BIF401 Today Current Final Term Paper Fall 2020 28-02-2021 Bif401....(9:30 Am) 1) spectrometer (2) 2) salient features of ORF 3) is protein sequence determine difficult? 4) how we have the algorithm of best protein sequence 5) how we can determine the sequence of protein 6) factors affecting the protein folding 7) what happen when protein infolding 8) how can find out the loops when computing the a-helix and b-sheets Or mcqs ak, 2 chor K sab midterm K syllabus sy thy 9) goal of protein folding 10) Why Chou fasman algorithm is used. BIF401 Current Finalterm Papers Fall 2020 | 01-03-2021 Questions 1: shotgun proteomics and fingerprinting? 2: How protein sequence are identified? 3: what is ab - initio modeling and it's limitations? 4: role of Amino acids and goal of Amino acids ? 5: Chau fasman for alpha helixes?. 6: Define : title, source , compnd ,revdt BIF401 Current Finalterm Papers Fall 2020 | 28-02-2021 Bif401. Why shotgun method is different from peptide mass spectroscopy.3 Title,CMPND, Source,REVDT .3 Energy function in proteins structure prediction .5 How we can identify proteins sequence .5 Advantage of denatured proteins over folded,role of amino acid,how proteins fold. What is the goal of folding .5 Difference between DNA and RNA.2 role of amino acid Fragmentation of protein how Homology modeling determine unknown sequence of protein Briefly describe the secondary structure How chou fasman algorithm help in alpha helix Advantage or dis advantage of Ab intio algorithm Or discribe the given below Role of amino acid Why folding protein is better than denatured Fector of protein folding Gold of protein folding My today's bif401 ppr Time# 8:00 12 mcqs from past 1=what is tendem mass spectrometry? 2=what ab initio modeling? Describe its limitations as well? 3=describe following elements *Title* *Source* *REVDAT* *COMPND* 4=What is hydrophobicity of amino acid? 5=how propensity table can helps us? 6=describe secondary structure of protein? 7=chou fasman algorithm 8=silico fragment comparison? 9=seven steps of homology modeling? 10=describe *advantage of folded protein over denatured protein* *factor that participate in folding protein* *role of amino acid* *goal of folding protein* Q#1Describe the following 1Advantage of Folded Protein over Denatured Protein? Factors That Participate In Folding Protein? Role of Amino Acid? Folding protein function? Q#2.Need For Chou Fasman Algorithms? Q#3Advantages and Disadvantages Of Ab Initio Modeling? Q#4Optimal Energy Function In Protein? Q#5Silico Fragments Comparison? Q#6How Propensity Table Help Us? Q#7Function of Tandem MS? Q#8Explain the chou fasman method Q#9 Tendom Mass spectrometry Q#10 function of tendom MS MY BIF401 paper at 2:30 Today bif 401 paper ... 8:00.. Mcqs mostly mid/past papers... 1...differnce b/w similarty and identity?with formula? 2..Role of amino acid? 3...Charctersitc of amino acids? 4...Ab initio limitations? 5...how protein sequnce identified? 6...Summary of Alpha helix by chou's algorithum? 7...Example about the the chous fasman secondary structre of protein? 8...define top down pretomics? 9...difffernce b/w spectrometry or raw data? Yeh question yd thy baqi yd nh aa rhy Top down proteomics Shotgun proteomic and fingerprinting How buldges are formed ? How protein structures are identified ? Define title ,source, cmpnd , revdat. How protein sequence are udentified ? What is ab initio modelling and its limitations ? Home message of this course ? Advantages of folding of proteins over denature proteins? Role of amino acids, Goal of amino acids Characteristics of amino acids,? Chaou fasmsn for alpha helecies? Chaou fasman for secondary structures? Name 3 hydrophobic amino acids? Prediction of protein structures ? Forces involved in protein folding Techniques for protein structure Protein ionization Orf and fasta stands for Use of sequence data Importance of phylogemetics Choufasaman algorithm for beta turns And for alpha helix Ab initio and limitation Protein folding goal ,importance of protein folding and disruptive protein structure,importance of amino acids. Compnd,title ,source, revdat Bif401 13/9/2020 Sunday 2:30pm • What are psudoknots? (2 marks) • What is hydrophobicity of amino acids? (2 marks) • Ab initio modeling and limitaions? (3 marks) • Chou fasman algorithm for alpha helix (5 marks) • Chou fasman algorithm for beta sheets (3 marks) • what are the following PDB formats TITLE, SOURCE, COMPND, REVDAT (5 marks) • Advantage of folding protein over denatured Role of amino acids Goals of folding protein (5 marks) • Difference b/w fasta35 and fastx35 (3 marks) • Difference between shotgun proteomics and protein mass fingerprinting (3 or may be 5 marks) • PAM matrix (5 marks) MCQs from ppts (zyada asan nahi thay lekin mushkil bhi nahi thay as such) Today bif401 paper 2:30 Top down proteomics Shotgun proteomic and fingerprinting How buldges are formed ? How protein structures are identified Define title ,source, cmpnd , revdat How protein sequence are udentified What is ab initio modelling and its limitations ? Home message of this course ? Advantages of folding of proteins over denature proteins? Role of amino acids Goal of amino acids Characteristics of amino acids,? Chaou fasmsn for alpha helecies? Chaou fasman for secondary structures? Name 3 hydrophobic amino acids? Prediction of protein structures ?
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