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Signal proteins: reception and signaling proteins both receive and deliver ligands to coordinate cellular responses

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Transport proteins: ion pumps, channel proteins, active vs passive transport

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Integral proteins: embedded in the membrane. special functional region with the purpose of securing the protein in the membrane

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Increasing the number of double bonds will increase the fluidity of the membrane (lipids with polyunsaturated chains)

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Melting temperature of lipids:
With bigger non-polar interaction areas, there are more hydrophobic interactions and more stable interactions, thus making it less fluid at higher melting temperatures

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Floppase: moves inner phospholipid to outer

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Flippase: moves outer phospholipid to inner

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Cholesterol: in cold temperatures, the cholesterol increases fluidity of the bilayer; in warm temperatures the cholesterol stabilizes the membrane

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Hydrophobic tails facing inwards

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Hydrophilic (glycerol) heads facing outwards

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Membrane bound proteins

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Membrane fluidity: length and level of unsaturation determine the stability of the hydrophobic interactions and thus shift the transition phase

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Phospholipid bilayers

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Lipids: molecules that are soluble in organic solvents

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Regulates membrane fluidity: poikilothermic organisms cannot regulate their own body temperatures

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Primary roles:
Biological membranes, energy storage, signaling molecules

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Triacylglycerols: the form of fatty acids most commonly existing in plants and animals

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Hoogsteen Pairing:
Requires syn conformation (H-bonds not 180˚)
G–C bonds are reduced from 3 to 2 H-bonds

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Watson-Crick Pairing:
H-bonds are short, 180˚ (strong)
A–T and C–G

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Purine (A, G) and pyrimidine (C, T, U) bases form these bonds– 1 vs 2 rings

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Double helix structure is created with hydrogen bonds b/w bases on nucleotides

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Base pairing

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7 torsional angles of rotational freedom

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Flexibility and torsional angles

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N-link glycosidic bonds: linkage between ribose and bases

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Monomers linked via condensation reactions 

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Individual units comprised of phosphate, sugar, and a heterocyclic base

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Individual units of the polymer: nucleotides/nucleic acids

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Components

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Lipid Membranes

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DNA

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Glycine and Proline side chains: commonly present in B-turns; The lack of a large side chain in the case of glycine and the presence of a built-in bend in the case of proline allow the polypeptide backbone to fold into a tight U-shaped structure. Without turns, a protein would be large, extended, and loosely packed.

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B-turn: reversal of chain leads to H-bonds; toughness of proteins result from turns

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Tertiary structure: can bend and twist in order to achieve the highest stability in the lowest energy state

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Alpha helix: inner H-bonds, side chains are pointing out, helix dipole moment due to peptide bonds

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R group base stacking: standardizes double helix structure

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Cis vs trans: reduce effects of steric hinderance; depends on how the peptide bond forms (dipoles)

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Nucleic acids

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Proteins

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Carbohydrates: glycosidic bonding

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Critical in maintaining the 3D conformation of large molecules

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Protein–carbohydrate interactions are typically characterized by hydrogen bonds

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Involves dipole-dipole attraction between a partially positive hydrogen atom and a highly electronegative, partially negative oxygen, nitrogen, sulfur, or fluorine atom

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Packing of hydrophobic sugar faces results in van der Waals interactions

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Hydrophobic/hydrophilic bonds

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Hydrogen bonds

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van der Waals interactions

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Ribose pucker: rotation within the ribose is limited to accommodate phosphate repulsion and substituents of ribose atoms

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Alpha and zeta angles cause 7 torsional angles of rotational freedom

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Torsional angles: psi, phi angles govern the 3D structure of the backbone

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Nucleic acids

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Side chains: steric hinderance, charge of the side chains

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Peptide bonds

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Proteins

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Carbohydrates: dictated by glycosidic bonds (alpha vs beta)

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Stability

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Non Covalent Interactions

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Movement

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Peptide bonds: AA are linked via a dehydration reaction b/w a carboxyl group of one AA and the amino group of another

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Structure: AA structure dictates how R groups interact

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Amino acids polymerize by eliminating the elements of water

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Monomer units of protein that comprise peptides

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Amino Acids

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Heteropolysaccharides: more than one type of monosaccharide

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Homopolysaccharides: one type of monosaccharide

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Monosaccharides linked together by glycosidic bonds

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Endoglycosidases and exoclycosidases: enzyme that hydrolyzes monosaccharide units

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Epimers: sugars that differ only by the configuration around 1 carbon atom

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Anomers: pair of stereoisomers that differ at anomeric carbon (carbonyl carbon chiral center)

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Possible and common branching if more than one hydroxyl group exists

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Hydrolysis of a glycosidic bond will result in 2 monosaccharides

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Occurs b/w 2 different carbon atoms of different monosaccharides

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Glycosidic Linkages: carbohydrate polymers are built using energy to form glycosidic linkages

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Provides:
Structure, conjugation onto lipids/proteins/glycosylation, DNA backbone, DNA capping, RNA

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Monomer units for carbohydrates; can be joined to make a polymer by elimination of water

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Polysaccharides

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Monosaccharides

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May limit the conformational freedom of their attached polypeptide chains

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Tend to project away from the protein surface as sugars are hydrophilic

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Help to determine protein structure: usually attached to proteins at sequences that form surface loops or turns

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Smaller oligosaccharides are usually attached to the core protein near its site of attachment to hyaluronate; glycosidic linkage to the protein via the amide N of specific Asn residues known as N-linked oligosaccharides

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Oligosaccharides

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Proteins and glycosaminoglycans form proteoglycans

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Proteins and lipids with covalently attached carbohydrates

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Glycoproteins and Glycolipids

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Nutrient sources for organisms that do not produce their own energy via photosynthesis and/or cannot fix nitrogen

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Building blocks of life: break down into amino acids that help the body grow and repair

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Coded for by DNA

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Peptides can join together to make polypeptides which make up proteins which relates to how the R groups can join to the core and form different amino acids

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Carbohydrates

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Proteins