Biochemistry: Proteins, Amino Acids, Nucleic Acids, and DNA Replication

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Comprehensive vocabulary flashcards generated from lecture notes covering amino acid chemistry, protein secondary and tertiary structures, hemoglobin/myoglobin dynamics, nucleic acid conformations, RNA types, and core DNA replication mechanisms.

Last updated 3:35 PM on 10/1/26
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35 Terms

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Isoelectric Point (pIpI) of Hydrophobic Amino Acids

The pH value at which a hydrophobic amino acid carries net zero charge, calculated as the average of its two pKapK_a values (the carboxyl functional group and the amine functional group).

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Isoelectric Point (pIpI) of Polar and Charged Amino Acids

The pH value at which a polar or charged amino acid carries net zero charge, calculated by taking the average of its three pKapK_a values using the formula pKa1+pKa2+pKa33\frac{pK_{a1} + pK_{a2} + pK_{a3}}{3}.

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Aspartate

A negatively charged amino acid that contains two carboxylic functional groups and one amine functional group.

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Lysine

A positively charged polar amino acid that contains two amine functional groups and one carboxylic functional group.

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Antiparallel β\beta\text{-Pleated Sheet}

A protein secondary structure in which adjacent sheets run in opposite directions and intermolecular hydrogen bonds are vertically arranged, making it stronger than the parallel arrangement.

<p>A protein secondary structure in which adjacent sheets run in opposite directions and intermolecular hydrogen bonds are vertically arranged, making it stronger than the parallel arrangement.</p>
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Parallel β\beta\text{-Pleated Sheet}

A protein secondary structure in which adjacent polypeptide sheets run in the same direction and intermolecular hydrogen bonds are slanted in one direction to pair with corresponding molecules.

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Fibrous Proteins

Proteins composed entirely of a single type of secondary structure throughout their entire length (e.g., exclusively β\beta\text{-pleated sheets} or exclusively α\alpha\text{-helices}).

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Globular Proteins

Proteins whose overall structure contains more than one type of secondary protein structure.

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Collagen

A glycoprotein composed of three right-handed α\alpha\text{-chains} twisted into a left-handed helical structure, with a basic amino acid composition of Glycine (35%35\%), Alanine (11%11\%), and Proline plus Hydroxyproline (21%21\%).

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Scurvy

A condition caused by Vitamin C deficiency, which prevents the hydroxylation of proline residues to hydroxyproline, resulting in weakened collagen fibers and symptoms such as a smelly mouth.

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Methemoglobin (MetHb)

A form of hemoglobin in which iron is oxidized to its ferric (Fe3+Fe^{3+}) state, preventing oxygen (O2O_2) from reversibly binding.

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Myoglobin

A monomeric oxygen storage protein with high affinity for oxygen that yields a rectangular hyperbolic oxygen-binding curve.

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Hemoglobin

A tetrameric oxygen carrier protein that displays cooperative oxygen binding, yielding a sigmoidal oxygen-binding curve.

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Carbamino-hemoglobin

A complex formed when carbon dioxide binds to the N-terminal amine groups of the T form of hemoglobin, without competing with oxygen for the heme active site.

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2,3-Diphosphoglycerate (2,3-BPG)

A negatively charged allosteric regulator that binds to positively charged residues (2 His, 2 Lys, 2 N-termini) in the central cavity of hemoglobin, shifting the curve toward the T state to facilitate O2O_2 release.

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His E7 (Distal Histidine)

A histidine residue on the oxygen-binding side of heme that sterically hinders bound carbon monoxide (COCO), forcing it to tilt away from its preferred perpendicular orientation and reducing its binding affinity relative to O2O_2.

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Perutz Mechanism

A model describing cooperativity in hemoglobin, wherein oxygen binding to one heme group induces conformational changes in secondary, tertiary, and quaternary structures that increase the affinity of remaining heme groups.

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Purines

Nitrogenous bases containing a fused 5-membered and 6-membered ring system, comprising Adenine and Guanine.

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Pyrimidines

Nitrogenous bases containing a single 6-membered ring, comprising Cytosine, Uracil, and Thymine.

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β\beta\text{-N-Glycosidic Linkage}

The covalent bond connecting the 1′1' carbon of a pentose sugar to a nitrogenous base in nucleotides, configured in the β\beta position to prevent cleavage by human digestive enzymes.

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Sugar Pucker

The three-dimensional conformation of the pentose sugar ring (ribose or deoxyribose) in nucleotides, defined by the out-of-plane displacement of either the C2′C_2' or C3′C_3' carbon relative to the other four ring atoms.

<p>The three-dimensional conformation of the pentose sugar ring (ribose or deoxyribose) in nucleotides, defined by the out-of-plane displacement of either the $$C_2'$$ or $$C_3'$$ carbon relative to the other four ring atoms.</p>
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C2′C_2'\text{-endo Pucker}

A sugar pucker conformation where the C2′C_2' carbon is displaced out of the plane on the same side as the C5′C_5' carbon, representing the major sugar conformation in B-DNA.

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C3′C_3'\text{-endo Pucker}

A sugar pucker conformation where the C3′C_3' carbon is displaced out of the plane on the same side as the C5′C_5' carbon, representing the predominant conformation in A-DNA and double-stranded RNA.

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A-DNA

A short, broad, right-handed double helix of DNA featuring C3′C_3'\text{-endo} sugar puckers, which exists physiologically under dehydrated conditions.

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B-DNA

The standard hydrated, right-handed double-helical conformation of DNA with C2′C_2'\text{-endo} sugar puckers, a helix pitch of 3.4 nm3.4\,\text{nm}, and 10 bp10\,\text{bp} per turn.

<p>The standard hydrated, right-handed double-helical conformation of DNA with $$C_2'$$\text{-endo} sugar puckers, a helix pitch of $$3.4\,\text{nm}$$, and $$10\,\text{bp}$$ per turn.</p>
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Z-DNA

An elongated, thin, left-handed double helix with a zig-zag sugar-phosphate backbone containing alternating C2′C_2'\text{-endo} and C3′C_3'\text{-endo} puckers and a high frequency of G-C repeats.

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Heterogeneous Nuclear RNA (hnRNA)

The initial eukaryotic pre-mRNA transcript produced in the nucleus that contains coding exon regions interrupted by non-coding intron sequences.

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Poly(A) Tail

A string of 100–200100\text{--}200 adenylic acid residues appended to the 3′3' end of eukaryotic mRNA post-transcriptionally to enhance molecular stability.

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Transfer RNA (tRNA)

An adaptor RNA molecule featuring an acceptor stem (CCA-3′-OHCCA\text{-}3'\text{-OH}), D loop (containing dihydrouridine), anticodon loop, and TψC\text{T}\psi\text{C} loop (containing pseudouridine) that carries specific amino acids to the ribosome.

<p>An adaptor RNA molecule featuring an acceptor stem ($$CCA\text{-}3'\text{-OH}$$), D loop (containing dihydrouridine), anticodon loop, and $$\text{T}\psi\text{C}$$ loop (containing pseudouridine) that carries specific amino acids to the ribosome.</p>
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Small Nuclear RNA (snRNA)

A class of eukaryotic nuclear RNA molecules present in stable ribonucleoprotein complexes that process precursor pre-mRNA (hnRNA) into mature mRNA for cytoplasmic export.

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Vicinal 2′2'\text{-OH} Group

The hydroxyl group on the 2′2' carbon of ribose in RNA that makes the adjacent 3′3'\text{-phosphodiester} linkage vulnerable to nucleophilic cleavage and alkaline hydrolysis, causing RNA to be less stable than DNA.

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Kornberg Polymerase

DNA Polymerase I, the first DNA-synthesizing enzyme discovered, named in honor of Arthur Kornberg.

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Semiconservative Replication

The mode of DNA replication wherein each new daughter double helix consists of one intact original parental strand and one newly synthesized daughter strand.

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Bidirectional Replication

DNA replication that progresses in both directions simultaneously from an origin of replication via two active replication forks.

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DNA Polymerase Priming Requirement

The prerequisite that all DNA polymerases require a pre-existing RNA primer providing a free 3′3'\text{-OH} group to perform nucleophilic attack on incoming dNTPs and synthesize DNA in the 5′→3′5' \rightarrow 3' direction.