Term
who coined the term molecular biology? when? |
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Definition
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when was the double helix structure discovered? who? |
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Definition
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when was dna first isolated? who? what was it called? |
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what is the length of the E.coli genome? what form does it take? |
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Definition
single, circular chromosome. 4000kb |
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Term
how many genes in E.coli genome? |
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Definition
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Term
how many genes in the human genome? |
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Definition
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Term
what are the 4 stages of bacterial growth? |
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Definition
lag, log, stationary, death |
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Term
what causes stationary phase? |
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Definition
death rate = growth rate -nutrients being depleted bacteria waste accumulating |
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Term
what formula used to determine # of bactteria at certain time? |
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Definition
# cells = starting # x 2^n n = number of generations |
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Term
what is an operon? who discovered? |
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Definition
genetic control system of a particular gene. jacques monod |
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Term
how many chromosomes do yeasts have? |
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Definition
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Term
what is the generation time of S.cerevisiae? |
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Definition
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Term
what was the first eukaryotic org. to have genome completely sequenced? when? |
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Definition
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Term
what is the diff. between introns and exons? |
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Definition
exons - code for aa introns - don't code for aa |
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Term
ho much of yeast genome is introns? |
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Definition
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Term
how many genes in yeast genome? |
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Definition
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Term
what does the root of enzyme mean? |
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Definition
'en - zyme' = 'in yeast', first enzyme studies done with yeasts |
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Term
what species of nematode is considerd a model genetic organism? |
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Definition
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Term
how is C.elegans capable of producing clones? |
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Definition
worms are bisexual, can self-fertilize |
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Term
what is the life cycle of C.elegans? maturity time from egg? |
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Definition
maturity - 3 days life cycle - 2-3 weeks |
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Term
what is unusual about the cellular structure of C.elegans? |
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Definition
adults have exactly 959 cells |
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Term
what organism is ideal for studying life span, aging processes, and development? |
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Definition
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Term
what is apoptis? what organism was this first discovered in? |
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Definition
apoptis - programmed cell death C. elegans |
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Term
what is the scientific name for fruit fly? |
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Definition
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Term
how many chromosmes in fruit fly? |
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Definition
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Term
how many genes in fruit fly? |
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Term
what is the scientific name for zebra fish? |
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Term
why is D.rerio useful for development studies? |
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Definition
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Term
how many chromosomes does D.rerio have? |
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Definition
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Term
how homologous is D.rerio with the human genome? |
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Definition
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Term
what is the scientific name for mouse? |
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Definition
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Term
what is the lifespan and development time of the mouse? |
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Definition
lifespan 1-3 yrs sexually mature i 4 weeks |
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Term
how many chromosomes does M.musculus have? |
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Definition
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Term
how many genes does M.musculus have? |
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Definition
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Term
how many introns per gene in fruit fly? |
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Definition
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Term
how many introns per gene in mouse? |
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Definition
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Term
how homologous to human genome is the mouse? |
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Definition
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Term
what is the model genetic organism for plants? |
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Definition
Arabidopsis thaliana - mouse cress or mustard weed |
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Term
what is the lifecycle of A.thaliana? |
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Definition
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Term
how many chromosomes in A.thaliana? |
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Definition
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Term
how many genes does A.thaliana have? |
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Definition
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Term
what are the subcellular genetic elements? |
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Definition
virus viroid plasmid transposon prions |
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Term
what are the three types of viruses? |
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Definition
DNA virus RNA virus retrovirus |
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Term
how does a retrovirus work? |
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Definition
RNA injected, host synthesizes DNA from RNA |
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Term
what enzyme isolated from retroviruses? how is it used in molecular biology? |
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Definition
reverse transcriptase enzyme used to synthesize a gene from RNA |
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Term
what are the properties of a viroid? |
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Definition
1.naked (not protein coat) 2.self-replicating 3.circular RNA 4.not associate w/any proteins |
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Term
why do viroids have a rod shape? |
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Definition
complementary base pair regions |
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Term
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Definition
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Term
what is naked, self-replicating, circular DNA? |
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Definition
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Term
how is a plasmid diff. than a viroid? |
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Definition
viroid - 1.RNA 2.destroys cells 3.does not encode for any proteins |
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Term
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Definition
a transposable segment of DNA that can move as a unit from one location to another |
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Term
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Definition
a misfolded version of a normal nerve cell protein |
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Term
what are the main functions of proteins? |
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Definition
1.enzymes 2.structural 3.transporters 4.receptors 5.make up soem hormones |
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Definition
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Definition
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Term
how does a peptide bond form? |
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Definition
COOH (aa1) + NH2 (aa2) = C-N + H20 |
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Term
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Definition
chain of aa with 15+ peptide bonds |
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Term
how does a peptide bond affect the 3D shape of a protein? |
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Definition
has 'double bond' character. cannot rotate freely |
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Term
what is the size of a typical protein? |
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Definition
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Term
what is the molecular weight of a typical protein? |
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Definition
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Term
what is the moliecular weight of an average nucleic acid? |
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Definition
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Term
what is the length of an average polypeptide chain unfolded? folded? |
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Definition
0.1-0.5 microns 0.004-0.008 microns |
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Term
what type of proteins are water soluble? water insoluble? |
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Definition
soluble - globular proteins insoluble - fibrous |
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Term
what are some examples of fibrous proteins? |
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Definition
silk, keratin, collagen, fibrinogen |
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Term
what is the primary structure of a protein? |
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Definition
the linear sequence of aa |
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Term
what is responsible for the secondary structure of proteins? |
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Definition
hydrogen bonds and repeating conformations (alpha-helices and beta-sheets) |
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Term
explain the hydrogen bonding in the secondary structure of proteins. |
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Definition
the O in the carbonyl (C=O) bond of one peptied bond bonds with the H in the amide (N-H) of another peptide bond. occurs between every 4th peptide bond |
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Term
what direction is an alpha helix rotated? where are the side chains? |
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Definition
right handed helix side chains facing out |
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Term
which aa prevents formation of the alpha helix conformation? why? |
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Definition
proline - ring causes steric interference. amide is part of ring, no H available for hydrogen bonding (the one H would be used in peptide bond) |
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Term
which aa destabilizes the alpha helix conformation? why? |
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Definition
Glycine. b/c sidechain (H) freely rotates, very unconstrained |
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Term
what aas are considered good alpha helix formers? |
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Definition
(MEAL) - methionine, glutamic acid, alanine, leucine |
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Term
why would an arginine - lysine bond disrupt an alpha helix? |
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Definition
consecutive like charges cause repulsion greater than strength of H-bond |
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Term
explain why a chain of glutamic acid would only form an alpha helix at low pH? |
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Definition
high pH - high OH - OH would pull H off of carboxlic acid (on both ends of glutaic acid), leaving COO-. consecutive negative charges would repel helix formation |
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Term
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Definition
a molecule that has both + and - formal charges but is neutral overall |
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Term
what is the name for stable, flexible, non-repetitive regions of polypeptide chains? |
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Definition
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Term
what aa often form random coils? |
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Definition
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Term
how are side chains positioned in a beta-sheet? |
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Definition
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Term
how many strands make up a beta sheet? |
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Definition
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Term
which is more stable, parallel or antiparallel beta sheet? |
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Definition
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Term
what are the three beta sheet conformations? |
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Definition
1. flat rectangular 2.Twisted sheet 3.beta-barrel |
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Term
what is the tertiary structure? |
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Definition
the overall folding of the polypeptide in condensed shape |
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Term
what causes tertiary structure? |
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Definition
interactions between side chains |
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Term
what often causes quaternary structure? |
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Definition
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Term
what is the diff. between fibrous and globular proteins in regards to secondary structure? |
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Definition
globular - short, interspersed helices and sheets fibrous - long, uninterrupted helices and sheets |
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Term
what structure do most proteins exhibit? |
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Definition
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Term
what is an example of a protein that only has tertiary structure? |
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Definition
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Term
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Definition
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Term
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Definition
a subunit in a quaternary structure |
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Term
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Definition
an oligomer with 4 identical protomers |
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Term
why do most gobular proteins have quaternary structure? |
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Definition
1.mores stable 2.active sites often formed by 2 diff.polypeptides 3.smaller chains have less chance for error in synthesis 4.allows for changes in shape when proteins bind with other molecules |
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Term
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Definition
a molecule that binds with a protein |
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Term
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Definition
a region of a single polypeptide chain that folds up independantly |
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Term
what 6 forces may stabilize the 3-D structure of a protein? |
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Definition
1.hydrophobic bonds 2.hydrophobic clusters 3.ionic bonds 4. disulfide bonds 5.hydrogen bonds 6.van der waals forces |
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Term
what aas likely to result in ionic bonding? |
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Definition
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Term
what causes van der waals attraction? |
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Definition
close proximity of 2 atoms |
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Term
what aa can form disulfide bonds? |
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Definition
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