Amino Acid Sequence of Dog Heart Cytochrome c

McDowall, Max A.; Smith, Emil L.

doi:10.1016/s0021-9258(18)97002-x

Cited by 29 publications

(3 citation statements)

References 17 publications

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“…However, when this material was subjected to Edman degradation, it yielded Asp, Ser, and Gly in the first cycle with no other amino acids detected in the second cycle. It was concluded that the bonds Ser-239/Gly-240 and Gly-240/Glu-241, along with those involving the Asp-238, were cleaved with the prolonged digestion, as previously reported for similar peptide bonds (McDowall & Smith, 1965). In contrast, the Asn-217 residue, located between two valines, remains unaltered, attesting to the resistance of the peptide to acid hydrolysis.…”

Section: Resultssupporting

confidence: 72%

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Márquez¹,

Iriarte²,

Martinez‐Carrion³

1989

Biochemistry

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Chemical modification of the Torpedo californica acetylcholine receptor (AcChR) by the fluorescent agent N-(1-pyrenyl)maleimide (PM) under nonreducing conditions resulted in the labeling of cysteine residues in all subunits and marked inhibition of the AcChR ion channel opening [Clarke, J. H., & Martinez-Carrion, M. (1986) J. Biol. Chem. 261, 10063-10072]. The PM alkylation kinetics are not affected by the presence of agonists or a competitive antagonist. The PM-labeled alpha-subunit has been purified and digested with both CNBr and trypsin. The resulting fragments from both cleavages were fractionated by high-performance liquid chromatography. The amino acid analysis and sequencing data of the PM-labeled peptides identified cysteine-222 as the only residue labeled by PM on the alpha-subunit primary structure. Cysteine-222 is located in the middle of a hydrophobic domain designated M1, which contains a homologous class of cysteines (Cys-241 in the aligned sequences) conserved in the four subunits of the AcChR. Because of its reactivity and fluorescent properties of the bound probe, alpha Cys-222 seems to be free sulfhydryl group accessible through a hydrophobic pocket, and these properties should be incorporated into proposed folding models for the alpha-subunit.

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Section: Resultssupporting

confidence: 72%

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Márquez¹,

Iriarte²,

Martinez‐Carrion³

1989

Biochemistry

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“…Experimental Results. The amino acid sequences of the cytochrome c variants (Figure ) − show a maximum of six residue changes, involving substitutions including ionizable, uncharged polar, and hydrophobic residues. The chromatographic characteristics of the proteins result from the complicated interplay among these residue changes, which alter the charge distribution and the overall molecular geometry.…”

Section: Resultsmentioning

confidence: 99%

Electrostatic Contributions to Protein Retention in Ion-Exchange Chromatography. 1. Cytochrome c Variants

Yan

Lenhoff

2004

Anal. Chem.

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Among the factors that modulate protein interactions, several protein structural properties, such as size, shape, and charge distribution, may play significant roles. In this work, we investigate the influence of protein structure on binding in ion-exchange chromatography, in which electrostatic interactions are dominant. Chromatographic experiments show separation of cytochrome c variants with a limited number of sequence differences to be feasible. To probe the molecular basis for this behavior, protein-adsorbent electrostatic interactions were modeled in the context of continuum electrostatics accounting for the full 3D protein structure. Protein retention was modeled by averaging over all protein-adsorbent configurations using the full accessible surface of the protein. The electrostatic interaction free energy distribution shows that configurations in which numerous positive protein charges are close to the cation exchanger functional groups produce the most favorable binding. The calculated binding equilibrium constant, found by averaging over the full 3D configurational space, captures the chromatographic differentiation of closely related cytochrome c variants. To obviate the need for full sampling of protein configurations, calculations of interaction free energies at short protein-adsorbent separation distances or of protein surface potentials were found to yield reasonable semiquantitative descriptions of the retention trends.

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“…Position 33 is occupied by an asparaginyl residue, as contrasted to the histidyl residue commonly occurring at this location in other cytochromes c. The importance of this substitution is discussed in connection with recent findings concerning the nature of the hemochrome-forming groups in cytochrome c. from a number of different species have been established through the efforts of several groups of investigators. To date, in addition to the horse heart protein, the cytochromes c of known structure include those from man (Matsubara and Smith, 1963), pig (Stewart and Margoliash, 1965), cow (Yasunobu et al, 1963), chicken (Chan and Margoliash, 1966a), tuna (Kreil, 1963(Kreil, ,1965, a moth, Sarnia cynthia (Chan and Margoliash, 1966b), baker's yeast (Narita et al, 1963), a rhesus monkey (Rothfus and Smith, 1965), the dog (McDowall and Smith, 1965), the rattlesnake (Bahl and Smith, 1965), the mold Neurospora crassa (Heller and Smith, 1965), the rabbit (Needleman and Margoliash, 1966), the great grey kangaroo, Macropus canguru ( , and from the yeast, Candida krusei (Narlta and Titan!, 1966).…”

mentioning

confidence: 99%

Primary Structure of the Cytochrome c from the Snapping Turtle, Chelydra Serpentina^*

Chan¹,

Tulloss²,

Margoliash³

1966

Biochemistry

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Amino Acid Sequence of Dog Heart Cytochrome c

Cited by 29 publications

References 17 publications

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Electrostatic Contributions to Protein Retention in Ion-Exchange Chromatography. 1. Cytochrome c Variants

Primary Structure of the Cytochrome c from the Snapping Turtle, Chelydra Serpentina^*

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Amino Acid Sequence of Dog Heart Cytochrome c

Cited by 29 publications

References 17 publications

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Covalent modification of a critical sulfhydryl group in the acetylcholine receptor: cysteine-222 of the .alpha.-subunit

Electrostatic Contributions to Protein Retention in Ion-Exchange Chromatography. 1. Cytochrome c Variants

Primary Structure of the Cytochrome c from the Snapping Turtle, Chelydra Serpentina*

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Primary Structure of the Cytochrome c from the Snapping Turtle, Chelydra Serpentina^*