3.9 Article

ROLE OF SINGLE AMINO ACID MUTATION IN THE ALTERNATIONS IN PROTEIN STRUCTURE

期刊

POSTEPY BIOLOGII KOMORKI
卷 49, 期 1, 页码 3-21

出版社

POLSKIE TOWARZYSTWO ANATOMICZNE

关键词

single amino acid mutations; protein structure; structural changes; polypeptide chain

资金

  1. Statutory Subsidy Funds of the Department of Molecular and Cellular Biology [SUB.D260.22.016]

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This article investigates how single amino acid mutations impact the structure and function of proteins, and discusses the methods used to derive higher-level protein structures from amino acid sequences. The study aims to explain the interactions within polypeptide organization and their clinical implications.
Single amino acid mutations occur relatively often in various human proteins. These include the loss of function mutations and the accumulation of invalid protein. Even though the clinical representation of the diseases is already described, the molecular mechanism in which single amino acid mutations affect the folding of the polypeptide chain remains not clear. Prediction of the proteins' structure from the amino acid sequence of the polypeptide chain has always been the holy grail of biochemistry. In the past, several attempts were made to solve this problem and thus to be able to derive the conformation of the protein from its amino acid chain sequence. In the beginning, high hopes were addressed to the statistical methods, which used the probability tools to predict the structure with around 68% accuracy. Afterwards, the research turned into a different attempt the homology-based methods. Namely, the analysed sequence was compared with a protein with well-established conformation and a similar amino acid sequence in the region of concern. These approaches did not exceed 78% accuracy of prediction. Nowadays, more and more high computational power demanding methods are being introduced. In this paper, the authors described how the single amino acid alternations affect the structure and function of protein. To do so, we reviewed the methods, which are used to derive the higher-level structures from the amino acid sequence. This study aimed to explain the interactions on a higher level of polypeptide organization. Here we present the connection between the primary structure of the protein with its spatial arrangement and combine the biochemical considerations with its clinical implications.

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