino acid is attached to the amine group what happens?   It causes a kink in the protein  
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UV absorbed by this type of amino acid   Neutral aromatic; planar shape and stacking  
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Which amino acid R group is an SH   Cysteine; can be sulfur breach protein linkage  
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MUST know charged amino acids by name and structure   check PPT notes  
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an oxidized derivative of cysteine   Cystine; the disulfide S-S bond makes Cystine; free cysteine molecules bond to form cystine in the extracellular space. Once transported intot he cell cystine is reduced back to cysteine  
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The solubility of cystine decreases when pH is?   Low  
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Cystine causes disease under what conditions?   pH imbalance, precipitates in kidney  
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Characteristics of CHARGED amino acids   hydrophilic surfaces in proteins; salt bridges in proteins; acid/ base and covalent protein chemistry  
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Glucose is utilized by every cell in the body   Fat not utilized by brain or RBC's  
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NOT biosynthesized by humans, required in the diet   Essential Amino Acids  
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Tyrosine is biosynthesized from   Phenylalanine  
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Bulky Aliphatics and aromatics (except Tyrosine)   Esential amino acids  
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Short aliphatics, negative charges, amides   Non-essential; also Tyrosine  
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Semi-essential amino acids required by children and pregnant women   Histidine and Arginine  
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amino acids that are biosynthesized by humans   non-essential  
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If no Phenylalinine there is also no   Tyrosine  
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Cysteine is biosynthesized from   Methionine  
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Essential Amino Acids (8)   Iso; Leu; Lys; Meth; Phenyl; Threo; Trypto; Val  
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Recommended Daily Allowance of protein   0.8g "high quality"; contains all the essential amino acids (animal sources) milk, eggs, meat  
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Low quality protein   deficient in one or more essential amino acid (vegetable proteins)  
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High Lysine and low Arginine is used to deter   herpes outbreaks; lysine disrupts functioning of herpes because it uses high Arginine and Lysine inhibits ARginine utilization; viral replication disrupted  
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molecule that generates a second molecule   precursor  
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If asked the precursor to Epinephrine we would answer   Tyrosine; L- dopa; and Dopamine  
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Amino Acic; CNS neurotransmitter found in spinal fliud   Glycine  
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Non- standard amino acids   Hydroxylysine; HYdroxyproline: Ornithine; Citrulline; Carnitine; Creatine; Taurine; Homocysteine; NME- amino acids  
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Non-standard amino acid important for maintaining collagen structures   Hydroylysine and Hydroxyproline  
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Non- standard amino acid found in natural products from microorganisms; stabilize peptide against degradation   NMe amino acids (N-Methyl Glycine is sarcosine)  
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Non- standard amino acid; intermediates in the urea cycle   Ornithine and Citrulline  
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Non-standard amino acid; Lys derivative; fatty acid transport   Carnitine  
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Non- standard amino acid; Arg+ Gly derivative; accepts and donates phosphate group that can supply ATP in active muscle   Creatine  
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Non- standard amino acid; Cys derivative; Bile salt conjugate   Taurine  
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Non- standard; Met derivative; associated with heart disease   Homocysteine  
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Aspartic acid and Phenyl alanine=   Aspartame  
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Genetic defect of the lys-arg-orn-cystine transport protein in intestine and kidney; (1 in 2500-15000)   Cystinuria; Cysteine is not soluble; causes kidney stones. Treatment= basifying urine (acitozolamide penicillin); conjugating the cystine with drugs and lots of water  
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Genetic defect of the lysosomal cystine transport system   Cystinosis; Cystine accumulates in lysosomes causing increased cell death rates and organ failure (1 in 100,000- 200,000)  
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Genetic defect of a neutral amino acid transport protein in intestines and kidney   Hartnup disease; (1 in 24,000) Prevents proper absorption/reabsorption of these amino acids including Tryptophan (precursor of Vit B6); results in niacin deficiency and PELLAGRA  
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Genetic defect of a homocysteine- metabolizing enzyme, cystathionine synthase.   accumulation of homocysteine causes long, thin bones, lens dislocation, mental deficiencies, and HEART DISEASE. 50% respond to treatment with B6 or B12 and folic acid  
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Phenylketonuria   PKU; 1 in 15,000; inability to breakdown phenylalanine- it builds up and is toxic to brain  
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Symptoms of PKU   intellectual disability; seizures; nausea; vomiting; eczema- like rash; mousy body odor  
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what diet restriction allows normal growth for PKU?   Phenylalanine; BH4 oral can also reduce blood levels of this amino acid  
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amino acids cause the urine to smell like maple syrup; lack of amino acid metabolizing enzymes   maple syrup urine disease;Mennonite families; treatment = dialysis B1 (thiamin) injections; diet low in leucine, isoleucine, valine  
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lack of enzyme needed to metabolize tyrosine   Tyrosonemia; dysfunctional liver and kidney  
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B6, B12, and Folic acid have been shown to prevent atheroschlerotic plaque in what amino acid based disorder   Hyperhomocysteinemia; elevated blood homocysteine- not currently true that B vitamins help and hyperhomocysteinemia is not correlated to heart disease  
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pKa = -log (Ka)   no answer  
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the point of NO net charge   isoelectric point; when pH= pI there is no net charge  
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pH > pI means   negative charge  
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pH < pI means   positive charge  
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calculating pI   pK1 + pK2 divided by 2 = pI  
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how to calculate pI when 3 pKa values given   there will be 4 forms; ex: A-, A, A+, A--; the 4th form will either be 2+ or 2-  
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To determine what 4th form will be we need to know what?   If we are told the amino acid we will know whether it is positive or negative  
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Ex of 4th form with Histidine   A++__A+__A__A- ; fill in the blanks with the given pKa and use the 2 values to the right because they include a neutral A; p31 of notes  
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Low pKa= molecule likes to   release H+; requires high concentration of H+ to populate molecule with H+  
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the pKa's surrounding the neutral species are used to calculate pI   no answer p.36  
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amino acids react to form   peptide (amide) bonds  
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amino acids that make up a polymer are called   residues  
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The 1st amino's COO- binds to the 2nd amino's NH3+   H2O molecule created; H2 from amino, O from the carboxylic acid  
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Direction of free ends in naming a peptide always   N-terminal to C-terminal; -yl replaces -ine or -ate except the C terminal(last) amino acid in the sequence  
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2/3 residues   dipeptide/ tripeptide  
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A few residues   Oligo  
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many residues   polypeptide  
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a few residues with 2D or 3D shape, usually 40+   protein  
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naming example: H3N+-Gly-Asp-His-Leu-Val-Coo-   glycyl-aspartyl-hitidyl-leucyl-valine; start with the H3N side and leave the last amino acid in whole name  
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Isoelectric points are used to determine   electrophoretic mobility of amino acids, peptides, proteins, and manipulating protein solubility  
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When protein's pI= pH of solution, a protein is   least soluble  
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Ligands for opioid receptors; signal for pleasant feelings that counteract pain   Enkephalins and Endorphins; physiological peptides  
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peptide hormone; 9 amino acids (nonapeptide); released from pituitary after hypothalamus detection of lack of water   Vasopressin, or ADH; promotes water retention by kidneys and induces vasoconstriction to maintain blood pressure  
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Lack of the physiological peptide Vasopressin can lead to   diabetes Insipidus; excessive thirst and urination  
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Physiological peptide; doesn't cross blood- brain barrier; secreted from pituitary; uterine contractions   oxytocin  
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advantages of peptide drugs   specific, active,minimal drug interactions, less accumulation in other tissues, less toxicity, potent, diverse  
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disadvantages of peptide drugs   low absorption (injection often required); difficult membrane transport, costly, immunological risk, cleared from body quickly  
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