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Nitrogen in Proteins
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- 1Proteins1) complex molecules made of amino acids
2) synthesized using ribosomes and an mRNA template
transcription --> translation
3) fragile! can denature (change shape) when too hot or with a pH change
because the shape of a protein dictates its function, this denaturing (mutation) could make serious changes - 2What happens to protein function if it denatures?-the shape of a protein dictates its function
-if IMFS break apart or bond incorrectly --> the Amino Acid sequence will change --> function can be lost - 3How Proteins are Formed (General)DNA codon --> mRNA --> tRNA --> amino acid --> amino acid chain (protein)
- 4Amino Acid Structure/Function1) R group: determines AA interactions and protein shape (covalent structure and folding patterns)
2) Amino Group: hold a slightly positive charge (too few e-), also contain a Nitrogen!
3) Carboxyl Group: hold a slightly negative charge (too many e-) - 5Primary (1*) Structure-string of AA's (stretched out amino acids)
-sequence of AA's that make up polypeptide chain
-contain peptide bonds: C-N covalent polar bonds connecting the AA's
-because these bonds are covalent, they are very strong
- 6How Are Peptide Bonds Formed
- 72* Structure-regular, repeated patterns of folding of the protein backbone
-coiled (alpha helix): polypeptide backbone boils around an imaginary helix
-crimped (beta sheet): polypeptide backbone is near fully extended, R-groups alternately point above and below the backbone
-think of hair - ringlets vs crimped
-strong H bonds between the carboxyl and amino groups of the amino acid - 8Tertiary Structure-overall folding of the entire polypeptide chain into a specific 3D shape
-complex folding of a single chain
-Rgroups determine the 3D structure
-IMFs, ionic bonds, and sometimes Disulfide bridges determine exact folding patterns - 9Hydrogen Bonds-strong "temporary" attraction between partial charges (transient bonds that form and reform)
-elements with high Electronegativity (NOF) covalently bound to a partially positively charged Hydrogen
-polar: strong dipole-dipole interaction
-very important in water as well - 10Ionic Bonds-"permanent" attraction between whole charged molecules/atoms - ions (+1/-1)
-highly polarized - 11Van der Waals and Hydrophobic AttractionsVan der Waals Dipole-Dipole Interactions
-other groups beside hydrogen can be involved in polar covalent bonding with strongly electronegative atoms.
-dipoles are created by differences in electronegativities between nearby atoms
-similar to H-bonding, but differences in E's are smaller so the magnitudes of the dipoles is smaller (less polar molecule) and these interactions are weaker
-weakest IMF
Hydrophobic Attractions - 12Quaternary Structure-many proteins are formed from more than one polypeptide chain
-how the multiple tertiary subunits (polypeptide chains) bound together to form the overall protein structure - 13Covalent Bonds-atoms share electrons to complete valence shell
-this codependency (low energy state) holds them together
-very strong
-how these electrons are shared (evenly or unevenly) is determined by if it is a polar or non-polar bond
- 14Electronegativity-how tightly an atom holds onto its electrons
-increases from left --> right across periods and from bottom to top in groups
F is highest, O, Cl, and N are also high
- 15Atom Behavior Based On Electronegativitylow E: will donate an electron and leave an atom with a +1 charge
medium low: will share electrons but will donate them more often if a bonded atom has a significantly higher E (positive dipole symbol)
medium high: will share electrons but will keep them more often if a bonded atom has significantly lower E (negative dipole symbol)
high E: will hold onto their electrons much more often or will steal them from elements with low E, -1 charge - 16Polar Bonds-electrons are not shared evenly between atoms
-occurs when atoms have SIGNIFICANTLY different Electronegativities
-the result of these bonds is a partial positive and partial negative charge on either end (low E positive, high E negative) - 17Non-Polar Bonds-electrons are shared evenly between atoms and atoms have equal Electronegativities
-even if Electronegativities are a little different between atoms, they will still act Non-Polarnon - 18Polar Molecules-have charged regions (slightly positive, slightly negative)
-interact/dissolve well in water
-ex: water, methanol - 19Non-Polar Molecules-mostly non-polar bonds
-don't dissolve well in water (like dissolves like and water is polar)
-often have long strings of CH bonds
-ex: steric acid, methane - 20Methanolpolar
- 21MethaneNon-Polar
- 22Steric AcidNon-Polar
- 23WaterPolar
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- Biology Fichas sobre Nitrogen in Proteins, creado por Maggie Stephens el 22/09/2021.
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- Maggie Stephens
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