12 research outputs found
Moa Ammonium Bicarbonate-1
Moa ammonium bicarbonate extraction run #1 on Orbitrap X
Moa HCl control
Moa HCl extraction buffer control on Orbitrap X
MPM-PV 3267.
<p>Lamniform tooth in (A) lingual, (B) labial, and (C) lateral view. Note the slenderness of the principle cusp, the well-pronounced lingual protuberance lacking a nutrient groove, and the developed neck that maintains a constant width across all cusps. Scale bar equals 1 cm.</p
Dental measurements for recovered tooth fragments.
<p>All measurements are in millimeters. “>” indicates that broken surfaces preclude full measurement; given value significantly less than for the complete tooth. Abbreviations: TH, tooth height; CH, crown height; MCL, mesial cutting edge length; DCL, distal cutting edge length; DI, distal inclination.</p
MPM-PV 3268.
<p>Lamniform tooth in (A) lingual, and (B) labial view. Note distinct narrowing in the apical two-thirds of principle cusp. Scale bar equals 1 cm.</p
A selection of recovered tooth fragments showing size range and overall symmetry of crowns.
<p>(A) MPM-PV 3271, (B) MPM-PV 3272, (C) MPM-PV 3267, (D) MPM-PV 3273, (E) MPM-PV 3274, (F) MPM-PV 3275. All fragments are in lingual view. Arrows point to small nutrient foramina. Note that in all specimens, the lingual neck maintains a relatively equal width across the base of the crown. Scale bar equals 1 cm.</p
Locality map of discovery site.
<p>The star marked on the inset map denotes the location the selachian teeth were recovered from, approximately halfway between the eastern boundaries Lago Viedma and Lago Argentino (adapted from Mapa de la provincia de Santa Cruz, <a href="http://es.wikipedia.org/wiki/Archivo" target="_blank">http://es.wikipedia.org/wiki/Archivo</a>).</p
Expansion for the <i>Brachylophosaurus canadensis</i> Collagen I Sequence and Additional Evidence of the Preservation of Cretaceous Protein
Sequence
data from biomolecules such as DNA and proteins, which
provide critical information for evolutionary studies, have been assumed
to be forever outside the reach of dinosaur paleontology. Proteins,
which are predicted to have greater longevity than DNA, have been
recovered from two nonavian dinosaurs, but these results remain controversial.
For proteomic data derived from extinct Mesozoic organisms to reach
their greatest potential for investigating questions of phylogeny
and paleobiology, it must be shown that peptide sequences can be reliably
and reproducibly obtained from fossils and that fragmentary sequences
for ancient proteins can be increasingly expanded. To test the hypothesis
that peptides can be repeatedly detected and validated from fossil
tissues many millions of years old, we applied updated extraction
methodology, high-resolution mass spectrometry, and bioinformatics
analyses on a <i>Brachylophosaurus canadensis</i> specimen
(MOR 2598) from which collagen I peptides were recovered in 2009.
We recovered eight peptide sequences of collagen I: two identical
to peptides recovered in 2009 and six new peptides. Phylogenetic analyses
place the recovered sequences within basal archosauria. When only
the new sequences are considered, <i>B. canadensis</i> is
grouped more closely to crocodylians, but when all sequences (current
and those reported in 2009) are analyzed, <i>B. canadensis</i> is placed more closely to basal birds. The data robustly support
the hypothesis of an endogenous origin for these peptides, confirm
the idea that peptides can survive in specimens tens of millions of
years old, and bolster the validity of the 2009 study. Furthermore,
the new data expand the coverage of <i>B. canadensis</i> collagen I (a 33.6% increase in collagen I alpha 1 and 116.7% in
alpha 2). Finally, this study demonstrates the importance of reexamining
previously studied specimens with updated methods and instrumentation,
as we obtained roughly the same amount of sequence data as the previous
study with substantially less sample material. Data are available
via ProteomeXchange with identifier PXD005087
Expansion for the <i>Brachylophosaurus canadensis</i> Collagen I Sequence and Additional Evidence of the Preservation of Cretaceous Protein
Sequence
data from biomolecules such as DNA and proteins, which
provide critical information for evolutionary studies, have been assumed
to be forever outside the reach of dinosaur paleontology. Proteins,
which are predicted to have greater longevity than DNA, have been
recovered from two nonavian dinosaurs, but these results remain controversial.
For proteomic data derived from extinct Mesozoic organisms to reach
their greatest potential for investigating questions of phylogeny
and paleobiology, it must be shown that peptide sequences can be reliably
and reproducibly obtained from fossils and that fragmentary sequences
for ancient proteins can be increasingly expanded. To test the hypothesis
that peptides can be repeatedly detected and validated from fossil
tissues many millions of years old, we applied updated extraction
methodology, high-resolution mass spectrometry, and bioinformatics
analyses on a <i>Brachylophosaurus canadensis</i> specimen
(MOR 2598) from which collagen I peptides were recovered in 2009.
We recovered eight peptide sequences of collagen I: two identical
to peptides recovered in 2009 and six new peptides. Phylogenetic analyses
place the recovered sequences within basal archosauria. When only
the new sequences are considered, <i>B. canadensis</i> is
grouped more closely to crocodylians, but when all sequences (current
and those reported in 2009) are analyzed, <i>B. canadensis</i> is placed more closely to basal birds. The data robustly support
the hypothesis of an endogenous origin for these peptides, confirm
the idea that peptides can survive in specimens tens of millions of
years old, and bolster the validity of the 2009 study. Furthermore,
the new data expand the coverage of <i>B. canadensis</i> collagen I (a 33.6% increase in collagen I alpha 1 and 116.7% in
alpha 2). Finally, this study demonstrates the importance of reexamining
previously studied specimens with updated methods and instrumentation,
as we obtained roughly the same amount of sequence data as the previous
study with substantially less sample material. Data are available
via ProteomeXchange with identifier PXD005087