1. Proteomics is the study of proteomes, which are the entire set of proteins expressed by a genome.
2. Mass spectrometry combined with separation techniques like liquid chromatography are the main tools used in proteomics to identify and characterize proteins.
3. Modern proteomics utilizes multidimensional separation methods like multiple liquid chromatography columns or liquid chromatography coupled with capillary electrophoresis prior to mass spectrometry to better resolve complex protein mixtures.
introduction to upgma software , its history and origination, basic mening of upgma, the upgma algorithm, steps to perform upgma, and its diagramatic representation of the process along with an example, its application, advantages along with the disadvantages, and its uses.
introduction to upgma software , its history and origination, basic mening of upgma, the upgma algorithm, steps to perform upgma, and its diagramatic representation of the process along with an example, its application, advantages along with the disadvantages, and its uses.
Systems biology & Approaches of genomics and proteomicssonam786
This presentation provides the basic understanding of varous genomics and proteomics techniques.Systems biology studies life as a system .It includes the study of living system using various omic technologies .
Proteomics is the study of the proteome, the full protein complement of organisms e.g. plasma, cells and tissue.
Understanding the proteome allows for:
Characterisation of proteins
Understanding protein interactions
Identification of disease biomarkers
Proteomics and its applications in phytopathologyAbhijeet Kashyap
Dear friends, I Abhijeet kashyap presenting the basics of proteomics to you all . Proteomics is the large-scale study of proteins, particularly their structures and functions.Proteomics helps in understanding the structure and function of different proteins as well as protein-protein interactions of an organism.
Functional proteomics, methods and toolsKAUSHAL SAHU
INTRODUCTION
HISTORY
DEFINITION
PROTEOMICS
FUNCTIONAL PROTEOMICS
PROTEOMICS SOFTWARE
PROTEOMICS ANALYSIS
TOOLS FOR PROTEOM ANALYSIS
DIFFERENTS METHODS FOR STUDY OF FUNCTIONAL PROTEOMICS
APLLICATIONS
LIMITATIONS
CONCLUSION
With the DNA sequences of more than 90 genomes completed, as well as a draft sequence of the human genome, a major challenge in modern biology is to understand the expression, function, and regulation of the entire set of proteins encoded by an organism—the aims of the new field of proteomics. This information will be invaluable for understanding how complex biological processes occur at a molecular level, how they differ in various cell types, and how they are altered in disease states. The term proteomics describes the study and characterization of a complete set of proteins present in a cell, organ, or organism at a given time.
In general, proteomic approaches can be used (a) for proteome profiling, (b) for comparative expression analysis of two or more protein samples, (c) for the localization and identification of posttranslational modifications, and (d) for the study of protein-protein interactions. The human genome harbours 26000–31000 protein-encoding genes; whereas the total number of human protein products, including splice variants and essential posttranslational modifications (PTMs), has been estimated to be close to one million. It is evident that most of the functional information on the genes resides in the proteome, which is the sum of multiple dynamic processes that include protein phosphorylation, protein trafficking, localization, and protein-protein interactions. Moreover, the proteomes of mammalian cells, tissues, and body fluids are complex and display a wide dynamic range of proteins concentration one cell can contain between one and more than 100000 copies of a single protein.
A rapidly emerging set of key technologies is making it possible to identify large numbers of proteins in a mixture or complex, to map their interactions in a cellular context, and to analyze their biological activities. Mass spectrometry has evolved into a versatile tool for examining the simultaneous expression of more than 1000 proteins and the identification and mapping of posttranslational modifications. High-throughput methods performed in an array format have enabled large-scale projects for the characterization of protein localization, protein-protein interactions, and the biochemical analysis of protein function. Finally, the plethora of data generated in the last few years has led to approaches for the integration of diverse data sets that greatly enhance our understanding of both individual protein function and elaborate biological processes.
Systems biology & Approaches of genomics and proteomicssonam786
This presentation provides the basic understanding of varous genomics and proteomics techniques.Systems biology studies life as a system .It includes the study of living system using various omic technologies .
Proteomics is the study of the proteome, the full protein complement of organisms e.g. plasma, cells and tissue.
Understanding the proteome allows for:
Characterisation of proteins
Understanding protein interactions
Identification of disease biomarkers
Proteomics and its applications in phytopathologyAbhijeet Kashyap
Dear friends, I Abhijeet kashyap presenting the basics of proteomics to you all . Proteomics is the large-scale study of proteins, particularly their structures and functions.Proteomics helps in understanding the structure and function of different proteins as well as protein-protein interactions of an organism.
Functional proteomics, methods and toolsKAUSHAL SAHU
INTRODUCTION
HISTORY
DEFINITION
PROTEOMICS
FUNCTIONAL PROTEOMICS
PROTEOMICS SOFTWARE
PROTEOMICS ANALYSIS
TOOLS FOR PROTEOM ANALYSIS
DIFFERENTS METHODS FOR STUDY OF FUNCTIONAL PROTEOMICS
APLLICATIONS
LIMITATIONS
CONCLUSION
With the DNA sequences of more than 90 genomes completed, as well as a draft sequence of the human genome, a major challenge in modern biology is to understand the expression, function, and regulation of the entire set of proteins encoded by an organism—the aims of the new field of proteomics. This information will be invaluable for understanding how complex biological processes occur at a molecular level, how they differ in various cell types, and how they are altered in disease states. The term proteomics describes the study and characterization of a complete set of proteins present in a cell, organ, or organism at a given time.
In general, proteomic approaches can be used (a) for proteome profiling, (b) for comparative expression analysis of two or more protein samples, (c) for the localization and identification of posttranslational modifications, and (d) for the study of protein-protein interactions. The human genome harbours 26000–31000 protein-encoding genes; whereas the total number of human protein products, including splice variants and essential posttranslational modifications (PTMs), has been estimated to be close to one million. It is evident that most of the functional information on the genes resides in the proteome, which is the sum of multiple dynamic processes that include protein phosphorylation, protein trafficking, localization, and protein-protein interactions. Moreover, the proteomes of mammalian cells, tissues, and body fluids are complex and display a wide dynamic range of proteins concentration one cell can contain between one and more than 100000 copies of a single protein.
A rapidly emerging set of key technologies is making it possible to identify large numbers of proteins in a mixture or complex, to map their interactions in a cellular context, and to analyze their biological activities. Mass spectrometry has evolved into a versatile tool for examining the simultaneous expression of more than 1000 proteins and the identification and mapping of posttranslational modifications. High-throughput methods performed in an array format have enabled large-scale projects for the characterization of protein localization, protein-protein interactions, and the biochemical analysis of protein function. Finally, the plethora of data generated in the last few years has led to approaches for the integration of diverse data sets that greatly enhance our understanding of both individual protein function and elaborate biological processes.
Metabolomics is often described as the study of “the complete set of low molecular weight intermediates, which are context dependent, varying according to the physiology, developmental or pathological state of the cell, tissue, organ or organism”. In fact, metabolomics is a new term for an old science in which classical biochemical concepts are investigated. New and unique to the current research that is being conducted is the combination with genomics information and full system biology. In this refocus we will discuss the challenges in today's metabolomics research and how to address them
Combining Reichert’s SPR Systems With Other Informative TechniquesReichertSPR
The webinar focus is on how Reichert's Surface Plasmon Resonance (SPR) systems can generate additional valuable information that is not attainable on other commercial SPR platforms. SPR has traditionally been used as a research tool to characterize biomolecular interactions including the kinetics, affinity, and thermodynamics of the molecules under study. Reichert SPR systems can routinely carry out these traditional applications but have the added capability to interface with other analytical techniques and instruments. A recent example is that we have developed a system called SPR-PLUS that employs a gradient pump that can accelerate the discovery process by changing experimental variables such pH or buffer concentration in one experiment. Furthermore, this SPR-PLUS system can also easily combine a small chromatography column in series, so that additional separations before or after the initial binding experiment can be carried out in a single setup. Lastly, Reichert's open architecture creates the ability to combine SPR with other techniques such as Mass Spectrometry (MS) or Electrochemistry (Echem) so users can discover more about what is binding (MS) and also how changing potentials affects binding (Echem) to name a few potential applications.
Hyphenated technique is a combination or coupling of two analytical techniques with the help of proper interface.
In this presentation Hyphenated techniques-LC-MS/MS, GC-MS/MS, HPTLC-MS has been discussed
ARTIFICIAL INTELLIGENCE IN HEALTHCARE.pdfAnujkumaranit
Artificial intelligence (AI) refers to the simulation of human intelligence processes by machines, especially computer systems. It encompasses tasks such as learning, reasoning, problem-solving, perception, and language understanding. AI technologies are revolutionizing various fields, from healthcare to finance, by enabling machines to perform tasks that typically require human intelligence.
Tom Selleck Health: A Comprehensive Look at the Iconic Actor’s Wellness Journeygreendigital
Tom Selleck, an enduring figure in Hollywood. has captivated audiences for decades with his rugged charm, iconic moustache. and memorable roles in television and film. From his breakout role as Thomas Magnum in Magnum P.I. to his current portrayal of Frank Reagan in Blue Bloods. Selleck's career has spanned over 50 years. But beyond his professional achievements. fans have often been curious about Tom Selleck Health. especially as he has aged in the public eye.
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Introduction
Many have been interested in Tom Selleck health. not only because of his enduring presence on screen but also because of the challenges. and lifestyle choices he has faced and made over the years. This article delves into the various aspects of Tom Selleck health. exploring his fitness regimen, diet, mental health. and the challenges he has encountered as he ages. We'll look at how he maintains his well-being. the health issues he has faced, and his approach to ageing .
Early Life and Career
Childhood and Athletic Beginnings
Tom Selleck was born on January 29, 1945, in Detroit, Michigan, and grew up in Sherman Oaks, California. From an early age, he was involved in sports, particularly basketball. which played a significant role in his physical development. His athletic pursuits continued into college. where he attended the University of Southern California (USC) on a basketball scholarship. This early involvement in sports laid a strong foundation for his physical health and disciplined lifestyle.
Transition to Acting
Selleck's transition from an athlete to an actor came with its physical demands. His first significant role in "Magnum P.I." required him to perform various stunts and maintain a fit appearance. This role, which he played from 1980 to 1988. necessitated a rigorous fitness routine to meet the show's demands. setting the stage for his long-term commitment to health and wellness.
Fitness Regimen
Workout Routine
Tom Selleck health and fitness regimen has evolved. adapting to his changing roles and age. During his "Magnum, P.I." days. Selleck's workouts were intense and focused on building and maintaining muscle mass. His routine included weightlifting, cardiovascular exercises. and specific training for the stunts he performed on the show.
Selleck adjusted his fitness routine as he aged to suit his body's needs. Today, his workouts focus on maintaining flexibility, strength, and cardiovascular health. He incorporates low-impact exercises such as swimming, walking, and light weightlifting. This balanced approach helps him stay fit without putting undue strain on his joints and muscles.
Importance of Flexibility and Mobility
In recent years, Selleck has emphasized the importance of flexibility and mobility in his fitness regimen. Understanding the natural decline in muscle mass and joint flexibility with age. he includes stretching and yoga in his routine. These practices help prevent injuries, improve posture, and maintain mobilit
Recomendações da OMS sobre cuidados maternos e neonatais para uma experiência pós-natal positiva.
Em consonância com os ODS – Objetivos do Desenvolvimento Sustentável e a Estratégia Global para a Saúde das Mulheres, Crianças e Adolescentes, e aplicando uma abordagem baseada nos direitos humanos, os esforços de cuidados pós-natais devem expandir-se para além da cobertura e da simples sobrevivência, de modo a incluir cuidados de qualidade.
Estas diretrizes visam melhorar a qualidade dos cuidados pós-natais essenciais e de rotina prestados às mulheres e aos recém-nascidos, com o objetivo final de melhorar a saúde e o bem-estar materno e neonatal.
Uma “experiência pós-natal positiva” é um resultado importante para todas as mulheres que dão à luz e para os seus recém-nascidos, estabelecendo as bases para a melhoria da saúde e do bem-estar a curto e longo prazo. Uma experiência pós-natal positiva é definida como aquela em que as mulheres, pessoas que gestam, os recém-nascidos, os casais, os pais, os cuidadores e as famílias recebem informação consistente, garantia e apoio de profissionais de saúde motivados; e onde um sistema de saúde flexível e com recursos reconheça as necessidades das mulheres e dos bebês e respeite o seu contexto cultural.
Estas diretrizes consolidadas apresentam algumas recomendações novas e já bem fundamentadas sobre cuidados pós-natais de rotina para mulheres e neonatos que recebem cuidados no pós-parto em unidades de saúde ou na comunidade, independentemente dos recursos disponíveis.
É fornecido um conjunto abrangente de recomendações para cuidados durante o período puerperal, com ênfase nos cuidados essenciais que todas as mulheres e recém-nascidos devem receber, e com a devida atenção à qualidade dos cuidados; isto é, a entrega e a experiência do cuidado recebido. Estas diretrizes atualizam e ampliam as recomendações da OMS de 2014 sobre cuidados pós-natais da mãe e do recém-nascido e complementam as atuais diretrizes da OMS sobre a gestão de complicações pós-natais.
O estabelecimento da amamentação e o manejo das principais intercorrências é contemplada.
Recomendamos muito.
Vamos discutir essas recomendações no nosso curso de pós-graduação em Aleitamento no Instituto Ciclos.
Esta publicação só está disponível em inglês até o momento.
Prof. Marcus Renato de Carvalho
www.agostodourado.com
These simplified slides by Dr. Sidra Arshad present an overview of the non-respiratory functions of the respiratory tract.
Learning objectives:
1. Enlist the non-respiratory functions of the respiratory tract
2. Briefly explain how these functions are carried out
3. Discuss the significance of dead space
4. Differentiate between minute ventilation and alveolar ventilation
5. Describe the cough and sneeze reflexes
Study Resources:
1. Chapter 39, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 34, Ganong’s Review of Medical Physiology, 26th edition
3. Chapter 17, Human Physiology by Lauralee Sherwood, 9th edition
4. Non-respiratory functions of the lungs https://academic.oup.com/bjaed/article/13/3/98/278874
TEST BANK for Operations Management, 14th Edition by William J. Stevenson, Ve...kevinkariuki227
TEST BANK for Operations Management, 14th Edition by William J. Stevenson, Verified Chapters 1 - 19, Complete Newest Version.pdf
TEST BANK for Operations Management, 14th Edition by William J. Stevenson, Verified Chapters 1 - 19, Complete Newest Version.pdf
Knee anatomy and clinical tests 2024.pdfvimalpl1234
This includes all relevant anatomy and clinical tests compiled from standard textbooks, Campbell,netter etc..It is comprehensive and best suited for orthopaedicians and orthopaedic residents.
Ozempic: Preoperative Management of Patients on GLP-1 Receptor Agonists Saeid Safari
Preoperative Management of Patients on GLP-1 Receptor Agonists like Ozempic and Semiglutide
ASA GUIDELINE
NYSORA Guideline
2 Case Reports of Gastric Ultrasound
micro teaching on communication m.sc nursing.pdfAnurag Sharma
Microteaching is a unique model of practice teaching. It is a viable instrument for the. desired change in the teaching behavior or the behavior potential which, in specified types of real. classroom situations, tends to facilitate the achievement of specified types of objectives.
2. The completion of sequencing the human genome belongs to the ground breaking
discoveries in life science during the past decade.
The accomplishment of the complete genome also brings along a new and more
challenging task for scientists: The Characterization of the Human Proteome.
3. • The term “proteome” was used first in 1994 and describes a set of all
proteins expressed by a given genome.
• A protein, the basic unit of a proteome, is a molecule composed of one or
more long chain amino acid residues, further forming secondary, tertiary,
and quaternary three dimensional structures.
4. • Proteomics, the main tool for proteome research, is a relatively new and
extremely dynamically evolving branch of science, focused on the
evaluation of gene expression at proteome level.
• Current proteomics deals with different issues, such as:
Protein identification
Quantification
Characterization of posttranslational modification
Structure and function elucidation
Description of possible interactions
5. Approaches of
proteomics analysis
Sequence a few
peptide fragments and
match these sequences
with a previous mass
spectra libraries
De novo sequencing
when neither genomic
sequencing information
nor sufficient mass
spectrum data available
6. • The rapid development of proteomics during the past years was made
possible by progress in analytical instrumentation, especially in mass
spectrometry (MS).
• Beside the advances in technologies and methodologies dealing with
protein or peptide separation and sample complexity reduction, mainly in
liquid chromatography and electrophoretic techniques.
7. • The principle of chromatographic fractionation is based on the
interaction of the proteins or peptides with the stationary phase
and the mobile phase with instrumentation similar to that used in
conventional HPLC .
• The only difference is the magnitude of the flow rate (nl/min).
• The interaction may be:
Adsorption on silica surfaces
Partitioning on reversed-phase materials
Ion exchange
Affinity
Size exclusion
8. • The ever-increasing demand for more selectivity, sensitivity and
specificity has led to three main developments:
Improvements in existing RP hydrophobic stationary phases, allowing
operation with very low or no trifluoroacetic acid (TFA)
The emergence of monolithic columns, whose separation medium consists of
a continuous, rigid polymeric rod with a porous structure, enabling faster
separations
The development of miniaturized columns in a chip format
9. A multidimensional (i.e., 2D or 3D) method that combines separation
methods with different separation mechanisms with the following
advantages:
Significantly improve the chances of resolving a complex mixture of proteins
into its individual constituents
Extensive fractionation lowers the dynamic range requirements on the
instrumental technology (i.e., MS) used to detect the individual protein or
peptide species
It maximizes the overall peak capacity
10. • Mass spectrometers consist of three basic components:
An ion source
A mass analyzer
An ion detector
• It requires a method to transfer molecules from solution or
solid phase into an ionized gaseous phase either by:
Matrix assisted laser desorption/ionization (MALDI)
Electrospray ionization (ESI)
11.
12. It has made ESI more convenient for solid sample analysis
Large biomolecules have also been successfully detected
Ambient desorption electrospray ionization (DESI)
13. • After ionization, the sample reaches the mass analyzer, which separates
ions by their mass-to-charge (m/z) ratios. Ion motion in the mass analyzer
can be manipulated by electric or magnetic fields to direct ions to a
detector.
• Four basic types:
Time-of-flight (TOF)
Ion trap
Quadrupole (Q)
Fourier transform ion cyclotron resonance (FTICR)
14. • All four types differ in:
Sensitivity
Resolution
Mass accuracy
The possibility to fragment peptide ions
• Hybrid TOF/TOF, Q/TOF and ion trap/FTICR instruments can be also used
resulting in fragment ion spectra which are often more extensive and
informative and combining the advantages of each technique.
15. • This technique based on spectral counting or the comparison of signal
intensities across samples in a narrow m/z range.
• There are two types of quantitation:
Label-free quantitation
Label-based quantitation
16. • The basis of this approach is that the peak height or the area of a peak at a
selected mass-to-charge ratio is obtained by counting the number of ions
forming this peak (i.e. Spectral counting)
• The disadvantage is that the more abundant proteins can mask the
proteins of low abundance.
23. • Phosphorylated proteins and peptides show a high affinity towards metal ions
and form quite stable complexes with these ions.
• The most frequently used ions are Fe3+, Ga2+, Ni2+, Cr2+, Al3+, Zn2+ and Cu2+.
Metal cations are chelated by a multidentate ligand, which is immobilized onto
a support material.
24. • Unfortunately, it is not only the phosphopeptides which bind on to such a
column, but also the acidic non-phosphopeptides.
• In order to minimize this nonspecific binding, all free carboxyl groups of
the peptides in solution have been converted to the corresponding methyl
esters and then analyzed with IMAC followed by nano HPLC-MS.
25.
26. Advantages of monolithic columns in comparison to conventional HPLC
columns:
Easier preparation and functionalization
Enhanced mass transfer
Higher column efficiency
More robust
27. However, monolithic columns suffer from one very important limitation:
They are very often and very easily overloaded.
One possible way to resolve this problem is to use serial linkage of these
columns.
28. • Monolithic columns can allow the use of online enzymatic reactors.
• Trypsin has been immobilized on a monolithic column and compared to
the off-line in-solution digestion.
• The offline digestion took about 12 h, whereas a digestion of comparable
efficiency on the monolithic column took about 30 s.
• This approach needs further tuning but it seems to be promising in terms
of increasing the sample throughput.
29. • Another important aspect of future development is the miniaturization of
instrumentation, primarily of the separation columns.
• There are many publications describing miniaturized chips and their use
for separation of proteins and peptides.
• These chips suffered from high dead volumes and high chemical
background in MS, originating from the glue for the tips.
• Furthermore, the majority of chip developments focused on
electrophoresis.
30. • The development of a new chip designed to use existing nano-HPLC and
MS hardware and the use of a nano-HPLC chip for RP and 2D separation of
peptides obtained through tryptic digest of rat plasma were reported.
31. • Decreasing the particle size of the stationary phase by a factor of 2, from 3
to 1.5 µm, would increase the backpressure 4-fold (pressure is inversely
proportional to the square of the particle size).
• This would improve the peak shape and increase the column resolution.
• The use of UPLC for functional genomic discrimination of metabolic
phenotypes has been reported.
• The results achieved with UPLC were significantly better in comparison to
the results achieved with conventional HPLC.
32. Advantages of HPLC and CE multidimensional procedures:
They can be automated
Sensitive
Reproducible
Fast
Can be used for quantitative work
33. • The on-line LC-CE-ESI-FTICR-MS was employed to study the bovine serum
albumin (BSA) tryptic digestion product.
• Low detection limits were found (low ng/ml), while a high sequence
coverage (93 %) was obtained using this multidimensional set-up.
• An LC-CE-MS coupling was also used to separate peptides enabling protein
identification in complex mixtures.
35. • A similar strategy has been used for the analysis of human saliva and
mouse brain mitochondrial proteome.
• The strategy consisted of an off-line coupling of CE to nano-RP LC-ESI-MS
via a fraction collector.
• CE enables in-capillary sample concentration for the use of larger volume
injections.
• The developed CE-LC-MS method:
Resulted in complementary data
Resulted in higher number of detected mouse mitochondrial peptides and
proteins
36. Modern separation methods (LC and CE) have been used in a multidimensional format,
LC/LC or LC-CE for the separation of proteins/peptides combined with MS for protein
identification and profiling.
37. • MS-based proteomics by the rapid development of mass analyzers with
higher mass resolution and superior sequencing capabilities, along with
separation systems has established itself as the leading technology for a
high-throughput qualitative and quantitative analysis of protein mixtures.
• However, the analysis of difficult types of proteins that are present at low
abundance, hydrophobic, or extensively modified, remains to be
challenging and will require further development of improved analytical
tools and methodologies.
Editor's Notes
posttranslational modifications (PTMs) [which are processing events that change the properties of a protein by proteolytic cleavage or by covalent addition of a modifying group to one or more amino acids]
TFA used to sharpen the peaks in protein analysis.
Protein phosphorylation is a post-translational modification of proteins in which a serine, a threonine or a tyrosine residue is phosphorylated by a protein kinase by the addition of a covalently bound phosphate group. Regulation of proteins by phosphorylation is one of the most common modes of regulation of protein function, and is often termed "phosphoregulation". In almost all cases of phosphoregulation, the protein switches between a phosphorylated and an unphosphorylated form, and one of these two is an active form, while the other one is an inactive form.