Kavran_protein Flashcards
four classes of biological molecules
sugars, fatty acids, amino acids, nucleotides
T/F. Double bonds in biological molecules have rotational freedom
F. Double bonds are barrier to rotation, whereas single bonds are free to rotate
Sharing of electron forces that cause bound molecules to be coplanar
resonance
what limits how close nuclei can get to one another?
van der waals radius
what are dipoles and why do they form?
positive and negative charges separated by distance on same molecule, formed from unequal sharing of electrons between atoms in a polar molecule
energy of a C-C covalent bond
85 kcal/mol
types of noncovalent interactions (4)
hydrogen bonds, van der waals, ionic interactions and hydrophobic effect
optimal H bond distances
2.2-2.5 Å as “strong, mostly covalent”, 2.5-3.2 Å as “moderate, mostly electrostatic”, and 3.2-4.0 Å as “weak, electrostatic”
optimal salt bridge distance
2.7A, not angle dependent
name six broad functions of proteins
structural, enzymatic, mechanical, replication, transport, signalling
T/F. Proteins found in D form most commonly.
False, L isomer prevalent
Direction of polypeptide chain orientation (ie names of two termini)
N+ (amino) ——> C- (carboxyl)
T/F. Peptide bond is planar
True, H-N-C-O atoms lie in a plane from resonance, but side chains hooked to C-alpha are free to rotate
primary structure
amino acid sequence, written N to C
secondary structure
alpha helix, beta sheets, stabilized by H-bonds