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Chapter 9 Basic structure of proteins: current paradigms, trends, and perspective

  • Sheetal Dagar , Anil Panwar , Varruchi Sharma , Imran Sheikh , Vikas Kushwaha , Damanjeet Kaur , Anil K. Sharma und Sri Kant
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Bioinformatics
Ein Kapitel aus dem Buch Bioinformatics

Abstract

Proteins are essential biomolecules, serving as the building blocks of living organisms and playing vital roles in various biological processes. Amino acids, the fundamental units of proteins, consist of an amino group, a carboxyl group, and a unique side chain (R group). There are around 500 known amino acids, with 20 forming the genetic code. The structure of proteins can be categorized into primary, secondary, tertiary, and quaternary levels. Primary structure represents the linear sequence of amino acids, while the secondary structure involves the folding of segments into alpha helices and beta sheets. Tertiary structure results from long-range interactions between amino acids, and quaternary structure refers to the arrangement of multiple polypeptide chains. Protein motifs and domains are specific arrangements of secondary structures, providing functional and structural characteristics. Techniques such as nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography allow the determination of protein 3D structures. NMR is particularly valuable in native and dynamic environments, while X-ray crystallography requires crystallization. Understanding protein structures aids in drug design, biotechnology, and various research fields, contributing to advancements in science and medicine. However, challenges, such as obtaining crystals and nonphysiological conditions, remain in protein structure determination.

Abstract

Proteins are essential biomolecules, serving as the building blocks of living organisms and playing vital roles in various biological processes. Amino acids, the fundamental units of proteins, consist of an amino group, a carboxyl group, and a unique side chain (R group). There are around 500 known amino acids, with 20 forming the genetic code. The structure of proteins can be categorized into primary, secondary, tertiary, and quaternary levels. Primary structure represents the linear sequence of amino acids, while the secondary structure involves the folding of segments into alpha helices and beta sheets. Tertiary structure results from long-range interactions between amino acids, and quaternary structure refers to the arrangement of multiple polypeptide chains. Protein motifs and domains are specific arrangements of secondary structures, providing functional and structural characteristics. Techniques such as nuclear magnetic resonance (NMR) spectroscopy and X-ray crystallography allow the determination of protein 3D structures. NMR is particularly valuable in native and dynamic environments, while X-ray crystallography requires crystallization. Understanding protein structures aids in drug design, biotechnology, and various research fields, contributing to advancements in science and medicine. However, challenges, such as obtaining crystals and nonphysiological conditions, remain in protein structure determination.

Heruntergeladen am 13.12.2025 von https://www.degruyterbrill.com/document/doi/10.1515/9783111568584-009/html
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