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Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy.
Abstract: It has been proposed that combination of intraresidue, sequential and longer range nuclear Overhauser enhancements occurring in 1H nuclear magnetic resonance spectra of protein chains folded in a helix show a regular characteristic pattern. As a test case the spectra of horse muscle acylphosphatase were searched for this pattern together with other typical signs of a helical conformation (i.e. chemical shift, coupling constants and slow 2H-H exchange). Two amino acid sequences complying with these requirements were found. Just a few amino acid spin system assignments were then sufficient to locate the two segments within the primary structure (residues 22 to 35 and 55 to 66), thus providing the sequential assignment. The assignment of the side-chains was completed and a list of all nuclear magnetic resonance constraints within the two segments (126 intra- and 180 interresidue distances, 21 torsion angles phi and 19 hydrogen bonds) was produced. Distance geometry calculation shows that each segment forms an alpha-helix. The mutual orientation of the two helices was established subsequently.
Publication Date: 1989-01-05 PubMed ID: 2538623DOI: 10.1016/0022-2836(89)90377-xGoogle Scholar: Lookup The Equine Research Bank provides access to a large database of publicly available scientific literature. Inclusion in the Research Bank does not imply endorsement of study methods or findings by Mad Barn.
- Journal Article
Summary
This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.
The research study focuses on identifying alpha-helical regions in horse muscle acylphosphatase using hydrogen-1 (1H) nuclear magnetic resonance spectroscopy.
Objectives and Methodology
- A hypothesis suggested that when protein chains are folded into a helix, their intraresidue, sequential, and longer-range nuclear Overhauser enhancements exhibit a consistently regular pattern in the hydrogen-1 nuclear magnetic resonance spectra. The objective of this research was to test this theory using horse muscle acylphosphatase as the test case.
- The research involved exploring the spectra of horse muscle acylphosphatase for this characteristic pattern and other typical signs indicative of a helical conformation such as chemical shift, coupling constants, and slow 2H-H exchange.
Findings
- In this research, two amino acid sequences were found that comply with the required characteristics indicative of a helical conformation.
- Subsequently, with only a few amino acid spin system assignments, the two sequences were located within residues 22 to 35 and 55 to 66 in the primary structure, subsequently providing the sequential assignment.
Further Analyses and Conclusions
- The researchers completed the assignment of the side-chains, and compiled a list of all observed nuclear magnetic resonance constraints within the two sequences. This comprised of 126 intra- and 180 inter-residue distances, 21 torsion angles phi, and 19 hydrogen bonds.
- Further analyses through distance geometry calculation demonstrated that each of these two segments forms an alpha-helix.
- The researchers were also able to establish the mutual orientation of the two helices identified within horse muscle acylphosphatase.
In sum, this study used 1H nuclear magnetic resonance spectroscopy to validate the theory regarding the characteristic pattern exhibited by helically-folded protein chains’ nuclear Overhauser enhancements. Through the analysis of horse muscle acylphosphatase, the researchers identified and located alpha-helical regions within the molecule and could establish their interaction and orientation within its structure.
Cite This Article
APA
Saudek V, Atkinson RA, Williams RJ, Ramponi G.
(1989).
Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy.
J Mol Biol, 205(1), 229-239.
https://doi.org/10.1016/0022-2836(89)90377-x Publication
Researcher Affiliations
- Inorganic Chemistry Laboratory, University of Oxford, U.K.
MeSH Terms
- Acid Anhydride Hydrolases
- Amino Acid Sequence
- Animals
- Horses
- Magnetic Resonance Spectroscopy
- Models, Molecular
- Molecular Sequence Data
- Phosphoric Monoester Hydrolases
- Protein Conformation
Citations
This article has been cited 3 times.- Yang YS, Garbay C, Duchesne M, Cornille F, Jullian N, Fromage N, Tocque B, Roques BP. Solution structure of GAP SH3 domain by 1H NMR and spatial arrangement of essential Ras signaling-involved sequence. EMBO J 1994 Mar 15;13(6):1270-9.
- Berti A, Tremori E, Pazzagli L, Degl'Innocenti D, Camici G, Cappugi G, Manao G, Ramponi G. Rat muscle acylphosphatase: purification, amino sequence, and immunological characterization. J Protein Chem 1991 Feb;10(1):91-102.
- Mikou A, LaPlante SR, Guittet E, Lallemand JY, Martin-Eau Claire MF, Rochat H. Toxin III of the scorpion Androctonus australis Hector: proton nuclear magnetic resonance assignments and secondary structure. J Biomol NMR 1992 Jan;2(1):57-70.
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