X-ray crystallography is currently the most favored method for structural determination of proteins and other macromolecules. The requisite for a successful X-ray crystallographic application is to obtain single crystals of the target protein. Data is then collected by diffracting X-ray from the single crystal that has an ordered pattern of atomic orientation. The assembly of atoms and molecules in the crystal can be deduced from the measurement of Xray scattering.
https://www.creative-biostructure.com/protein-crystallization_26.htm
Compare density gradient centrifugation, magnet-activated cell sorting
(MACS), and fluorescence-activated cell sorting (FACS) in the isolation of pure stem cell populations from a heterogeneous suspension
X-ray crystallography is a powerful technique used in determining the three-dimensional structure of molecules at atomic resolution. It involves the use of X-rays to probe the arrangement of atoms in a crystal lattice. The information obtained from X-ray crystallography can be used to understand the function of biomolecules such as proteins, DNA, and RNA.
Compare density gradient centrifugation, magnet-activated cell sorting
(MACS), and fluorescence-activated cell sorting (FACS) in the isolation of pure stem cell populations from a heterogeneous suspension
X-ray crystallography is a powerful technique used in determining the three-dimensional structure of molecules at atomic resolution. It involves the use of X-rays to probe the arrangement of atoms in a crystal lattice. The information obtained from X-ray crystallography can be used to understand the function of biomolecules such as proteins, DNA, and RNA.
X ray crystallography to visualize protein structure.Ritam38
This ppt discusses in detail the process of X ray Crystallography.
Made by the following 3rd year Bs-Ms students of IISER Kolkata:
B Sri Sindhu
Rasiwala Hassan Shabbir
Ritam Samanta
Himanshu Gupta
Sakshi Ajay Shrisath
Aditya Borkar
Diana Denzil Fernandez
Neha Kumari
.Sowmya
Anjali Mohan
Debanjana Mondal
Aanandita Gope
Shruti Santosh Sail
INTRODUCTION
STRUCTURAL PROTEOMICS
WHAT IS THE IMPORTANCE OF STUDY OF PROTEIN
METHODS FOR SOLVING PROTEIN STRUCTURE
1. X- RAY CRYSTALLOGRAPHY
INTRODUCTION
PROCEDURE
LIMITATIONS
2.NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE DETERMINATION
3. MASS SPECTROMETER
MALDI
ESI
STRUCTURE MODELING
APPLICATIONS
CONCLUSION
REFERENCES
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.
X-ray crystallography is one of the most favored techniques for the determination of the atomic structure of proteins, nucleic acids and other molecules. Creative Biostructure has built this X-ray crystallography platform to provide service and scientific support to customers from both industry and academia for their structural biology projects. It offers our customers the state-of-the-art tools to identify and optimize crystallization conditions as well as X-ray diffraction data processing for any macromolecule of interest.
Our understanding of life at the molecular level is highly dependent on the ability to map the molecular details of individual proteins and nucleic acids as well as their interactions with each other and with small molecules (inhibitors, cofactors, substrates, etc.). The determination of 3-D structures of proteins is crucial for the understanding of these interactions as well as their structure–function relationships, which also has many practical applications in drug design and protein engineering.
NMR spectroscopy is a key analytical technique for structure elucidation of a wide range of materials from small molecules to compounds. The technique provides detailed molecular information that allows researchers have in-depth understanding of composition, chemical structure, morphology, and dynamics. NMR is particularly useful in analysis of pharmaceuticals, screening weak-binding compounds and developing into drug-like inhibitors for drug discovery. Supported by our NMR platform, Creative Biostructure offers high quality customized services ranging from production of labeled-proteins to acquisition and analysis of high-field NMR data for researchers in science and pharmaceutical industry.
Electron microscopy (EM) has become an extremely popular method for the ultrastructural study of macromolecules, cells and tissues. An aqueous biological sample is frozen rapidly and irradiated with a beam of electrons. A detector senses how the electrons are scattered and a computer reconstructs the 3D-shape of the molecule.
X ray crystallography to visualize protein structure.Ritam38
This ppt discusses in detail the process of X ray Crystallography.
Made by the following 3rd year Bs-Ms students of IISER Kolkata:
B Sri Sindhu
Rasiwala Hassan Shabbir
Ritam Samanta
Himanshu Gupta
Sakshi Ajay Shrisath
Aditya Borkar
Diana Denzil Fernandez
Neha Kumari
.Sowmya
Anjali Mohan
Debanjana Mondal
Aanandita Gope
Shruti Santosh Sail
INTRODUCTION
STRUCTURAL PROTEOMICS
WHAT IS THE IMPORTANCE OF STUDY OF PROTEIN
METHODS FOR SOLVING PROTEIN STRUCTURE
1. X- RAY CRYSTALLOGRAPHY
INTRODUCTION
PROCEDURE
LIMITATIONS
2.NUCLEAR MAGNETIC RESONANCE
PROTEIN STRUCTURE DETERMINATION
3. MASS SPECTROMETER
MALDI
ESI
STRUCTURE MODELING
APPLICATIONS
CONCLUSION
REFERENCES
X-ray crystallography is the experimental science determining the atomic and molecular structure of a crystal, in which the crystalline structure causes a beam of incident X-rays to diffract into many specific directions. By measuring the angles and intensities of these diffracted beams, a crystallographer can produce a three-dimensional picture of the density of electrons within the crystal. From this electron density, the mean positions of the atoms in the crystal can be determined, as well as their chemical bonds, their crystallographic disorder, and various other information.
X-ray crystallography is one of the most favored techniques for the determination of the atomic structure of proteins, nucleic acids and other molecules. Creative Biostructure has built this X-ray crystallography platform to provide service and scientific support to customers from both industry and academia for their structural biology projects. It offers our customers the state-of-the-art tools to identify and optimize crystallization conditions as well as X-ray diffraction data processing for any macromolecule of interest.
Our understanding of life at the molecular level is highly dependent on the ability to map the molecular details of individual proteins and nucleic acids as well as their interactions with each other and with small molecules (inhibitors, cofactors, substrates, etc.). The determination of 3-D structures of proteins is crucial for the understanding of these interactions as well as their structure–function relationships, which also has many practical applications in drug design and protein engineering.
NMR spectroscopy is a key analytical technique for structure elucidation of a wide range of materials from small molecules to compounds. The technique provides detailed molecular information that allows researchers have in-depth understanding of composition, chemical structure, morphology, and dynamics. NMR is particularly useful in analysis of pharmaceuticals, screening weak-binding compounds and developing into drug-like inhibitors for drug discovery. Supported by our NMR platform, Creative Biostructure offers high quality customized services ranging from production of labeled-proteins to acquisition and analysis of high-field NMR data for researchers in science and pharmaceutical industry.
Electron microscopy (EM) has become an extremely popular method for the ultrastructural study of macromolecules, cells and tissues. An aqueous biological sample is frozen rapidly and irradiated with a beam of electrons. A detector senses how the electrons are scattered and a computer reconstructs the 3D-shape of the molecule.
Electron microscopy (EM) has become an extremely popular method for the ultrastructural study of macromolecules, cells and tissues. An aqueous biological sample is frozen rapidly and irradiated with a beam of electrons. A detector senses how the electrons are scattered and a computer reconstructs the 3Dshape of the molecule.
https://www.creative-biostructure.com/cryo-em-services_4.htm
Here is the updated list of Top Best Ayurvedic medicine for Gas and Indigestion and those are Gas-O-Go Syp for Dyspepsia | Lavizyme Syrup for Acidity | Yumzyme Hepatoprotective Capsules etc
These lecture slides, by Dr Sidra Arshad, offer a quick overview of the physiological basis of a normal electrocardiogram.
Learning objectives:
1. Define an electrocardiogram (ECG) and electrocardiography
2. Describe how dipoles generated by the heart produce the waveforms of the ECG
3. Describe the components of a normal electrocardiogram of a typical bipolar lead (limb II)
4. Differentiate between intervals and segments
5. Enlist some common indications for obtaining an ECG
6. Describe the flow of current around the heart during the cardiac cycle
7. Discuss the placement and polarity of the leads of electrocardiograph
8. Describe the normal electrocardiograms recorded from the limb leads and explain the physiological basis of the different records that are obtained
9. Define mean electrical vector (axis) of the heart and give the normal range
10. Define the mean QRS vector
11. Describe the axes of leads (hexagonal reference system)
12. Comprehend the vectorial analysis of the normal ECG
13. Determine the mean electrical axis of the ventricular QRS and appreciate the mean axis deviation
14. Explain the concepts of current of injury, J point, and their significance
Study Resources:
1. Chapter 11, Guyton and Hall Textbook of Medical Physiology, 14th edition
2. Chapter 9, Human Physiology - From Cells to Systems, Lauralee Sherwood, 9th edition
3. Chapter 29, Ganong’s Review of Medical Physiology, 26th edition
4. Electrocardiogram, StatPearls - https://www.ncbi.nlm.nih.gov/books/NBK549803/
5. ECG in Medical Practice by ABM Abdullah, 4th edition
6. Chapter 3, Cardiology Explained, https://www.ncbi.nlm.nih.gov/books/NBK2214/
7. ECG Basics, http://www.nataliescasebook.com/tag/e-c-g-basics
Adv. biopharm. APPLICATION OF PHARMACOKINETICS : TARGETED DRUG DELIVERY SYSTEMSAkankshaAshtankar
MIP 201T & MPH 202T
ADVANCED BIOPHARMACEUTICS & PHARMACOKINETICS : UNIT 5
APPLICATION OF PHARMACOKINETICS : TARGETED DRUG DELIVERY SYSTEMS By - AKANKSHA ASHTANKAR
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.
Basavarajeeyam is an important text for ayurvedic physician belonging to andhra pradehs. It is a popular compendium in various parts of our country as well as in andhra pradesh. The content of the text was presented in sanskrit and telugu language (Bilingual). One of the most famous book in ayurvedic pharmaceutics and therapeutics. This book contains 25 chapters called as prakaranas. Many rasaoushadis were explained, pioneer of dhatu druti, nadi pareeksha, mutra pareeksha etc. Belongs to the period of 15-16 century. New diseases like upadamsha, phiranga rogas are explained.
Basavarajeeyam is a Sreshta Sangraha grantha (Compiled book ), written by Neelkanta kotturu Basavaraja Virachita. It contains 25 Prakaranas, First 24 Chapters related to Rogas& 25th to Rasadravyas.
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
Ozempic: Preoperative Management of Patients on GLP-1 Receptor Agonists
Protein crystallization
1. Protein Crystallization
X-ray crystallography is currently the most favored method for structural determination of
proteins and other macromolecules. The requisite for a successful X-ray crystallographic
application is to obtain single crystals of the target protein. Data is then collected by
diffracting X-ray from the single crystal that has an ordered pattern of atomic orientation. The
assembly of atoms and molecules in the crystal can be deduced from the measurement of X-
ray scattering.
At present, more than 120,000 protein structures resolved by X-Ray crystallography
experiments have been deposited in protein databank, accounting for nearly 90% of the
resolved proteins, suggesting a predominant popularity of X-Ray crystallography in structural
determination.
https://www.creative-biostructure.com/protein-crystallization_26.htm
