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Wgu Module 1-3

QuestionAnswer
What is codominance? When both traits and a combination of those traits are exhibited. Ex: red,red,white,red+white
What is incomplete dominance? When both traits and those traits mixed are exhibited. Ex: red,white,pink,pink
What is complete dominance? Both traits are exhibited only. Ex:red,red,white,white
Double bond between w sulphur atoms in cysteine side chains is what kind of bond? Disulfide bond
What is a hydrophobic interaction? An interaction between R groups od hydrophobic amino acids.
Amino acids are linked together by what specific type of bond? Peptide bond
What is a single protein chain consisting of several amino acids bonded by peptide bonds? Polypeptide
Sequence of amino acids in a polypeptide? Primary structure
Spatial arrangement of 2 or more individual polypeptide chains known as subunits? Quarternary structure
Electrostatic interaction between two ionic groups of opposite charge is what? Ionic interactions
Local spatial arrangement of polypeptide backbone atoms with out regard to confirmations of its side chains? Secondary structure
Single polypeptide chain that is part of a protein with quarternary structure? Subunit
Primary structure has what type of bond? Peptide bonds
What secondary structure shapes and what bond stabilizes structure? A he lives and beta sheets with hydrogen bonds
What type of bonds or interactions are susceptible to temperature changes? Hydrophobic bonds
Carrier parents with both genders equally effected? Autosomal recessive
Carrier parents with only males effected? Sex liked recessive
Recessive diseases are inherited when a person inherits what? 2 copies one from each carrier parent.
A person that is a carrier of A recessive trait has what? One copy of the recessive trait unless make and recessive trait is on the x chromosome??
Describe hemoglobin and what it does. Delivers oxygen to the lungs and tissues. Exists in the R state-planar-red color-oxygenated state,dark purple color- T state-deoxygenated. Contains a heme group w/iron atom positioned in middle of the structure.
Primary structure Stringing of amino acids of peptide bonds
Peptide backbone causes shape pleated sheet a helices & hydrogen bond causes shape. Secondary structure
Tertiary structure R groups added, folds back on self to R-R interactions- twists,bends,kinks-all types of bonds
Contains one polypeptide chain called subunit each (subunit) chain have there own tertiary structure,chains interact via R group interactions. Quarternary structure
Hydrolysis Water is added to break down bond
Dehydration Water is removed to build a peptide bond between amino acids
What amino acids will not cross blood brain barrier? Polar
What types of amino acid is easily cross blood brain barrier? Hydrophobic
What group is always interior in tertiary structure,away from water and hydrophobic interactions to exclude water? Hydrophobic-non polar
Cysteine Polar-hydrogen bond,disulfide bridges which are strong covalent bond. Found in proteins -skin,hair,nails
Charged Have negative & positive groups & charge, can from ionic bonds, If mutated one would repel each other & disrupt tertiary structure
Polar Hydrophilic uncharged R group from hydrogen bonds & If mutated interaction would be disrupted & tertiary structure affected.
Nurture that affects nature environmental factors that affect DNA, inheritance no change to nucleotides but to structure of nucleosomes. Can increase and decrease gene expressions. Epigentics
Proteins that read promoter region & signal RNA polymerase to synthesis Transcription factors
Proteins promote cooling of DNA & prevent tangling Histones
Histone & dsDNA Nucleosome
NH+3 Amino group
COO- Carboxyl group
Can't bind with polar but is not hydrophobic or charged. Glycine
-H Glycine
What bond has a R group with a negative or positive at the end Charged bond
What bond has a R group that has a. -OH & -NH on the end? Polar
What bond has a -SH at the end of the group? Polar -cysteine
In hemoglobin CO (carbon monoxide) stabilizes the __ state? Relaxed state
I'm hemoglobin 2,3-BPG stabilizes the ___ state? Tense state
In hemoglobin +H stabilizes the ___ state? Tense state
What increases in pregnant woman so increased o2 goes to the baby? Tense state
How does hemoglobin bind to oxygen? Quarternary structure when bonds to oxygen causes a shift to tertiary structure. When oxygen binds it will shift from T state to R state and encourages the 2nd,3rd,4th.
Template strand of DNA is 5-3 mRNA 3-5 how is mRNA read to determine codons? Flip mRNA to run 5-3
What is used to separate strands and create mRNA strand for mRNA? RNA polymerase
What is on the 5' end and what is on the 3' end? 5-phosphate. 3-sugar
DNA is made up of? Phosphate,base AGCT and deoxyribose sugar
Amino acid proteins include what? Carboxyl group,amino group & R chain/side chain
Enzyme and bond is determined by what? R chain/side chain
Damage to a single nucleotide,DNA repair enzyme removes base,DNA polymerase inserts new base,DNA ligase repairs nick (backbone) Base excision repair
Damage to small number of bases,DNA repair enzyme cuts out damaged area, DNA polymerase will fill in DNA ligands deals Nick in backbone. Nucleotide Excision Repair
Broken ends of DNA are glued together with out regard for sequence (last resort) Non-homologous repair
Info from intact strand of DNA provides needed sequence to repair damage. Homologous repair
RNA is produced in what direction? 5'-3' new strand 3'-5' template strand
To determine amino acid of a tRNA strand must write in what direction? 5'-3'--If written in 3'-5' must invert
What is mRNA into amino acid using mRNA as template for tRNA using base pairing and three nucleotides code for a particular codon? Translation
Where does translation occur? In ribosome and cytoplasm
Females get what chromosome from mom & dad? XX
Makes get what chromosome for mom & dad? X mom Y dad
What type of structures do amino acids come in? Primary,secondary,tertiary and quarternary
Structure name,shape and bond? Primary-linear-peptide:secondary-A helixs,Beta sheets,random coil-hydrogen bond:Tertiary-held together by R groups-hydrophobic-charged-Polar, hydrophobic-weak bond-contributes most of the structures stability found in interior of protein.
In what ways can we target enzymes? Modify diet,enzyme therapy,drugs increase substrate of enzyme
In what disease does a excess of mucus enzyme cause? Cystic fibrosis
Dominant trait has ____ parents? No carrier parents
Effected male parent and all daughters? Sex liked dominent
What is polymerase chain reaction? Genetic testing
PCR- includes what structures? Template DNA, Nucleotides,DNA primer,DNA polymerase
Steps involved in PCR? 1st-Denaturation , 2nd Annealing , 3rd Elongation
DNA primer in PCR does what? Book ends gene that is getting looked at and gives polymerase help starting.
Polymerase in PCR does what? Copies DNA
How much product is produced after each cycle of PCR? 2 molecules 1st round and doubles each round.little product means no mutation ,large amount means mutation present.
What can cause imbalance of molecules in a pathway leading To disease? Defective or absent enzyme ex: parkinsons,cystic fibrosis
Enzyme activity is what leading to disease or inhibition of an enzyme can improve a condition? Activity is increased. Ex: erectile dysfunction
What type of bond can be broken by heat? Hydrophobic
What bond can be broken by salt concentration or ph? Hydrogen & ionic
What bond is strong and can be broken by a chemical? Disulfide bond
One nucleotide (letter) changed and now codes for stop codon. Nonsense
Single nucleotide changed and changes the protein made? Missense
Change a single nucleotide(letter) Point mutations
One nucleotide changed but same amino acid is coded Silent
DNA copies using 5'-3' (non coding) template strand with complementary base pairing Replication
DNA into mRNA using antiparelle base pairing exchanging T in DNA for U in mRNA Transcription
Every one has a carboxyl group,amino group and a R group/side chain Amino acid
Only have to inherit one copy of bad gene to show the disease. Dominant disease
R chain ends in CH Hydrophobic bond
What part of the amino acid determines the type? R chain/side chain
Heat DNA to 95c which separates strands Denaturation
Cooled to 50c,primer sticks to region of DNA copied , primer provides 3' prime end for DNA polymerase Annealing
70c enables DNA polymerase to copy nucleotides to make new strands of DNA Elongation
Adding of 2 nucleotides in DNA which disrupts mRNA & protein made. Insertion
Removal of 2 nucleotides disrupts mRNA and protein made. Deletion
PCR techniques to repair mutations Make primers that flank to mutations & sequence products, make primers that stick (anneal) to the mutation.
1/2 female carriers,1/2 female healthy,1/2 male healthy,1/2 male carriers Sex linked recessive
PCR little product produced means__ mutation a lot means __ mutation. Little,alot
What happens with out NER enzyme? Mutations accumulate since not being fixed proteins that keep cell division in check are damaged and can lead to cancer.
Causes of mutations? X Rays,carcinogens, RNA polymerase
Proofreading/Mismatch repair Mistake in DNA replication. DNA repair enzyme recognizes mistake,DNA polymerase removes in correct base by back tracking and removing one. Ligands deals remaining nick.
Uncontrolled cell divison? Cancer
Repairs mutations? NER
Stores oxygen in muscle cells. 1 subunit,1 polypeptide chain binds to 1 oxygen molecule in low concentrations & only releases when oxygen levels are low. Myoglobin
Delivers oxygen by picking up in lungs and delivers to tissue. 4 subunits and each binds to one oxygen molecule. Hemoglobin
R group ends in -OH & -NH Polar
R group Ends in -SH Cysteine -disulfide bond
+ or - at the end of the R group Charged -Ionic bond
R group Ends in CH Hydrophobic
Both parents unaffected with affected children? Carrier parents
Both parents affected can have unaffected children? Autosomal dominant
Created by: Emilyramos
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