Biochemistry of Complex Proteins: Structure, Properties, and Functions

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Comprehensive vocabulary flashcards covering the definitions, structures, and classes of complex proteins, as well as specific functional groups, allosteric regulation, and transport mechanisms.

Last updated 12:32 AM on 9/25/26
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23 Terms

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Complex Protein

A biomolecule, also known as a conjugated protein, composed of an amino acid chain (the protein portion) and a non-protein component known as a prosthetic group.

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Apoprotein

The protein portion of a complex protein that is typically inactive on its own and requires a prosthetic group for biological functionality.

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Prosthetic Group

A non-protein molecule essential for the biological activity of a complex protein, often directly involved in catalysis or ligand binding.

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Holoprotein

The complete, biologically active complex protein formed by the combination of an apoprotein with its prosthetic group.

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Quaternary Structure

The structural organization defining the number and order of connection of individual polypeptide chains (protomers) in an oligomeric protein.

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Protomer

An individual monomeric polypeptide chain that connects with other chains via non-covalent interactions to form an oligomeric protein.

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Glycoproteins

A class of complex proteins whose prosthetic group consists of carbohydrate chains (heterooligosaccharides) covalently attached to the polypeptide backbone.

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Lipoproteins

Complex lipid-protein particles consisting of a hydrophobic core of cholesterol esters and triglycerides surrounded by a shell of phospholipids, free cholesterol, and apoproteins used for lipid transport.

<p>Complex lipid-protein particles consisting of a hydrophobic core of cholesterol esters and triglycerides surrounded by a shell of phospholipids, free cholesterol, and apoproteins used for lipid transport.</p>
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Metalloproteins

A class of complex proteins that contain metal ions (such as Fe\text{Fe}, Cu\text{Cu}, or Zn\text{Zn}) as their prosthetic group.

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Phosphoproteins

Complex proteins containing phosphoric acid residues attached via ester bonds to the hydroxyl groups of amino acids, predominantly serine and threonine.

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Chromoproteins

A class of complex proteins containing colored pigment molecules, such as heme or flavins, as their prosthetic group.

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Hemoglobin

A tetrameric chromoprotein composed of four globin subunits (two 12\frac{1}{2} or β\beta chains) and four heme groups responsible for oxygen transport in vertebrate blood.

<p>A tetrameric chromoprotein composed of four globin subunits (two $$\frac{1}{2}$$ or $$\beta$$ chains) and four heme groups responsible for oxygen transport in vertebrate blood.</p>
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<p>Heme Group</p>

Heme Group

A prosthetic group consisting of a porphyrin ring system complexed with a single ferrous iron ion (Fe2+\text{Fe}^{2+}) that serves as the reversible binding site for oxygen.

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2,3-Bisphosphoglycerate (BPG)

A strongly negatively charged regulatory ligand synthesized in red blood cells that binds to hemoglobin's central allosteric cavity, reducing its affinity for O2\text{O}_2 by 26 times.

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Methemoglobin (met-Hb)

A blue-brown form of hemoglobin produced when the central iron ion is oxidized from Fe2+\text{Fe}^{2+} to Fe3+\text{Fe}^{3+}, rendering it incapable of binding O2\text{O}_2 or CO\text{CO}.

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Carboxyhemoglobin (HbCO)

A stable complex formed when carbon monoxide binds to hemoglobin, requiring 200 times lower partial pressure than oxygen and causing death when 70% of hemoglobin is bound.

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Carbaminohemoglobin

A compound formed by the reversible binding of carbon dioxide to amino groups on the globin chains of hemoglobin.

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Bohr Effect

The physiological mechanism where elevated hydrogen ion concentration (lower pH) and higher temperature in tissues decrease hemoglobin's affinity for oxygen, promoting oxygen release.

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Flavoproteins

Enzymes that contain flavin adenine dinucleotide (FAD) or flavin mononucleotide (FMN) derived from riboflavin (Vitamin B2\text{B}_2) to catalyze metabolic redox reactions.

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Succinate Dehydrogenase

A flavoprotein enzyme that catalyzes the oxidation of succinate to fumarate while reducing FAD to FADH2\text{FADH}_2.

<p>A flavoprotein enzyme that catalyzes the oxidation of succinate to fumarate while reducing FAD to $$\text{FADH}_2$$.</p>
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Nucleoproteins

Complexes composed of nucleic acids bound to proteins, classified as deoxyribonucleoproteins (DNP) or ribonucleoproteins (RNP).

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Histones

Positively charged eukaryotic nuclear proteins rich in basic amino acids that interact electrostatically with DNA to pack it into chromosomes.

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Chromatin

The substance in eukaryotic cell nuclei composed of nuclear DNA, histones, and non-histone chromosomal proteins that condenses to form chromosomes during cell division.