Week 1 part 2 Flashcards
Protein
Linear polymer of a.a. joined by peptide bond (polypeptide)
Made by translation mRNA transcribed from genomic DNA
Biologic point of DNA/RNA allow synthesis of specific protein
Functions of P r determined by overall shape
Scale
Genome-DNA
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P primary structure (Sequence)
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P 3D structure
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Function
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Cell biology
Hydrophobic vs hydrophilic
Hydrophilic:
Polar electronic charge distribution (might carry a net +/- charge)
Interact well w/ polar solvent water
Hydrophobic:
Non-polar chain distribution
Do not interact well as polar solvent water
-Hydrophoic effect
Hydrophobic effect
WAter molecule adopt a constrained (cage-like) organization
If hydrophobic molecule coalesce, the # of water molecule is reduced(less water when hydrophobic mol. is bigger)
Lower intropy–>Higher entropy
“oil drop”=impo becasues cytoplasm is an aqueous solution… each protein has only one structure… if there’S more=conformations
What determined the path of the peptide backbone (shape of mol.)
2ndary and tertiary structure
The molecular structure of protein
Primary (sequence)
Secondary (local folding and hydrogen bonding… involve peptide backbone)
TErtiary (overall conformation)
Quaternary (multimetric structure=many polyp)
Supramolecular (large-scale assembly… they can assemble and unassemble)
Function of Protein
Determined by structure
Structure
Movement
Molecular transformation
Transport
Signaling
Binding
Catalysis
REgulation
Primary structure
A.A. squence determine structure and function
so DNA inderctly determin the P function
SEcondary structure
only looking at backbon(no side chain)
a helix and B sheet
both r based on H-bonding between
peptide bond carbonyl O atoms one aminio residue
&
amino group hydrigens on a diff. amino acid residue
60% of P corrsponds to these structure… others have a definite one but not those
a-helix
Periodicity of 3.6 residue/turn (titlted axis)
…every 36 a.a.=10 turn…
H-bond between N and N+4
Gross structure straight rod
Surface properties depend on side chain becasue they are the one that interacts with other part of P… so it is there that the propensity for the helox to form is decided
B-sheet
H-bond between 2 adj. B-strands
Can creat large surface
Side chai=above and below sheet’S plane and they determine the propensity of the sheet to form by interactin with other part of the P
Antiparallel or parallel
Tertiart structure
OVerall conformation of the polypeptide (spatial organization of the multipel secondary structure element)…ex: a-helix+B-sheet+side chains
Amino acid side-chain mediate interaction (non-convalent)
between diff. part of the P and between the P and its lgand GDP
IMPO: COVALENT BOND: CYSTEINE
Cysteine
Contains a sulfhydryl group that form convalent S-S(disulfide) bonds w/ other cysteine side chains
In P, disulfide bonds can be intrachain (teritary structure) or interchain (quaternary structure)
Quaternary structure
Check image
Motids of P structure
Coiled-coil motif
EFhand/helix-loop-helix-motif
Zinc-finger motif