Search results “Determining protein structure by nmr spectra”
Peptide NMR: The Basics
Here is a very short, simplified, and rough animation describing the very core of NMR and peptide NMR. Be sure to check out other, detailed NMR videos on youtube if you wish to learn the topic. This is aimed to give you a broad idea. Also, this is part of a bigger series. Future updates are to come on the topic, so stay tuned and subscribe. Enjoy...
Views: 5153 Dipan Ghosh
Protein NMR - using 1D, 2D and 3D experiments to solve structure
In this video, I will talk briefly about how solution NMR can be used to solve the structure of a protein molecule.
Views: 922 Renuk Lakshman
NMR spectroscopy
NMR spectroscopy lecture by Suman Bhattacharjee - This lecture explains about the NMR spectroscopy basics. Nuclear magnetic resonance spectroscopy, most commonly known as NMR spectroscopy, is a research technique that exploits the magnetic properties of certain atomic nuclei. It determines the physical and chemical properties of atoms or the molecules in which they are contained. It relies on the phenomenon of nuclear magnetic resonance and can provide detailed information about the structure, dynamics, reaction state, and chemical environment of molecules. The intramolecular magnetic field around an atom in a molecule changes the resonance frequency, thus giving access to details of the electronic structure of a molecule. Most frequently, NMR spectroscopy is used by chemists and biochemists to investigate the properties of organic molecules, although it is applicable to any kind of sample that contains nuclei possessing spin. Suitable samples range from small compounds analyzed with 1-dimensional proton or carbon-13 NMR spectroscopy to large proteins or nucleic acids using 3 or 4-dimensional techniques. The impact of NMR spectroscopy on the sciences has been substantial because of the range of information and the diversity of samples, including solutions and solids. NMR spectra are unique, well-resolved, analytically tractable and often highly predictable for small molecules. Thus, in organic chemistry practice, NMR analysis is used to confirm the identity of a substance. Different functional groups are obviously distinguishable, and identical functional groups with differing neighboring substituents still give distinguishable signals. NMR has largely replaced traditional wet chemistry tests such as color reagents for identification. A disadvantage is that a relatively large amount, 2–50 mg, of a purified substance is required, although it may be recovered. Preferably, the sample should be dissolved in a solvent, because NMR analysis of solids requires a dedicated MAS machine and may not give equally well-resolved spectra. The timescale of NMR is relatively long, and thus it is not suitable for observing fast phenomena, producing only an averaged spectrum. Although large amounts of impurities do show on an NMR spectrum, better methods exist for detecting impurities, as NMR is inherently not very sensitive. NMR spectrometers are relatively expensive; universities usually have them, but they are less common in private companies. Modern NMR spectrometers have a very strong, large and expensive liquid helium-cooled superconducting magnet, because resolution directly depends on magnetic field strength. Less expensive machines using permanent magnets and lower resolution are also available, which still give sufficient performance for certain application such as reaction monitoring and quick checking of samples. There are even benchtop NMR spectrometers. This important and well-established application of nuclear magnetic resonance will serve to illustrate some of the novel aspects of this method. To begin with, the nmr spectrometer must be tuned to a specific nucleus, in this case the proton. The actual procedure for obtaining the spectrum varies, but the simplest is referred to as the continuous wave (CW) method. A typical CW-spectrometer is shown in the following diagram. Article source - Wikipedia.org For more information, log on to- http://www.shomusbiology.com/ Get Shomu's Biology DVD set here- http://www.shomusbiology.com/dvd-store/ Download the study materials here- http://shomusbiology.com/bio-materials.html Remember Shomu’s Biology is created to spread the knowledge of life science and biology by sharing all this free biology lectures video and animation presented by Suman Bhattacharjee in YouTube. All these tutorials are brought to you for free. Please subscribe to our channel so that we can grow together. You can check for any of the following services from Shomu’s Biology- Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching We are social. Find us on different sites here- Our Website – www.shomusbiology.com Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching NMR spectroscopy lecture by Suman Bhattacharjee.
Views: 364748 Shomu's Biology
Determining Protein Struture
http://www.aklectures.com/lecture/determining-protein-structure-part-i https://www.facebook.com/aklectures The website organizes the videos into clear and structured chapters that you can use to watch the videos in sequential and logical order as taught by most educational institutions. Each lecture contains a description along with a customized comment section that you can use to ask questions regarding the topic. Posting questions on the site allows us to answer them much quicker than on YouTube. This site was created for the purpose of providing students access to a quality education in the sciences and we are continually working on improving the website's functionality and features. http://www.aklectures.com
Views: 5635 AK LECTURES
NMR Spectroscopy- Structure Determination of Organic Compound using NMR data
Link for spectral data table: http://www.chemohollic.com/2018/05/important-spectroscopic-data-tables-ir.html In this video we will learn, how to determine structure of an organic compound using NMR data. Espectroscopía de RMN NMR spektroskopija NMR zowonetserako zojambulajambula NMR spektroskopií NMR-spectroscopie Spectroscopie RMN NMR φασματοσκοπία Spektroskopi NMR NMR分光法 ЯМР спектроскопияга NMR स्पेक्ट्रोस्कोपी Espectroscopia de RMN НМР спектроскопија NMR-spektroskopi -phổ phổ NMR
Views: 28500 All 'Bout Chemistry
NMR, its applications and the Dutch uNMR-NL facility
What is nuclear magnetic resonance (NMR) and what can we do with it? This video, produced for the occasion of the official opening of the uNMR-NL research facility at the Bijvoet Center for Biomolecular Research of Utrecht University in the Netherlands, shows how, with NMR spectroscopy, we can determine the structure of molecules to help develop the materials, food and medicine of the future. An NMR spectrometer works using the same principle as an MRI scanner in a hospital, in order to visualise the structure of molecules. Molecules are the foundation for life and for the materials that we as humans can make. In order to understand the role a specific protein plays in the development of cancer, or why a new nanomaterial displays certain properties, you have to understand the structure of the molecules. The uNMR-NL research facility at Utrecht University was opened by State Secretary for Education, Culture and Science of the Netherlands Sander Dekker on Thursday, 5 November, 2015. With its ultra-powerful 22 Tesla magnet, uNMR-NL is among the world’s leading NMR facilities, allowing researchers to study very large molecules for the first time, with an extremely high spectral resolution. The magnet can be used for chemical, biological, and materials science research. The uNMR-NL facility was set up by the universities of Utrecht, Eindhoven, Leiden, Nijmegen and Wageningen in cooperation with the public-private institute for analytical chemistry COAST and is part of the National Road Map programme for large-scale research facilities of the Netherlands Organisation for Scientific Research NWO. Website of uNMR-NL: http://www.unmr.nl Produced by Sensu: http://www.sensu.org
Protein Structure Prediction and Determination - Dr. Ram Mettu, Tulane University
Dr. Mettu's research interests are in algorithms, machine learning and computational biology. Specifically, his work is focused on the design and analysis of algorithms with guarantees on running time and solution quality that are motivated by, and are necessary for, problems in computational biology. Applications of my work include protein structure prediction and determination, protein-protein interactions, compound screening, as well as problems in high-throughput sequencing and proteomics. http://tulane.edu/sse/cs/faculty/ramgopal-mettu.cfm Filmed and edited by Patrick Niddrie: http://www.patrickniddrie.com
Views: 6533 Tulane University
NMR Made Easy! Part 6A - NMR to Molecule Structure - Organic Chemistry
Hey guys guess what?!?! My 8 months late videos are finally up! NMRs Part 6A and 6B are perfect in case any of you are still having any problems with NMRs or know someone who is. In this video I go over Degrees of Unsaturation, Integration, my Awesome Table that organizes the NMRs information and we put it altogether to get the structure of our mysterious molecule. Hope you guys like it ;) ●Become a Patron + Free Tutoring Lottery! http://www.Patreon.com/OrgoMadeEasy ●Private Tutoring Information: I offer in-person private tutoring in Boston and NYC, and if you live elsewhere on this awesome planet I offer online Skype tutoring that is accompanied with a whiteboard program. For more info check here: http://orgomadeeasy.org/private-tutoring/ and contact me via my "Orgo Made Easy" Facebook page or email: [email protected] ●NMR 1/6 Electronegativity and Shielding(NMRs) http://www.youtube.com/watch?v=9orcRVTKcS0 ●NMR 2/6 Equivalent Hydrogens- http://www.youtube.com/watch?v=NZ7KCwFRzp8 ●NMR 2.5/6 Equivalent Hs Part II http://www.youtube.com/watch?v=9B7w8dK7yiI ●NMR 3/6 What NMRs Tell Us- http://youtu.be/wi-evRDwDGQ ●NMR 4/6 Molecules to NMR- http://www.youtube.com/watch?v=uB5emmz9Kn4 ●NMR 5/6 Complex Splitting- http://www.youtube.com/watch?v=1IKHQwU1Evs ●NMR 6A/6 NMR to Molecules- https://www.youtube.com/watch?v=5Uy7GiRaV2A ●NMR 6B/6 NMR to Molecules- https://www.youtube.com/watch?v=yJ6ChsVZTmE Make sure you share this with your friends if you found it helpful, and I would love it if you leave some comments to let me know if I'm on the right track ;). Subscribe to get updated when I make new videos! https://www.youtube.com/user/OrgoMadeEasy Connect with me on Facebook/Instagram/Twitter! Official Website-----------------------http://OrgoMadeEasy.org/ Facebook-------------------------------https://Facebook.com/OrgoMadeEasy Instagram-------------------------------http://Instagram.com/FrankMWong Tweet Tweet---------------------------https://Twitter.com/OrgoMadeEasy Help Support Me Here--------------http://www.Patreon.com/OrgoMadeEasy
Views: 236680 Frank Wong
WeNMR lecture on structure detemination of biomolecules by NMR given by Prof. A. Rosato
A lecture about structure determination of biomolecules by NMR given by Prof. Antonio Rosato from the University of Florence at the WeNMR workshop (http://www.wenmr.eu) in Taipei, March 2013, at the occasion of the International Symposium on Cloud and Grid Computing (http://event.twgrid.org/isgc2013).
Views: 2756 WeNMR/West-Life VRC
Experimental Determination of Protein Structure - Bioinformatics-I (Lecture 177)
Bioinformatics Protein Structures Experimental Determination of Protein Structure
Draw the NMR Spectrum of ethanol
How to predict and draw the hydrogen (1H) NMR spectrum of an alcohol (ethanol). Find the equivalent hydrogens, determine the peak splitting and then draw each set of peaks at the appropriate chemical shift. Check me out: http://www.chemistnate.com
Views: 91276 chemistNATE
A New Approach to NMR-Based Protein Structure
(1992) This is a video that demonstrates the medical scientific uses of visualization technology. The video, created in collaboration with Dr. Michael E. Johnson, Director of the Center for Biotechnology at the University of Illinois, Chicago, introduces a new software approach to NMR-Based protein structure determination developed at the Center for Biotechnology's Bimolecular Analysis Laboratory. The program's developers are introduced and each demonstrated the functionality and advances of the new software. The developers include; Dr. Simon Sherman, a mathematical physicist who developed the basic algorithms, Dr. Leela Kar, an NMR spectroscopist who developed the applications, and Alan Verlo, a computer visualization specialist who developed the program's visualizations. The video introduces the new program and shows the program's functionality, it's visualizations, and explains the medical and potentially therapeutic benefits to the use of this technology.
Views: 11209 evltube
Restrained Molecular Dynamics structure determination of protein 1GB1 from nmr. OpenCL-3d-hd
structure determinatio of 1GB1 using simulated annealing. Restrained molecular dynamics implemented in OpenCL. SA protocol: sa.inp from program Xplor-Nih. Initial protein configuration: extended strand 3d rendering: pymol encoding: x264
Views: 1095 istispl
NMR Spectroscopy
Looking for some more organic chemistry practice? Try http://www.studyorgo.com and ace that test. Use the coupon code “Dave” and save 20% right away! What are these things?! All the lines! Splitting? Integration? This is the most confusing thing I've ever seen! OK, take it easy chief. Let Professor Dave take you through the very basics of interpreting NMR spectra. To support this channel and keep up on STEM news at the same time, click on the link below and subscribe to this FREE newsletter: http://www.jdoqocy.com/click-9021241-13591026 Subscribe: http://bit.ly/ProfDaveSubscribe [email protected] http://patreon.com/ProfessorDaveExplains http://professordaveexplains.com http://facebook.com/ProfessorDaveExpl... http://twitter.com/DaveExplains General Chemistry Tutorials: http://bit.ly/ProfDaveGenChem Organic Chemistry Tutorials: http://bit.ly/ProfDaveOrgChem Biochemistry Tutorials: http://bit.ly/ProfDaveBiochem Classical Physics Tutorials: http://bit.ly/ProfDavePhysics1 Modern Physics Tutorials: http://bit.ly/ProfDavePhysics2 Mathematics Tutorials: http://bit.ly/ProfDaveMaths Biology Tutorials: http://bit.ly/ProfDaveBio American History Tutorials: http://bit.ly/ProfDaveAmericanHistory
Views: 290091 Professor Dave Explains
Proton NMR of ethyl acetate : JGEEBILS 2018 question (chemistry part)
This video is about the basics tips that can be learned to predict Proton NMR spectral graph of any compound. Here ethyle acetate has been explained . Proton NMR is a type of Nuclear Magnetic Resonance Spectroscopy which can be used to determine structure of any compound. In Life Sciences research this spectroscopy is used to determine the structure of peptides and proteins in solution. For any type of queries regarding the concept leave a comment below. If you like this then subscribe and share this video .
Comparison of Single crystal X-ray diffraction, NMR and Cryo-EM
A video on the comparison of single crystal X-ray diffraction, NMR, and Cryo-EM, which could help you to chose the analysis method when you need the structure details.
NMR Structure Determination
This video is captured using TinyTake. http://tinytake.com
Views: 547 Martin Moxon
362L Structure Determination by NMR (#1)
Proton (1H) and carbon (13C) NMR spectra for ethyl acetate, 4-methyl-2-pentanone, and 2-heptanone are obtained and analyzed using a JOEL 400MHz NMR. Breanne McGee helped develop this experiment. Chemistry Lab at Eastern Kentucky University, U.S. www.youtube.com/user/ekuchemlab
Views: 1062 eku_chem_lab
NMR for Protein Structure Determination & Dynamics II ; M. multicellularis: Magnetic Organism I
Originally Titled : NMR for Protein Structural Determination and Dynamics, part 2; Magnetoglobus Multicellularis: magnetic organism, part 1 Part (2/2) : NMR for Protein Structural Determination and Dynamics + Part (1/2) : Magnetoglobus Multicellularis : Magnetic Organism Hits on scivee.tv prior to youtube upload: 1036
Views: 293 ICAM - I2CAM
Towards Automation of Protein NMR
Protein structure is the key to deciphering its function and biological role. Nuclear Magnetic Resonance (NMR) spectroscopy is one of the major experimental protein structure determination methods. Manual NMR process is cumbersome and time-consuming, and there is a great need to automate this process. Therefore, a plethora of research is conducted on developing computational tools that aim to fully-automate the NMR process. Although protein NMR is shown to be a promising method for studying structural aspects of a protein (i.e. protein folding), it is limited to small proteins. Several issues emerge when the NMR method is applied to large proteins: (a) numerous overlapping signals make identifying individual signals challenging; and (b) the signals become broader and weaker to the extent of becoming almost undetectable. In this talk, I will describe a novel approach to developing a fully-automated protein NMR method for larger proteins, and present the five modules I have designed and developed for the automation of NMR pipeline.
Views: 184 Microsoft Research
High-resolution NMR protein structure
NMR solution of protein in vitro vs. in vivo. Red: NMR solution of protein in living cell. Blue: NMR solution of protein in vitro
Views: 1886 Olexandr Isayev
Molecular Basis of Genetic Regulation II  + NMR for Protein Structure Determination & Dynamics I
Part (2/2) : Molecular Basis of Genetic Regulation + Part (1/2) : NMR for Structural Determination and Dynamics Presented at the I2CAM/FAPERJ Spring School, 2008 in Rio de Janeiro, Brazil Daniel Schultz (0:00) Ana Paula Valente (15:30) Hits on scivee.tv prior to youtube upload: 706
Views: 24 ICAM - I2CAM
Structure determination of proteins by X ray Crystallography
#BiotechReview #XRay #XRayCrystallography #ProteinStructure
Views: 14931 Biotech Review
Determination of Protein structure
Subject:Biophysics Paper: Techniques Used in Molecular Biophysics II (Based on Spectroscopy)
Views: 48 Vidya-mitra
1-D and 2-D NMR Spectroscopy: Structure Determination of Small Molecule Organic Compounds
Register here: http://proed.acs.org/course-catalog/courses/1d-and-2d-nmr-spectroscopy-structure-determination-of-small-molecule-organic-compounds/
Integrative NMR: Secondary structure analysis
Demonstrating comparison between chemical shift based secondary structure prediction (GetSBY), structure derived determination (STRIDE) and DSSP (from PyMOL).
Views: 664 Woonghee Lee
X ray crystallography basics explained | x ray diffraction
X ray crystallography basics explained - This lecture explains about the X ray crystallography technique to understand the protein structure. X-ray Crystallography is a scientific method used to determine the arrangement of atoms of a crystalline solid in three dimensional space. This technique takes advantage of the interatomic spacing of most crystalline solids by employing them as a diffraction gradient for x-ray light. This video lecture describes the principles of x ray crystallography and the mechanisms of x ray diffraction studies that gives arise to the crystallographic structure of unknown protein samples. For more information, log on to- http://www.shomusbiology.com/ Get Shomu's Biology DVD set here- http://www.shomusbiology.com/dvd-store/ Download the study materials here- http://shomusbiology.com/bio-materials.html Buy Shomu’s Biology lecture DVD set- www.shomusbiology.com/dvd-store Shomu’s Biology assignment services – www.shomusbiology.com/assignment -help Join Online coaching for CSIR NET exam – www.shomusbiology.com/net-coaching Thank you for watching X ray crystallography basics lecture
Views: 174700 Shomu's Biology
Lecture 19. The Nuclear Overhauser Effect in Stereochemistry and Structure Determination
This video is part of a 28-lecture graduate-level course titled "Organic Spectroscopy" taught at UC Irvine by Professor James S. Nowick. The course covers infrared (IR) spectroscopy, mass spectrometry, and nuclear magnetic resonance (NMR) spectroscopy, the latter of which is the main focus. Topics covered in the NMR spectroscopy part of the course include chemical shifts, spin-spin coupling, dynamic effects in NMR spectroscopy, and 2D NMR spectroscopy (COSY, HMQC, HMBC, TOCSY, NOESY, ROESY). Any questions or concerns regarding this class, please e-mail: jsnowick at uci.edu. Copyright © 2011 The Regents of the University of California All Rights Reserved Filmed by the Teaching, Learning, and Technology Center CC-BY-SA
Views: 28288 UCI Media
2D NMR Spectroscopy   Overview | Structure of Organic Molecules | Griti
Griti is a learning community for students by students. We build thousands of video walkthroughs for your college courses taught by student experts who got an A+. SUBSCRIBE to the channel and explore overviews for every concept in your calculus, chemistry and physics courses for FREE! Register at www.GRITI.co REQUEST VIDEOS FOR MORE HELP? + get thousands of study problems for exam prep
Views: 7872 Griti
New Tools for Understanding Allosteric Signaling in G Protein Coupled Receptors
New Tools for Understanding Allosteric Signaling in G Protein Coupled Receptors Presented at Drug Discovery 2018: https://www.labroots.com/virtual-event/drug-discovery-2018 Speaker: Matthew Eddy, PhD- Postdoctoral Research Fellow, The Scripps Research Institute Matthew Eddy received his PhD in physical chemistry from the Massachusetts Institute of Technology in the laboratory of Professor Robert Griffin. During his PhD, Dr. Eddy developed new approaches for using nuclear magnetic resonance (NMR) in the solid state to determine structures of membrane proteins in cellular-like environments. Following his PhD, Dr. Eddy joined the laboratories of Professors Raymond Stevens and Kurt Wüthrich at The Scripps Research Institute as an American Cancer Society Postdoctoral Fellow. As a postdoctoral fellow, Dr. Eddy used an integrative structural biology approach to study the structures, conformational dynamics, and functions of human G protein-coupled receptors (GPCRs), focusing on the application of nuclear magnetic resonance to improve our understanding of GPCR allosteric function. New Tools for Understanding Allosteric Signaling in G Protein Coupled Receptors One-third of FDA-approved drugs target G protein-coupled receptors (GPCRs), transmembrane cell surface proteins that recognize small molecules and polypeptides with diverse chemical scaffolds. When a drug binds to the GPCR extracellular cavity, the information is communicated over 30 Ŭ¬¬ through the plasma membrane to the receptor intracellular surface, inducing changes in the receptor structure that enable complex formation with intracellular partner proteins. Over the past decade, x-ray crystallography has revealed the three-dimensional structures and binding modes of a growing number of unique GPCR-ligand complexes. To better understand mechanisms of GPCR activation, this information must be complemented by knowledge of dynamic signaling pathways connecting drug-binding sites to the intracellular surface. Here we present the development of novel approaches that reveal GPCR signaling pathways with nuclear magnetic resonance (NMR) spectroscopy in solution. Specific applications of this approach are described for the human A2A adenosine receptor (A2AAR), where NMR uncovers the role of a key allosteric center in drug-induced signal transduction. Finally, I will discuss the potential extension of these findings and of the presented methods toward studies of other human GPCRs. Earn PACE/CME Credits: 1. Make sure you’re a registered member of LabRoots: https://www.labroots.com/virtual-event/drug-discovery-2018 2. Watch the webinar on YouTube or on the LabRoots Website: https://www.labroots.com/virtual-event/drug-discovery-2018 3. Click Here to get your PACE expires 5/21/2018: http://www.labroots.com/credit/pace-credits/2744/third-party LabRoots on Social: Facebook: https://www.facebook.com/LabRootsInc Twitter: https://twitter.com/LabRoots LinkedIn: https://www.linkedin.com/company/labroots Instagram: https://www.instagram.com/labrootsinc Pinterest: https://www.pinterest.com/labroots/ SnapChat: labroots_inc
Views: 238 LabRoots
Realistic GB3 protein dynamics obtained from NMR
Realistic dynamics of the third immunoglobulin binding domain of protein G (GB3). We calculated the spatial sampling from exact NOEs as obtained from Nuclear Magnetic Resonance (NMR) spectroscopy. The motions are slowed down a billion times. (Produced by Beat Vögeli, Peter Güntert, Roland Riek)
Views: 2842 perltaucher1
More proteins for your NMR analysis
Poor growth, low levels of expression and insufficient labeled protein are the most frequent challenges faced when using minimal medium to prepare proteins for structural characterization by NMR analysis. EnPresso® B Defined Nitrogen-free is a pre-sterilized, chemically-defined growth system that increases the yield of ¹⁵N-labeled proteins. Scientists are changing from traditional M9 growth media. Visit www.biosilta.com to see their results.
25. C-13 and 2D NMR. Electrophilic Aromatic Substitution
Freshman Organic Chemistry II (CHEM 125B) Proton decoupling simplifies C-13 NMR spectra. Dilute double labeling with C-13 confirmed the complex rearrangement scheme in steroid biosynthesis. Two-dimensional NMR yields correlations between NMR signals that underlie structural determination of proteins and identification of the mechanism of a rapid carbocation rearrangement. Substitution of an electrophile for a proton on an aromatic ring proceeds by a two-step association-dissociation mechanism involving a cyclohexadienyl cation intermediate. The relative rates of forming various products from substituted benzenes correlates with the substituents' influences on the stability of the various cyclohexadienyl cation intermediates. The spectrum of electrophile reactivities is very broad. Important contributions for activating electrophiles were made by Friedel and Crafts working in Paris. 00:00 - Chapter 1. Proton Decoupling 04:39 - Chapter 2. C-13 NMR: Double Labeling and Lanosterol Biosynthesis 19:51 - Chapter 3. 2-D NMR for Protein Structure and Rearrangement Rate 39:07 - Chapter 4. Electrophilic Aromatic Substitution: Substituent Effects 46:25 - Chapter 5. Electrophile Activation: Friedel and Crafts Complete course materials are available at the Open Yale Courses website: http://oyc.yale.edu This course was recorded in Spring 2011.
Views: 4778 YaleCourses
IN THIS VIDEO I HAVE EXPLAINED ABOUT THE ABSORPTION PHENOMENON IN NMR SPECTROSCOPY. ALSO I HAVE EXPLAINED IN SHORT ABOUT THE LIGHT AND ITS POLARIZATION IN HINDI. Want to show your support? Donate and help us to grow more and reach out more students. Click the link below for donation. https://imjo.in/gZPfW9
Views: 1916 Chemistry Untold
Chapt 18 Determination of Protein Structure Pt 1 X-ray
Recorded with http://screencast-o-matic.com
Views: 190 Woon Lim