Front
Glycine
Back
Smallest achiral amino acid
Provides flexibility in protein structures; often found in collagen triple helices.
Public Deck
Biochemistry - 50 Essential Concepts
Study biochemistry with 50 flashcards covering amino acids, enzymes, metabolism, nucleic acids, and lipid chemistry.
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Front
Proline
Back
Cyclic amino acid (imino acid)
Induces 'kinks' or 'breaks' in alpha-helices; critical for collagen stability.
Front
Cysteine
Back
Sulfur-containing amino acid
Forms disulfide bridges (covalent bonds) to stabilize tertiary and quaternary protein structures.
Front
Histidine
Back
Basic amino acid with pKa ~6.0
Acts as a versatile pH-dependent buffer and proton shuttle in enzyme active sites.
Front
Primary Structure of Proteins
Back
Linear sequence of amino acids
Determined by DNA sequence; held together by covalent peptide bonds.
Front
Alpha-Helix
Back
Secondary structure stabilized by hydrogen bonds
H-bonds occur between the carbonyl oxygen and amide hydrogen four residues apart.
Front
Tertiary Structure
Back
Three-dimensional folding of a single polypeptide
Driven by hydrophobic interactions, ionic bonds, and disulfide bridges.
Front
Hemoglobin (Quaternary Structure)
Back
Tetrameric protein (2 alpha, 2 beta subunits)
Exhibits cooperativity (sigmoidal curve) for oxygen transport in red blood cells.
Front
Essential Amino Acids
Back
Amino acids that must be obtained from diet
Includes PVT TIM HaLL: Phe, Val, Thr, Trp, Ile, Met, His, Leu, Lys.
Front
Zwitterion
Back
Molecule with both positive and negative charges (net zero)
Amino acids exist in this state at their isoelectric point (pI).
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