What exactly is this alpha helix and what is its relevance to science, biology and chemistry?
The alpha (α) helix is a central structural motif present in proteins of all living organisms. The amino acids that make up protein molecules are arranged like pearls along a string that can form a spiral to make the α-helix structure. Using calculations of bond angles and turning the atoms in the amino acids around each other to make new theoretical hydrogen bonds along the protein chain, the α-helix structure came to Pauling during, the story is told, when he was laid up in bed with a cold—he quite frequently suffered from colds and secondary sinus infections. The theory for the α-helix structure was formulated by Pauling while convalescing.
The α-helix was a key piece of knowledge by which investigators astutely used in order to propose the structural model of DNA. Scientists James Watson, Francis Crick, Rosalind Franklin and even Linus Pauling himself applied the α-helix motif of protein chains to formulate the double helix and (inaccurately) the triple helix structural models of DNA.
Students of Biochemistry courses and especially Biochemistry undergraduate majors, are regularly taught all about the famous α-helix structure and its discovery. The hydrogen bonds and the peptide bond angles, their bond rotations, the side chain orientations, etc., in the α-helix are all classically taught in lectures and are unfailingly presented in any good Biochemistry textbook.
The α-helix is one of my favorite molecular structures; in fact, for my Ph.D. thesis, I studied a bacterial antimicrobial efflux pump that shared an evolutionarily conserved amino acid sequence motif; this particular sequence motif had an α-helix structure to it. I think it’s an elegant and beautiful structure.
The α-helix structure figures prominently in the inner workings of many proteins, perhaps, for example, by binding to key substrates in enzymes in order to catalyze biochemical reactions or by changing its protein configurations of transporter proteins during the uptake of nutrients by cells or by expelling toxic compounds (like antimicrobials) or waste products from cells. Virtually all biochemical and cellular functions involving proteins will have their molecular mechanisms carried out by protein structures composed of the α-helix.
The alpha (α) helix is a central structural motif present in proteins of all living organisms. The amino acids that make up protein molecules are arranged like pearls along a string that can form a spiral to make the α-helix structure. Using calculations of bond angles and turning the atoms in the amino acids around each other to make new theoretical hydrogen bonds along the protein chain, the α-helix structure came to Pauling during, the story is told, when he was laid up in bed with a cold—he quite frequently suffered from colds and secondary sinus infections. The theory for the α-helix structure was formulated by Pauling while convalescing.
The α-helix was a key piece of knowledge by which investigators astutely used in order to propose the structural model of DNA. Scientists James Watson, Francis Crick, Rosalind Franklin and even Linus Pauling himself applied the α-helix motif of protein chains to formulate the double helix and (inaccurately) the triple helix structural models of DNA.
Students of Biochemistry courses and especially Biochemistry undergraduate majors, are regularly taught all about the famous α-helix structure and its discovery. The hydrogen bonds and the peptide bond angles, their bond rotations, the side chain orientations, etc., in the α-helix are all classically taught in lectures and are unfailingly presented in any good Biochemistry textbook.
The α-helix is one of my favorite molecular structures; in fact, for my Ph.D. thesis, I studied a bacterial antimicrobial efflux pump that shared an evolutionarily conserved amino acid sequence motif; this particular sequence motif had an α-helix structure to it. I think it’s an elegant and beautiful structure.
The α-helix structure figures prominently in the inner workings of many proteins, perhaps, for example, by binding to key substrates in enzymes in order to catalyze biochemical reactions or by changing its protein configurations of transporter proteins during the uptake of nutrients by cells or by expelling toxic compounds (like antimicrobials) or waste products from cells. Virtually all biochemical and cellular functions involving proteins will have their molecular mechanisms carried out by protein structures composed of the α-helix.
What exactly is this alpha helix and what is its relevance to science, biology and chemistry?
The alpha (α) helix is a central structural motif present in proteins of all living organisms. The amino acids that make up protein molecules are arranged like pearls along a string that can form a spiral to make the α-helix structure. Using calculations of bond angles and turning the atoms in the amino acids around each other to make new theoretical hydrogen bonds along the protein chain, the α-helix structure came to Pauling during, the story is told, when he was laid up in bed with a cold—he quite frequently suffered from colds and secondary sinus infections. The theory for the α-helix structure was formulated by Pauling while convalescing.
The α-helix was a key piece of knowledge by which investigators astutely used in order to propose the structural model of DNA. Scientists James Watson, Francis Crick, Rosalind Franklin and even Linus Pauling himself applied the α-helix motif of protein chains to formulate the double helix and (inaccurately) the triple helix structural models of DNA.
Students of Biochemistry courses and especially Biochemistry undergraduate majors, are regularly taught all about the famous α-helix structure and its discovery. The hydrogen bonds and the peptide bond angles, their bond rotations, the side chain orientations, etc., in the α-helix are all classically taught in lectures and are unfailingly presented in any good Biochemistry textbook.
The α-helix is one of my favorite molecular structures; in fact, for my Ph.D. thesis, I studied a bacterial antimicrobial efflux pump that shared an evolutionarily conserved amino acid sequence motif; this particular sequence motif had an α-helix structure to it. I think it’s an elegant and beautiful structure.
The α-helix structure figures prominently in the inner workings of many proteins, perhaps, for example, by binding to key substrates in enzymes in order to catalyze biochemical reactions or by changing its protein configurations of transporter proteins during the uptake of nutrients by cells or by expelling toxic compounds (like antimicrobials) or waste products from cells. Virtually all biochemical and cellular functions involving proteins will have their molecular mechanisms carried out by protein structures composed of the α-helix.
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