Protein structure and synthesis

Protein structure and synthesis

POM

POM

Gluconeogenesis
Glycogen metabolism
Amino acid metabolism
Fatty acid synthesis
Fatty acid oxidation
Ketone body metabolism
Cholesterol metabolism
Carbohydrates and sugars
Fats and lipids
Proteins
Cellular structure and function
Cell membrane
Selective permeability of the cell membrane
Extracellular matrix
Cell-cell junctions
Endocytosis and exocytosis
Osmosis
Resting membrane potential
Nernst equation
Cell signaling pathways
Cytoskeleton and intracellular motility
Nuclear structure
DNA structure
Transcription of DNA
Translation of mRNA
Amino acids and protein folding
Protein structure and synthesis
Nucleotide metabolism
DNA replication
Lac operon
DNA damage and repair
Cell cycle
Mitosis and meiosis
DNA mutations
Polymerase chain reaction (PCR) and reverse-transcriptase PCR (RT-PCR)
Gel electrophoresis and genetic testing
ELISA (Enzyme-linked immunosorbent assay)
Karyotyping
DNA cloning
Fluorescence in situ hybridization
Mendelian genetics and punnett squares
Hardy-Weinberg equilibrium
Inheritance patterns
Independent assortment of genes and linkage
Gene regulation
Epigenetics
Evolution and natural selection
Bacterial structure and functions
Free radicals and cellular injury
Necrosis and apoptosis
Ischemia
Hypoxia
Inflammation
Atrophy, aplasia, and hypoplasia
Hyperplasia and hypertrophy
Metaplasia and dysplasia
Oncogenes and tumor suppressor genes
Anticoagulants: Heparin
Anticoagulants: Warfarin
Anticoagulants: Direct factor inhibitors
Antiplatelet medications
Thrombolytics
Blood histology
Blood components
Blood groups and transfusions
Platelet plug formation (primary hemostasis)
Coagulation (secondary hemostasis)
Role of Vitamin K in coagulation
Clot retraction and fibrinolysis
Iron deficiency anemia
Beta-thalassemia
Alpha-thalassemia
Sideroblastic anemia
Anemia of chronic disease
Lead poisoning
Hemolytic disease of the newborn
Glucose-6-phosphate dehydrogenase (G6PD) deficiency
Autoimmune hemolytic anemia
Pyruvate kinase deficiency
Paroxysmal nocturnal hemoglobinuria
Sickle cell disease (NORD)
Hereditary spherocytosis
Aplastic anemia
Fanconi anemia
Megaloblastic anemia
Diamond-Blackfan anemia
Chronic leukemia
Acute leukemia
Microcytic anemia: Pathology review
Non-hemolytic normocytic anemia: Pathology review
Intrinsic hemolytic normocytic anemia: Pathology review
Extrinsic hemolytic normocytic anemia: Pathology review
Macrocytic anemia: Pathology review
Heme synthesis disorders: Pathology review
Coagulation disorders: Pathology review
Platelet disorders: Pathology review
Mixed platelet and coagulation disorders: Pathology review
Thrombosis syndromes (hypercoagulability): Pathology review
Lymphomas: Pathology review
Leukemias: Pathology review
Plasma cell disorders: Pathology review
Myeloproliferative disorders: Pathology review
Thymus histology
Spleen histology
Lymph node histology
Introduction to the immune system
Cytokines
Innate immune system
Complement system
T-cell development
B-cell development
MHC class I and MHC class II molecules
T-cell activation
B-cell activation, differentiation, and contraction
Cell-mediated immunity of CD4 cells
Cell-mediated immunity of natural killer and CD8 cells
Antibody classes
Somatic hypermutation and affinity maturation
VDJ rearrangement
Contracting the immune response and peripheral tolerance
B- and T-cell memory
Anergy, exhaustion, and clonal deletion
Vaccinations
Type I hypersensitivity
Type II hypersensitivity
Type III hypersensitivity
Type IV hypersensitivity

Flashcards

Protein structure and synthesis

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Key Takeaways

Protein synthesis occurs in cells through a process called translation. The genetic code for a protein, in the form of messenger RNA (mRNA), is read by a ribosome, which then assembles the appropriate sequence of amino acids according to the code. The process of translation requires the help of transfer RNA (tRNA) molecules, which deliver the correct amino acid to the ribosome. Once proteins are synthesized, they are further folded into their unique 3D structure.

There are hierarchical degrees of complexity in the formation of a mature, fully-folded protein. Primary structure describes a linear chain of amino acids formed by sequential peptide bonds. The secondary structure consists of backbone interactions in the polypeptide chain that are stabilized by hydrogen bonds between amino acids, forming α-helices and β-pleated sheets. In tertiary structure, secondary structures come together and further orient themselves depending on hydrophobic interactions, ionic interactions, and disulfide bridges. Finally, the quaternary structure consists of multiple tertiary structures coming together to form subunits of a larger protein.