Peptide Mass Fingerprinting | Protein Fingerprinting | PMF | Protein Identification | PENS#90

#peptidemassfingerprinting #PMF #proteinidentification
Peptide Mass Fingerprinting | Protein Fingerprinting | PMF | Protein Identification | PENS#90
Peptide mass fingerprinting (PMF) (also known as protein fingerprinting) is an analytical technique for identifying proteins by first cleaving an unknown protein of interest into smaller peptides and then mass spectrometrically analyzing them, such as MALDITOF and ESITOF. You can use the meter to accurately measure the absolute mass. This method was originally developed by several groups in 1993. Peptide mass is compared to a database or genome containing known protein sequences. This is achieved using a computer program that converts the known genome of an organism into proteins, theoretically cleaves the proteins into peptides, and calculates the absolute mass of the peptide from each protein. Next, the peptide mass of the unknown protein is compared to the theoretical peptide mass of each protein encoded in the genome. The results are statistically analyzed to find the best one.
The advantage of this method is that you only need to know the mass of the peptide. In that case, time-consuming de novo peptide sequencing is not required. The disadvantage is that the protein sequence must be present in the database of interest. In addition, most PMF algorithms assume that the peptide is derived from a single protein. The presence of the mixture can significantly complicate the analysis and affect the results. The requirements for isolated proteins are common in PMF-based protein identification. Mixtures with more than 23 proteins usually require additional use of MS / MS-based protein identification to achieve sufficient identification specificity . Therefore, a typical PMF sample is a protein isolated from a two-dimensional gel electrophoresis (2D gel) or an isolated SDS-PAGE band.
The Lectures are given Dr. Nagendra Singh aiming to spread basic understanding and awareness of biological molecules and reactions. Dr. Nagendra Singh finished his Doctoral and Post Doctoral studies from "All India Institute of Medical Sciences" (AIIMS) New Delhi. Dr. Singh has a vast experience of research and Teaching in the fields of Structure & Molecular Biology and Biochemistry, which also include Biomolecules, Proteomics, Protein Engineering and Drug Design.
Dr. Nagendra Singh currently works at the School of Biotechnology, Gautam Buddha University, Greater Noida, INDIA (www.gbu.ac.in/FacultyProfiles/.... He does research in Molecular Biology, Structural Biology and Biotechnology. His current research interest include 'Structural and functional characterization of proteins involved in RNA metabolism from human and microbial origin. Dr Singh has published over 70 research articles in intentional Journals of good repute. He has over 20 awards and honors on his name. Few of the awards include "National Academy of Sciences of India (NASI, Allahabad) young scientist award", UGC-NET, CSIR-JRF, GATE, Best Research Awards etc. Dr. Singh has participated and presented research work at over 50 national and International conferences world wide.

[@subsstation2418]

Much helpful lecture sir, thanks a ton

[@DrAlmaTammour]

Thank you very much. So informative and well explained.

[@proteinengineering007]

My pleasure @Dr. Alma Tammour