Structural mechanisms of nonplanar hemes in proteins

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The objective is to assess the occurrence of nonplanar distortions of hemes and other tetrapyrroles in proteins and to determine the biological function of these distortions. Recently, these distortions were found by us to be conserved among proteins belonging to a functional class. Conservation of the conformation of the heme indicates a possible functional role. Researchers have suggested possible mechanisms by which heme distortions might influence biological properties; however, no heme distortion has yet been shown conclusively to participate in a structural mechanism of hemoprotein function. The specific aims of the proposed work are: (1) to characterize and quantify the ... continued below

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Medium: P; Size: 35 p.

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Shelnutt, J.A. May 1, 1997.

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  • Sandia National Laboratories
    Publisher Info: Sandia National Labs., Albuquerque, NM (United States)
    Place of Publication: Albuquerque, New Mexico

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Description

The objective is to assess the occurrence of nonplanar distortions of hemes and other tetrapyrroles in proteins and to determine the biological function of these distortions. Recently, these distortions were found by us to be conserved among proteins belonging to a functional class. Conservation of the conformation of the heme indicates a possible functional role. Researchers have suggested possible mechanisms by which heme distortions might influence biological properties; however, no heme distortion has yet been shown conclusively to participate in a structural mechanism of hemoprotein function. The specific aims of the proposed work are: (1) to characterize and quantify the distortions of the hemes in all of the more than 300 hemoprotein X-ray crystal structures in terms of displacements along the lowest-frequency normal coordinates, (2) to determine the structural features of the protein component that generate and control these nonplanar distortions by using spectroscopic studies and molecular-mechanics calculations for the native proteins, their mutants and heme-peptide fragments, and model porphyrins, (3) to determine spectroscopic markers for the various types of distortion, and, finally, (4) to discover the functional significance of the nonplanar distortions by correlating function with porphyrin conformation for proteins and model porphyrins.

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Medium: P; Size: 35 p.

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OSTI as DE97006214

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  • Other Information: PBD: May 1997

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  • Other: DE97006214
  • Report No.: SAND--97-0915
  • Grant Number: AC04-94AL85000
  • DOI: 10.2172/477744 | External Link
  • Office of Scientific & Technical Information Report Number: 477744
  • Archival Resource Key: ark:/67531/metadc674773

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  • May 1, 1997

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  • July 25, 2015, 2:21 a.m.

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  • May 5, 2016, 8:17 p.m.

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Shelnutt, J.A. Structural mechanisms of nonplanar hemes in proteins, report, May 1, 1997; Albuquerque, New Mexico. (digital.library.unt.edu/ark:/67531/metadc674773/: accessed May 25, 2018), University of North Texas Libraries, Digital Library, digital.library.unt.edu; crediting UNT Libraries Government Documents Department.