Biochemistry the Polypeptide Chain Configuration in Hemoglobin Article Review

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Biochemistry

The Polypeptide Chain Configuration in Hemoglobin and other Globular Proteins

By Linus Pauling and Robert B. Corey (1951)

The article named above describes a continuation in the study of hydrogenbonded planar-amide configurations of polypeptide chains. It also discusses evidence on the possibility of the existence of such chains in fibrous proteins, and in molecules of globular proteins.

The article first notes that globular patterns such as ovalbumin, can "on denaturation be converted into a form showing the B-keratin x-ray pattern." Because of such reactions, there is an observance of the fiber axis distance, which is the same as that of ft keratin, which the authors claim has already been suggested in a previous paper.

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For this reason as well, the authors here claim that the same structure (observed above) should be represented by denatured proteins, with some modifications, which they claim is quite an important discovery.

Significant data on this subject is subsequently discussed, especially that relating to the structure of globular proteins, such as those found in carbonmonoxyhemoglobin. The reason this data is mentioned is to provide support for the above theory, namely and specifically to "provide some support for the idea that the 3.7-residue helix is a principal feature of the structure….....

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"Biochemistry The Polypeptide Chain Configuration In Hemoglobin" (2012, February 08) Retrieved June 5, 2026, from
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"Biochemistry The Polypeptide Chain Configuration In Hemoglobin", 08 February 2012, Accessed.5 June. 2026,
https://www.aceyourpaper.com/essays/biochemistry-polypeptide-chain-configuration-54073
   

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