Top-down proteomics
Encyclopedia
Top-down proteomics
is a method of protein
identification that uses an ion trap
ping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry
analysis. The name is derived from the similar approach to DNA seqencing. Proteins are typically ionized by electrospray ionization
and trapped in a Fourier transform ion cyclotron resonance
(Penning trap
) or quadrupole ion trap
(Paul trap) mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron-capture dissociation or electron-transfer dissociation.
Recently, a top-down approach has been developed for mapping the connectivity of the disulfide-rich peptide hedyotide B2 . This method allows rapid characterization of the disulfide pattern of cystine-knot miniproteins such as cyclotides, conotoxin, knottin and plant defensins.
Proteomics
Proteomics is the large-scale study of proteins, particularly their structures and functions. Proteins are vital parts of living organisms, as they are the main components of the physiological metabolic pathways of cells. The term "proteomics" was first coined in 1997 to make an analogy with...
is a method of protein
Protein
Proteins are biochemical compounds consisting of one or more polypeptides typically folded into a globular or fibrous form, facilitating a biological function. A polypeptide is a single linear polymer chain of amino acids bonded together by peptide bonds between the carboxyl and amino groups of...
identification that uses an ion trap
Ion trap
An ion trap is a combination of electric or magnetic fields that captures ions in a region of a vacuum system or tube. Ion traps have a number of scientific uses such as mass spectrometery and trapping ions while the ion's quantum state is manipulated...
ping mass spectrometer to store an isolated protein ion for mass measurement and tandem mass spectrometry
Tandem mass spectrometry
Tandem mass spectrometry, also known as MS/MS or MS2, involves multiple steps of mass spectrometry selection, with some form of fragmentation occurring in between the stages.-Tandem MS instruments:...
analysis. The name is derived from the similar approach to DNA seqencing. Proteins are typically ionized by electrospray ionization
Electrospray ionization
Electrospray ionization is a technique used in mass spectrometry to produce ions. It is especially useful in producing ions from macromolecules because it overcomes the propensity of these molecules to fragment when ionized...
and trapped in a Fourier transform ion cyclotron resonance
Fourier transform ion cyclotron resonance
Fourier transform ion cyclotron resonance mass spectrometry, also known as Fourier transform mass spectrometry, is a type of mass analyzer for determining the mass-to-charge ratio of ions based on the cyclotron frequency of the ions in a fixed magnetic field...
(Penning trap
Penning trap
Penning traps are devices for the storage of charged particles using a homogeneous static magnetic field and a spatially inhomogeneous static electric field. This kind of trap is particularly well suited to precision measurements of properties of ions and stable subatomic particles which have...
) or quadrupole ion trap
Quadrupole ion trap
A quadrupole ion trap exists in both linear and 3D varieties and refers to an ion trap that uses constant DC and radio frequency oscillating AC electric fields to trap ions. It is commonly used as a component of a mass spectrometer...
(Paul trap) mass spectrometer. Fragmentation for tandem mass spectrometry is accomplished by electron-capture dissociation or electron-transfer dissociation.
Recently, a top-down approach has been developed for mapping the connectivity of the disulfide-rich peptide hedyotide B2 . This method allows rapid characterization of the disulfide pattern of cystine-knot miniproteins such as cyclotides, conotoxin, knottin and plant defensins.