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تحميل كتاب Mass Spectrometry of Proteins and Peptides Humana Press pdf
المؤلف : John R Chapman
عن الكتاب : تحميل كتاب Mass Spectrometry of Proteins and Peptides Humana Press pdf تأليف John R Chapman pdf مجانا ... 2000م - 1443هـ
نبذه عن الكتاب:
Recent developments in technology and instrumentation have made mass
spectrometry the method of choice for the identification of gel-separated proteins using rapidly growing sequence databases (1). Proteins with a full-length
sequence present in a database can be identified with high certainty and high
throughput using the accurate masses obtained by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry peptide mapping (2). Simple protein mixtures can also be deciphered by MALDI peptide mapping (3) and the
entire identification process, starting from in-gel digestion (4) and finishing
with acquisition of mass spectra and database search, can be automated (5).
Only 1–3% of a total digest are consumed for MALDI analysis even if the
protein of interest is present on a gel in a subpicomole amount. If no conclusive
identification is achieved by MALDI peptide mapping, the remaining protein
digest can be analyzed by nanoelectrospray tandem mass spectrometry (Nano
ESI-MS/MS) (6). Nano ESI-MS/MS produces data that allow highly specific
database searches so that proteins that are only partially present in a database,
or relevant clones in an EST database, can be identified (7). It is important to
point out that there is no need to determine the complete sequence of peptides
in order to search a database—a short sequence stretch consisting of three to
four amino acid residues provides enough search specificity when combined
with the mass of the intact peptide and the masses of corresponding fragment
.
أعلان
عن الكتاب
تحميل كتاب Mass Spectrometry of Proteins and Peptides Humana Press pdf تأليف John R Chapman pdf مجانا ... 2000م - 1443هـ
نبذه عن الكتاب:
Recent developments in technology and instrumentation have made mass
spectrometry the method of choice for the identification of gel-separated proteins using rapidly growing sequence databases (1). Proteins with a full-length
sequence present in a database can be identified with high certainty and high
throughput using the accurate masses obtained by matrix-assisted laser desorption/ionization (MALDI) mass spectrometry peptide mapping (2). Simple protein mixtures can also be deciphered by MALDI peptide mapping (3) and the
entire identification process, starting from in-gel digestion (4) and finishing
with acquisition of mass spectra and database search, can be automated (5).
Only 1–3% of a total digest are consumed for MALDI analysis even if the
protein of interest is present on a gel in a subpicomole amount. If no conclusive
identification is achieved by MALDI peptide mapping, the remaining protein
digest can be analyzed by nanoelectrospray tandem mass spectrometry (Nano
ESI-MS/MS) (6). Nano ESI-MS/MS produces data that allow highly specific
database searches so that proteins that are only partially present in a database,
or relevant clones in an EST database, can be identified (7). It is important to
point out that there is no need to determine the complete sequence of peptides
in order to search a database—a short sequence stretch consisting of three to
four amino acid residues provides enough search specificity when combined
with the mass of the intact peptide and the masses of corresponding fragment
.
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