Hypertrophic cardiomyopathy is one of the most common inherited heart diseases and is chromosomally dominant. It is clinically manifested by myocardial hypertrophy, especially asymmetric hypertrophy of the ventricular septum, arrhythmias, impaired exercise tolerance and sudden death, and is a disease of cardiac origin. Molecular genetic studies have revealed that mutations in the genes encoding structural proteins of myocardial vesicles are the underlying cause of hypertrophic cardiomyopathy, and mutations in one of several genes can cause the disease. The following genes have been identified in the domestic and international literature to cause HCM: 1. Cardiac troponin I gene (TNNI3): mutations in TNNI3 are considered to be a rare cause of HCM, but several mutations in this gene have been reported in recent years, mainly manifesting as apical hypertrophy. Based on this morphological alteration, it is possible that mutations in TNNI3 are the main genetic cause in patients with apical hypertrophic cardiomyopathy, and that some mutations are present in some patients with both HCM and pre-excitation syndrome (WPW). 2. Cardiac troponin T gene (TNNT2): Various TNNT2 gene defects (missense mutations, splice signaling mutations, small fragment deletions) cause about 15% of all HCM. Localized on chromosome 1q32, approximately 17 kb, consisting of 17 exons, 30 different mutations in TNNT2 have been identified. cTnT includes several functional structural domains, an N-terminal phosphorylation region, and a pro-myosin binding domain located between exons 9 and 12. 3. β-myosin heavy chain gene (MYH7): encoding β-myosin heavy chain (β-MYHC) is located on chromosome 14q11.2-q13 containing 40 exons, 38 of which are involved in the expression of a protein encoding 1935 amino acid residues. Among them, the MYH7 gene is the most important causative gene for hypertrophic cardiomyopathy. The MYH7 gene is located between band 1 and band 2 of the long arm 1 of chromosome 14, and encodes a myosin that is divided into a globular head region S1, a head-rod binding S2, and a rod tail region, with the head region containing the ATPase active site and the interface with the actin binding site and the must chain (binding), which is an important functional region of myosin. MYH7 mutations account for 35% to 50% of all HCM cases. The MYBPC3 mutation accounts for 20%-25% of HCM cases. Myocardial myosin-binding proteins belong to the intracellular globulin superfamily and bind to myosin at structural domains C8 to C10. Myosin and myosin, which bind MyBP-C, have a more stable myosin structure. Cardiac myosin-binding proteins have a specific N-terminal module sequence between the C1 and C2 structural domains that serves as the site of action for cAMP-dependent protein kinases as well as calmodulin-dependent protein kinases. Phosphorylation of the myocardium-specific module sequence regulates myocardial contractility, so MyBP-C is not only involved in the maintenance of myocardial structure, but also in intracellular messaging and influences the diastolic movement of myofilaments.