FUN2/Proteins Flashcards by Adarsh Aratikatla

In an amino acid, what determines the chemical properties?

side-chain/r group

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once inserted into a _____, amino acid properties determine how they will behave

polypeptide chain

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What are all the essential amino acids?

PVT TIM G. HALL
phenylalanine, valine, threonine, tryptophan, isoleucine, methionine, (glutamine - critically ill) histidine, arginine (children) lycine, and leucine

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What does Private Tim G. Hall LIV for?

the branches, (leucine, isoleucine, and valine)

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Where does private time g hall live?

Basic training HAL (histidine, arginine, lysine)

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Which is the smallest r group?

glycine

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Which of the amino acids are hydrophobic?

IMPACT GVLP

A-Alanine, T-tryptophan, G-Glycine, L-Leucine

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What of the amino acids are hydrophilic?

STALAG GHAT

T-Tyrosine Threonine, A-Asparagine, Aspartic Acid, Arginine, L-Lycine, G-Glutamic Acid, Glutamine

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What do all of the charged amino acids have in common?

they are all hydrophilic

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Does alanine fold easily or difficultly?

easily

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Which of the amino acids are negatively charged?

GA(glutamic and aspartic)

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which of the amino acids are positivly charged?

HAL(histidine, arginine, and lysine)

private tim g hall has a POSITIVE experience living in the BASIC training hall

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What type of group does Tyrosine have on it?

hydroxyl group

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True or false? Tyrosine can be phosphorylated?

true

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In tryptophan, the main part is considered hydro_____, but can be considered slightly hydro______ because of the ___?

phobic, philic, N

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Asparagine interacts with a ______?

carbohydrate

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What is the interaction with a carbohydrate called?

glycosylation

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How many amino acids contain sulphur atoms and what are they?

2, Cystine and methionine

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What type of bonds is cystine involved in?

disulphide bonds

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What type of amino acid is proline?

imino amino acid

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Which amino acid is found at bends and turns in protein structure?

proline

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What type of reaction is used to form a peptide bond?

condensation reaction, dehydration reaction

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What is the basic chemical formula for a peptide bond?

C(O)NH

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The start of a polypeptide chain is called the _____ terminus, and the end of a polypeptide chain is called the _____ terminus.

amino (N), carboxyl (C)

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What does native conformation mean?

3-D structure

What structure does native conformation start at?

secondary

What are the 2 types of secondary structures?

alpha helix and beta pleated sheet

The alpha helix is stablized by ______ bonds between every _____ (number) amino acid.

hydrogen, fourth

The hydrogen bonds form between what groups?

CO1- and NH1+

Can the alpha helix structure be predicted?

yes

How many amino acid residues are there in a 360 degree turn of the helix?

3.6

Do the hydrogen bonds in the beta pleated sheet form adjacent or away from each other?

adjacent

What are the 2 ways adjacent chains in a beta pleated sheet can run?

parallel and antiparallel

ex. of alpha helix

collagen and keratin in hair

ex. of beta pleated sheet

silk

When a protein folds into tertiary structure what form does it take?

globular

What determines the tertiary structure?

aa sequence

There are ____ (more/less) distant interactions within proteins in tert. structure

What type of interactions are hydrogen bonds?

electrostatic

A disulphide bond is formed from a reaction of 2 ______.

cyteines

What 2 things controls folding in a protein?

aa seq and disulphide bonds

A peptide bond is a partial ____ bond?

double

What are 2 characteristics of a peptide bond?

rigid and planar

is there a lot or a little bit of rotation in a peptide bond?

very limited

A peptide bond has what type of configuration?

trans

what is a trans configuration in a peptide bond?

alpha carbons are opposite to each other

how many polypeptide chains does Quaternary structure consist of at least?

in Quaternary structure do they polypeptide chains have to be the same or do they have to be different?

does not matter, they can be the same or diff

What holds the Quaternary structure together?

noncovalent interactions and interchain disulphide bonds

ex. of globular proteins

myoglobin

Are globular proteins compact or loose?

compact

in globular proteins the hydrophobic aa's are on the_____

inside

in globular proteins the hydrophilic aa's are on the_____

outside

in globular proteins the _______ aa's are on the inside

hydrophobic

in globular proteins the _____ aa's are on the outside

hydrophilic

What 4 things stabilize globular proteins?

disulphide bonds hydrophobic interactions hydrogen bonds ionic interactions

globular proteins are a combination of _____ structure elements?

secondary

regions in globular proteins are connected by _______

loops/alpha helix | arrows/beta pleated sheet

super-secondary structures are called_____

domains/motifs

ex. of beta pleated sheet BARREL

porin

what is the function of porin?

forms pores in the cell membrane

what is the structure of fibrous proteins?

it is a long rigid structure where 3 polypeptides are wound like a rope-like triple helix

what aa's are rich in fibrous proteins?

proline and glycine

proline and lysine residues are _______ated?

hydroxylated

What are the processes of protein structure?

assembly, folding, packing, interaction

name some functions of a protein once it is in native conformation (6)

catalysis, protection, regulation, signal transduction, storage, transport

what kind of modification happens in post translational modification? (PTM)

chemical

what is attached to the amino acid in PTM, and what happens to the entire protein after that

a functional (R) group, changed the protein's function

PTM: phosphorylation

add phosphate onto serine, threonine, tyrosine

PTM: glycolsylation

add sugar group onto asparagine, serine, threonine

PTM: acylation

add fatty acid on N termini onto serine, alanine, methionine, glycine, and threonine

PTM: ubiquitination

add ubiquitin onto lysine, serine, threonine, cysteine

PTM: nitrosylation

add nitric oxide onto cysteine

what is ubiquitin

helps in the destruction of defective proteins

a deficiency of enzymes in the _________ ________ pathway can cause abnormal glycosylation which can interfere with proper metabolism

oligosaccharide synthetic

go over some context CDG

protein ppt

when protein aggregation is abnormal, the ______ are misfolded

fibrils

ex. of a fibril

amyloid

amyloid can be formed from ______ (number) proteins

over 20

ex. of abnormal protein aggregation/misfolded proteins in brain

alzheimers diesease