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Sequencing Amino Acids and Edman Degradation
 
09:26
Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/sequencing-amino-acids-and-edman-degradation Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 56977 AK LECTURES
Determining the N-terminal Residue
 
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Determining the sequence of amino acids in a protein requires a sequence of chemical reactions that selectively cleave one peptide from the chain at a time. This webcast covers how to use chemical reactions to determine the N-terminal residue of a peptide.
Views: 15050 Michael Evans
PROTEIN SEQUENCING & ASSAYS | C-TERMINAL ANALYSIS | PART-3
 
12:30
 Once we determine the amino acid composition of protein, our next step is to find the order of amino acids in that protein. In C-terminal amino acid analysis we basically determine, which amino acid forms the C-terminal of the peptide. Less methods are available for C terminus amino acid analysis as compared to N terminus analysis processes. This method is very helpful in determining the sequence of peptides whose N terminus is blocked. Protein sequencing is a process employed to determine the amino acid sequence of a protein. It is important for understanding cellular functions. In Finding the evolutionary history of protein, helps in prediction of the function related to protein. Important in targeting drug for specific metabolic pathways. There are several methods by which we can determine sequence of a protein. For More Information, & Queries Do Like My Facebook Page https://www.facebook.com/tanejanehaofficial
PROTEIN SEQUENCING & ASSAYS | N & C TERMINAL AMINO ACID ANALYSIS | PART-1
 
29:37
Protein sequencing is a process employed to determine the amino acid sequence of a protein. It is important for understanding cellular functions. In Finding the evolutionary history of protein, helps in prediction of the function related to protein. Important in targeting drug for specific metabolic pathways. There are several methods by which we can determine sequence of a protein. For More Information, & Queries Do Like My Facebook Page https://www.facebook.com/tanejanehaofficial
Identifying the N Terminus
 
03:45
To prepare for a discussion of how peptide sequencing works, an understanding of the reactivity of the amino terminus of polypeptides is essential. This webcast describes two methods for identifying the N terminus of polypeptides. Both involve the use of an electrophilic, fluorescent "tag" molecule that reacts selectively with the N termini of polypeptides.
Views: 11866 Michael Evans
Peptide sequencing problem | CSIR NET analytical problems for Part C
 
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Peptide sequencing problems | CSIR NET analytical problems for Part C - This lecture explains about the peptide sequencing problems for CSIR NET life sciences exam. Watch this video lecture to know more about how to answer csir net analytical problems for part C. Here we discussed about protein cleavage by enzymes like pepsin, trypsin, chymotrypsin, protease v8 and cyanogen bromide. 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 Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching the CSIR NET analytical problems video on polypeptide sequencing involving the cut site of different protease enzymes.
Views: 15664 Shomu's Biology
Sequencing Amino Acids in Proteins
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/determining-protein-structure-part-iv Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 13863 AK LECTURES
Edman Degradation
 
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Views: 46280 AK LECTURES
Sanger Degradation
 
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Donate here: http://www.aklectures.com/donate.php Website video link: http://www.aklectures.com/lecture/determining-protein-structure-part-ii Facebook link: https://www.facebook.com/aklectures Website link: http://www.aklectures.com
Views: 15406 AK LECTURES
Protein Sequencing - Edman Degradation Part 1
 
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In this video we study a method for analysing the sequence of amino acids of the primary polypeptide structure
Views: 49680 Ben1994
Protein Fragmentation Analysis
 
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http://teachingcenter.ufl.edu/vsi
Views: 2364 UF Teaching Center
LC-MS/MS for Bioanalytical Peptide and Protein Quantification: Chromatographic Considerations
 
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Bioanalytical scientists are faced with developing robust, reliable, and sensitive methods. This is especially challenging when we deal with peptides and proteins. Mary Lame, Waters Principal Applications Chemist, walks you through a basic LC screening method designed specifically with peptides in mind. http://www.waters.com/dmpk
Views: 412 Waters Corporation
PROTEIN SEQUENCING & ASSAYS | PROTEOLYTIC CLEAVAGE OF PEPTIDE | PART-4
 
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 Proteolytic enzymes or proteases are the enzymes that breakdown the proteins into smaller fragments. These enzymes are present in bacteria, archaea, certain types of algae, some plants & animals. Once we determine the amino acid composition of protein, our next step is to find the order of amino acids in that protein. In C-terminal amino acid analysis we basically determine, which amino acid forms the C-terminal of the peptide. Less methods are available for C terminus amino acid analysis as compared to N terminus analysis processes. This method is very helpful in determining the sequence of peptides whose N terminus is blocked. Protein sequencing is a process employed to determine the amino acid sequence of a protein. It is important for understanding cellular functions. In Finding the evolutionary history of protein, helps in prediction of the function related to protein. Important in targeting drug for specific metabolic pathways. There are several methods by which we can determine sequence of a protein. The solution shown for 1 question in the video, is shown by taking last amino acid residur as 'R' by mistake, but according to that answer is correct. But according to actual question in which last amino acid is "F" correct answer would be 0 or option 4. For More Information, & Queries Do Like My Facebook Page https://www.facebook.com/tanejanehaofficial
protein sequence analysis
 
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protein sequence analysis - lecture explains about the primary sequence analysis of a protein. http://shomusbiology.com/ 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 Facebook page- https://www.facebook.com/ShomusBiology/ Twitter - https://twitter.com/shomusbiology SlideShare- www.slideshare.net/shomusbiology Google plus- https://plus.google.com/113648584982732129198 LinkedIn - https://www.linkedin.com/in/suman-bhattacharjee-2a051661 Youtube- https://www.youtube.com/user/TheFunsuman Thank you for watching In this video, the process of primary sequence analysis of protein is described. Source of the article published in description is Wikipedia. I am sharing their material. © by original content developers of Wikipedia. Link- http://en.wikipedia.org/wiki/Main_Page
Views: 21417 Shomu's Biology
PROTEIN SEQUENCING & ASSAYS | EDMAN DEGRADATION METHOD | PART-2
 
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 In N-terminal amino acid we basically determine, which amino acid forms the N-terminal of the peptide. A technique developed by Pehr Edman called EDMAN DEGRADATION is used to determine what the first amino acid is. Protein sequencing is a process employed to determine the amino acid sequence of a protein. It is important for understanding cellular functions. In Finding the evolutionary history of protein, helps in prediction of the function related to protein. Important in targeting drug for specific metabolic pathways. There are several methods by which we can determine sequence of a protein. For More Information, & Queries Do Like My Facebook Page https://www.facebook.com/tanejanehaofficial
Edman degradation
 
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The sequence of amino acids in a protein or peptide can be identified by Edman degradation, which was developed by Pehr Edman. This method can label and cleave the peptide from N-terminal without disrupting the peptide bonds between other amino acid residues.
Views: 7194 Creative Proteomics
C-Terminal Modified Peptide Synthesis Research
 
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Hasina Saraha and Christine Arbour of the Stockdill Lab at Wayne State University discuss their latest research on c-terminal modified peptide synthesis.
PROTEIN SEQUENCING & ASSAYS | QUESTIONS ON PROTEOLYTIC CLEAVAGE OF PEPTIDE | PART-5
 
14:45
 Proteolytic enzymes or proteases are the enzymes that breakdown the proteins into smaller fragments. These enzymes are present in bacteria, archaea, certain types of algae, some plants & animals. Once we determine the amino acid composition of protein, our next step is to find the order of amino acids in that protein. In C-terminal amino acid analysis we basically determine, which amino acid forms the C-terminal of the peptide. Less methods are available for C terminus amino acid analysis as compared to N terminus analysis processes. This method is very helpful in determining the sequence of peptides whose N terminus is blocked. Protein sequencing is a process employed to determine the amino acid sequence of a protein. It is important for understanding cellular functions. In Finding the evolutionary history of protein, helps in prediction of the function related to protein. Important in targeting drug for specific metabolic pathways. There are several methods by which we can determine sequence of a protein. For More Information, & Queries Do Like My Facebook Page https://www.facebook.com/tanejanehaofficial
Protein sequence analysis
 
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Protein sequencing is a technique to determine the amino acid sequence of a protein, as well as which conformation the protein adopts and the extent to which it is complexed with any non-peptide molecules. Discovering the structures and functions of proteins in living organisms is an important tool for understanding cellular processes, and allows drugs that target specific metabolic pathways to be invented more easily. The two major direct methods of protein sequencing are mass spectrometry and the Edman degradation reaction. It is also possible to generate an amino acid sequence from the DNA or mRNA sequence encoding the protein, if this is known. However, there are many other reactions that can be used to gain more limited information about protein sequences and can be used as preliminaries to the aforementioned methods of sequencing or to overcome specific inadequacies within them. Bioinformatics tools exist that translate nucleic acid sequences into their corresponding polypeptide chain. Such tool takes an input of a nucleic acid sequence and will produce the corresponding amino acid sequence based on the selected settings. Another option is to use a bioinformatics tool that takes an amino acid sequence and back-translates it into the most likely nucleic acid sequence.
Trypsin digestion
 
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For more information, log on to- http://shomusbiology.weebly.com/ Download the study materials here- http://shomusbiology.weebly.com/bio-materials.html Trypsin digestion or in-gel digestion is part of the sample preparation for the mass spectrometric identification of proteins in course of proteomic analysis. The method was introduced 1992 by Rosenfeld.[1] Despite innumerable modifications and improvements the basic elements of the procedure remain largely unchanged. The in-gel digestion primarily comprises the four steps destaining, reduction and alkylation (R&A) of the cysteines in the protein, proteolytic cleavage of the protein and extraction of the generated peptides. Afterwards the eponymous step of the method is performed, the in-gel digestion of the proteins. By this procedure, the protein is cut enzymatically into a limited number of shorter fragments. These fragments are called peptides and allow for the identification of the protein with their characteristic mass and pattern. The serine protease trypsin is the most common enzyme used in protein analytics. Trypsin cuts the peptide bond specifically at the carboxyl end of the basic aminoacids arginine and lysine. If there is an acidic amino acid like aspartic acid or glutamic acid in direct neighborhood to the cutting site, the rate of hydrolysis is diminished, a proline C-terminal to the cutting site inhibits the hydrolysis completely.[21] An undesirable side effect of the use of proteolytic enzymes is the self digestion of the protease. To avoid this, in the past Ca2+-ions were added to the digestion buffer.[22][23] Nowadays most suppliers offer modified trypsin where selective methylation of the lysines limits the autolytic activity to the arginine cutting sites.[24] Unmodified trypsin has its highest activity between 35°C and 45°C. After the modification, the optimal temperature is changed to the range of 50°C to 55°C.[15][25] Other enzymes used for in-gel digestion are the endoproteases Lys-C,[26][27][28] Glu-C,[29][30][31] Asp-N [32] and Lys-N.[33][34] These proteases cut specifically at only one amino acid e.g. Asp-N cuts n-terminal of aspartic acid.[26] Therefore a lower number of longer peptides is obtained. The analysis of the complete primary sequence of a protein using only one protease is usually not possible. In those cases the digestion of the target protein in several approaches with different enzymes is recommended. The resulting overlapping peptides permit the assembly of the complete sequence of the protein.[29][35][36] For the digestion the proteins fixed in the matrix of the gel have to be made accessible for the protease. The permeation of the enzyme to the gel is believed to be facilitated by the dehydration of the gel pieces by treatment with acetonitrile and subsequent swelling in the digestion buffer containing the protease. This procedure relies on the presumption that the protease permeates to the gel by the process of swelling.[37] Different studies about the penetration of the enzymes to the gel showed the process to be almost completely driven by diffusion. The drying of the gel does not seem to support the process.[6][15] Therefore, the improvement of the in-gel digestion has to be achieved by the reduction of the way of the enzyme to its substrate e.g. by cutting the gel to pieces as small as possible. Usually, the in-gel digestion is run as an overnight process. For the use of trypsin as protease and a temperature of 37°C the time of incubation found in most protocols is 12-15 h. However, experiments about the duration of the digestion process showed that after 3 h there is enough material for successful mass spectrometric analysis.[38] Furthermore, the optimisation of the conditions for the protease in temperature and pH allows for the completion of the digestion of a sample in 30 min.[15] Surfactant (detergents) can aid in the solubilization and denaturing of proteins in the gel and thereby shorten digestion times and increase protein cleavage and the number and amount of extracted peptides, especially for lipophilic proteins such as membrane proteins. Cleavable detergents are detergents that are cleaved after digestion, often under acidic conditions. This makes the addition of detergents compatible with mass spectrometry.
Views: 28663 Shomu's Biology
Peptide Synthesis in the Laboratory
 
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Synthesis of a polypeptide with defined sequence from the monomeric amino acids is a difficult problem. This webcast introduces the fundamental problems and solutions in the field of peptide synthesis.
Views: 37713 Michael Evans
Biochemistry: Protein sequencing problems (1)
 
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Biochemistry: Protein sequencing problems, i.e., the determination of the primary structure of a peptide. Hydrolysis. Dansyl chloride. Proteolytic enzymes. Trypsin. Chymotrypsin. Circular peptides. Thermolysin. Disulfide bonds. Carboxypeptidase. Cyanogen bromide This is a recording of a tutoring session, posted with the student's permission. These videos are offered on a "pay-what-you-like" basis. You can pay for the use of the videos by making a monthly pledge at my Patreon page: http://www.patreon.com/freelanceteacher Or, if you prefer to make a one-time payment, you can do so by using the PalPal "Donate" button on my website: http://www.freelance-teacher.com/videos.htm For a list of all the available video series, arranged in suggested viewing order, go to my website. For a document containing the video (1) homework problems, click here: http://www.freelance-teacher.com/protein_sequencing_homework1.pdf TABLE OF CONTENTS VIDEO (1) 0:00 The amino acid sequence. Amino acid composition 8:10 Hydrolysis 19:10 Dansyl chloride 39:50 Trypsin VIDEO (2) Homework Homework continued. Chymotrypsin Another problem Circular peptides Thermolysin. Disulfide bonds VIDEO (3) Homework Carboxypeptidase Cyanogen bromide tags: education college student students university exam test educational study campus school class
Views: 10389 freelanceteach
Organic Chemistry 51C. Lecture 18. Amino Acids, Peptides, and Proteins.
 
01:04:57
UCI Chem 51C Organic Chemistry (Spring 2012) Lec 18. Organic Chemistry -- Amino Acids, Peptides, and Proteins -- View the complete course: http://ocw.uci.edu/courses/chem_51c_organic_chemistry.html Instructor: James S. Nowick, Ph.D. License: Creative Commons BY-NC-SA Terms of Use: http://ocw.uci.edu/info. More courses at http://ocw.uci.edu Description: This is the third quarter course in the organic chemistry series. Topics covered include: Fundamental concepts relating to carbon compounds with emphasis on structural theory and the nature of chemical bonding, stereochemistry, reaction mechanisms, and spectroscopic, physical, and chemical properties of the principal classes of carbon compounds. Organic Chemistry 51C is part of OpenChem. http://ocw.uci.edu/collections/open_chemistry.html Recorded on June 6, 2012 Index of Topics: 2:49-Amino Acid Structure 5:55-Examples of Polypeptides 12:18-20 Common Amino Acids 17:03-Polar & Charged Amino Acids 22:35-Chemical Synthesis of Peptides and Proteins 27:49-Protecting Groups 31:54-DCC 40:07-Boch Deprotection Mechanism 42:44-Special Amino Acids 43:33-Additional Protecting Groups 46:42-Modern Solid-Phase Peptide Synthesis 54:20-Boch Opolystyrene Example 59:54-Fmoc Group Required attribution: Nowick, James S. Organic Chemistry 51C (UCI OpenCourseWare: University of California, Irvine), http://ocw.uci.edu/courses/chem_51c_organic_chemistry.html [Access date]. License: Creative Commons Attribution-ShareAlike 3.0 United States License (http://creativecommons.org/licenses/by-sa/3.0/us/deed.en_US).
Views: 26099 UCI Open
end group analysis || अन्त्य समूह विश्लेषण || bsc topic || d's classes || amit dwivedi
 
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https://www.facebook.com/Ds-classes-1391615131088506/ https://www.facebook.com/amit.dw.1 https://www.facebook.com/mahadevsss2016/ यह चैनल मुख्य रूप से उन लोगों के लिए बनाया गया है जो प्रतियोगी परीक्षा की तैयारी कर रहे हैं और इसके आलावा वह विद्यार्थी जो ग्रेजुएशन कर रहे हैं उनके केमिस्ट्री ( रसायन विज्ञान ) विषय से सम्बंधित भी सारे लेक्चर लाइव मिलेंगे , इस कक्षा का मुख्य उद्देश्य उन सभी को पढ़ाना है जो कहीं न कहीं से आर्थिक रूप से कमजोर हैं। Amit Dwivedi D's Classes 9993265131 , 8962564211
Introduction to Peptides and Proteins for Bioanalysis Using LC-MS
 
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Khalid Khan, Senior Manager Business Development, discusses the basic structure of amino acids, peptides, and proteins, including specific examples like monoclonal antibodies. http://www.waters.com/dmpk
Views: 2368 Waters Corporation
Sequence Determination One Terminal Unit at a Time
 
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The Edman Degradation sequentially cleaves one amino acid at a time, facilitating the sequencing of a protein from N- to C-terminus.
Views: 41650 Michael Evans
Determining the Amino Acid Composition of a Protein
 
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How do scientists determine the relative amounts of amino acids present in a protein? It's all organic chemistry! Learn more in this webcast.
Views: 22466 Michael Evans
Protein Structure (Part 2 of 4) - Secondary Structure - Alpha Helix
 
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Moof's Medical Biochemistry Video Course: http://moof-university.thinkific.com/courses/medical-biochemistry-for-usmle-step-1-exam For Related Practice Problems with Worked Video Solutions on Protein Structure and Function, visit courses.moofuniversity.com. In this video, I explain the details of the alpha helix (alpha helices). The alpha helix is an important type of secondary protein structure. The alpha helix is, specifically, a right handed helix held together by hydrogen bonds (H-bonds) between the carbonyl oxygen and amide hydrogen of the polypeptide backbone. These hydrogen bonds are parallel to the axis of the helix, and they exist between every 4th amino acid of the backbone. The side chains of the amino acids (R-groups) extend out of the helix, running perpendicular to the axis of the helix. The alpha helix is often thought of as having polarity, with the N-terminus (amino terminus) having a partial positive charge, while the C-terminus (carboxy terminus) carries a partial negative charge. There are a few things that can disrupt or damage and alpha helix: 1. Proline – Proline’s side chain is wrapped around and connected to its alpha amino group. This restricts rotation that is necessary to form the particular structure of the alpha helix. Also, when proline’s amino group is part of a peptide bond, it has no hydrogen on it that can hydrogen bond. In short, substituting a proline in for an amino acid that is part of an alpha helix will ruin the alpha helix’s structure. 2. Electrostatic Repulsions between Side Chains with Like Charges – If the R groups of the amino acids that extend outward from the alpha helix happen to be next to each other with like charges, they can repel each other and bend the helix in a way that compromises its structure. For instance, if two negatively charged aspartate side chains are next to each other, they will repel. Likewise, this could occur with two positively charged arginine side chains. 3. Steric Hindrance – The alpha helix is a fairly tightly packed helix, and amino acids with bulky side chains can disrupt its structure by taking up too much space being next to each in the peptide chain that makes up the helix. For example, two phenylalanine side chains next to each other means two aromatic rings (bulky) next to each other. This could disrupt the alpha helix. For a suggested viewing order of the videos, information on tutoring, personalized video solutions, and an opportunity to support Moof University financially, visit MoofUniversity.com, and follow Moof University on the different social media platforms. Don't forget to LIKE, COMMENT, and SUBSCRIBE: http://www.youtube.com/subscription_center?add_user=MoofUniversity SUPPORT MOOF UNIVERSITY: http://www.moofuniversity.com/support-moof/ BUY A T-SHIRT https://shop.spreadshirt.com/moofuniversity/ INFORMATION ABOUT TUTORING AND PERSONALIZED VIDEO SOLUTIONS: http://www.moofuniversity.com/tutoring/ INSTAGRAM: https://instagram.com/moofuniversity/ FACEBOOK: https://www.facebook.com/pages/Moof-University/1554858934727545 TWITTER: https://twitter.com/moofuniversity
Views: 79549 Moof University
Edman Degradation Detailed Overview
 
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How do scientists determine the amino acid sequence of unknown proteins and peptides? Tune in to find out!
Views: 1639 Vincent Stevenson
Analysis of Amino Acids
 
01:00:01
This Lecture talks about Analysis of Amino Acids
Views: 952 Cec Ugc
The Problem of Protein Sequencing
 
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Proteins are composed of linear sequences of amino acids. How do protein chemists determine the sequence of a given protein? This webcast explores some of the problems associated with peptide sequencing.
Views: 15221 Michael Evans
N terminal sequencing service
 
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Although database search identification of proteins by mass spectrometry is well established, the method does not apply if the protein sequence does not exist in the current database. Therefore, de novo sequencing is the only method for identifying novel peptides, unsequenced organisms, and antibodies drugs, which database search methods were not able to detect. However, de novo sequencing poses more challenging than the traditional database search approach, such as, ambiguous assignments of fragment ions, insufficient product ions generated in incomplete fragmentation leading to low sequence coverage and difficulty in distinguishing ion series, notably N-terminal from C-terminal MS/MS product ions (b ions from y ions). source: http://www.creative-proteomics.com/services/de-novo-peptides-proteins-sequencing-service.htm
Views: 254 Bennie George
Protein Sequencing - Edman Degradation Part 3
 
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In this video we study a method for analysing the sequence of amino acids of the primary polypeptide structure
Views: 10672 Ben1994
Solution of Question based on Primary amino acid sequence and Growth rate-CSIR NET JRF
 
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In this video two questions were discussed. Both of these questions are from CSIR JRF NET. First question is all about finding primary sequence of amino acid in the peptide. The primary sequence of amino acid is find out with the help of treatment of various enzymes, like trypsin, chymotrypsin, acid hydrolysis etc. Second question is based on growth rate. In the second question we have to find out death rate from the initial population, final population and growth rate.
Protein Sequencing Part 1
 
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This video screencast was created with Doceri on an iPad. Doceri is free in the iTunes app store. Learn more at http://www.doceri.com
Views: 10086 Dr. K's Chemistry
"Amino Acid Sequencing of a Peptide Chain" | Biochemistry with Educator.com
 
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"Amino Acid Sequencing of a Peptide Chain" | Biochemistry with Educator.com ►Watch more at http://educator.com/chemistry/biochemistry/hovasapian/ Understand your Biochemistry homework and ace the test with Educator.com's awesome hand-picked instructors. More features you'll see on Educator.com: -Full lessons complete with extra examples, downloads, and quizzes -Searchable and jumpable topics to save you time -Ability to ask questions to instructor and other students --- More subjects including: Multivariable ► http://educator.com/mathematics/multivariable-calculus/hovasapian/ Organic Chemistry ► http://educator.com/chemistry/organic-chemistry/starkey/ Linear Algebra ► http://educator.com/mathematics/linear-algebra/hovasapian/ Our Biochemistry Playlist ► http://www.youtube.com/playlist?list=PLDOH1OG4-NqMWRheBEALMe1Hy9Gm83jQE --- http://Educator.com --- http://facebook.com/EducatorInc http://twitter.com/Educator http://youtube.com/EducatorVids
Views: 672 Educator.com
Determination of Primary Structure & Synthesis of Peptides
 
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Subject :Bio-medical Science Course :1st year/paper 7 Keyword : SWAYAMPRABHA
Sequence Determination One Terminal Residue at a Time
 
03:21
We're now ready to illustrate how the Edman degradation process facilitates the sequencing of polypeptides one N-terminal residue at a time. Learn the concepts and chemistry behind this extremely useful process in this webcast.
Views: 14147 Michael Evans
Giulio Gabbiani MD PhD, "The N-terminal peptide of a-smooth..." 2010 Miami Dupuytren Symposium.
 
17:58
Giulio Gabbiani MD PhD, Professor, University of Geneva, Geneva, Switzerland presents "The N-terminal peptide of a-smooth muscle actin Ac-EEED inhibits myofibroblast contraction: therapeutic implications."at the 2010 Miami Dupuytren Symposium.
AP1: BIOCHEMISTRY: AMINO ACID SEQUENCE
 
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AMINO ACID SEQUENCE
Views: 1101 Walter Jahn
Biochemistry: Protein sequencing problems (2)
 
01:25:53
Biochemistry: Protein sequencing problems, i.e., the determination of primary structure. Hydrolysis. Dansyl chloride. Proteolytic enzymes. Trypsin. Chymotrypsin. Circular peptides. Thermolysin. Disulfide bonds. Carboxypeptidase. Cyanogen bromide This is a recording of a tutoring session, posted with the student's permission. These videos are offered on a "pay-what-you-like" basis. You can pay for the use of the videos by making a monthly pledge at my Patreon page: http://www.patreon.com/freelanceteacher Or, if you prefer to make a one-time payment, you can do so by using the PalPal "Donate" button on my website: http://www.freelance-teacher.com/videos.htm For a list of all the available video series, arranged in suggested viewing order, go to my website. For a document containing the video (1) homework problems, click here: http://www.freelance-teacher.com/protein_sequencing_homework1.pdf For a document containing the video (2) homework problems, click here: http://www.freelance-teacher.com/protein_sequencing_homework2.pdf TABLE OF CONTENTS VIDEO (1) Amino acid sequence. Amino acid composition Hydrolysis Dansyl chloride Trypsin VIDEO (2) 0:00 Homework 24:00 Homework continued. Chymotrypsin 35:40 Another problem 45:00 Circular peptides 1:20:20 Thermolysin. Disulfide bonds VIDEO (3) Homework Carboxypeptidase Cyanogen bromide tags: education college student students university exam test educational study campus school class
Views: 3240 freelanceteach
Using a Knowledgebase to Improve Peptide Sequence Assignments
 
07:09
This video is a short presentation of how X! Tandem uses knowledgebases to determine which post-translational modifications should be tested for specific proteins.
Views: 371 gpmdb01

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