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Protein Structure Prediction
Submitted By :-
Name : Md.Selim Reza
Id : 183-15-12020
W E L - C O M E T o M y P r e s e n t a t i o n
On
Submitted To :
Mohd. Saifuzzaman
Lecturer, Daffodil International University
What is Protein structure prediction ?
Protein structure prediction is the inference of the three-
dimensional structure of a protein from its amino
acid sequence—that is, the prediction of
its secondary and tertiary structure from primary structure.
Different Levels of Protein Structure
METHODS FOR PROTEIN STRUCTURE PREDICTION
1.EXPERIMANTAL METHODS
2.COMPUTIONAL METHODS
Experimental Protein Structure Determination
•
•
•
X.ray crystallography
– most accurate
– in vitro
– needs crystals
– ~$100-200K per structure
–time consuming and expansive.
NMR
– fairly accurate
– in vivo
– no need for crystals
– limited to very small proteins
–time consuming and hardly .
Electron-microscopy
– imaging technology
– low resolution
– not more observable.
Computational method
• Major Techniques
– Template Modeling
• Homology Modeling
• Threading
• Both are use known protein structure
– Template-Free Modeling
• ab initio Methods
– Physics-Based
– Knowledge-Based
– without use of known protein structure
Homology Modelling
• also called comparitive modeling.
• predict protein structures based on sequence
homology with known structure.
• Principle:-
• if two proteins share a high enough sequence
similarity,they are likely to have very similar
three dimensional structure.
• modeling server:-modbase,swiss-model etc.
• Fail in absence of homology
Homology Modelling
6 steps:-
1.template selection (BLAST and FASTA)
2.sequence alignment (T-coffee and PRALINE)
3.model building (CODA)
(a)backbone model building
(b)loop modeling
4.side chain refinement (SCWRL)
5.model refinement using energy function (GROMOS)
6.model evalution (PROCHECK & WHAT IF)
• Has been observed that even proteins with 30% sequence identity
fold into similar structures
• Does not work for remote homologs (< 30% pairwise identity)
Threading
• Given:
– sequence of protein 'P 'with unknown structure
– Database of known folds
• Find:
– Most plausible fold for 'P'
– Evaluate quality of such arrangement
• Places the residues of unknown 'P' along the
backbone of a known structure and determines
stability of side chains in that arrangement
Threading and fold recognition
• predicts the structural fold of unknown protein
sequences by fitting the sequence into a
structural database and selecting the best
fitting fold.
• we can identify structurally similar proteins
even without detectablesequence similarity.
• two algorithms:-
1.pairwise energy based method
2.profile based method
Protein Sequence
Database Searching
Multiple Sequence
Alignment
Homologue
in PDB
Homology
Modelling
Secondary
Structure
Prediction
No
Yes
3-D Protein Model
Fold
Recognition
Predicted
Fold
Sequence-Structure
Alignment
Ab-initio
Structure
Prediction
No
Yes
Overall Approach
Protien Structure Prediction

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Protien Structure Prediction

  • 1. Protein Structure Prediction Submitted By :- Name : Md.Selim Reza Id : 183-15-12020 W E L - C O M E T o M y P r e s e n t a t i o n On Submitted To : Mohd. Saifuzzaman Lecturer, Daffodil International University
  • 2. What is Protein structure prediction ? Protein structure prediction is the inference of the three- dimensional structure of a protein from its amino acid sequence—that is, the prediction of its secondary and tertiary structure from primary structure.
  • 3. Different Levels of Protein Structure
  • 4. METHODS FOR PROTEIN STRUCTURE PREDICTION 1.EXPERIMANTAL METHODS 2.COMPUTIONAL METHODS
  • 5. Experimental Protein Structure Determination • • • X.ray crystallography – most accurate – in vitro – needs crystals – ~$100-200K per structure –time consuming and expansive. NMR – fairly accurate – in vivo – no need for crystals – limited to very small proteins –time consuming and hardly . Electron-microscopy – imaging technology – low resolution – not more observable.
  • 6. Computational method • Major Techniques – Template Modeling • Homology Modeling • Threading • Both are use known protein structure – Template-Free Modeling • ab initio Methods – Physics-Based – Knowledge-Based – without use of known protein structure
  • 7. Homology Modelling • also called comparitive modeling. • predict protein structures based on sequence homology with known structure. • Principle:- • if two proteins share a high enough sequence similarity,they are likely to have very similar three dimensional structure. • modeling server:-modbase,swiss-model etc. • Fail in absence of homology
  • 8. Homology Modelling 6 steps:- 1.template selection (BLAST and FASTA) 2.sequence alignment (T-coffee and PRALINE) 3.model building (CODA) (a)backbone model building (b)loop modeling 4.side chain refinement (SCWRL) 5.model refinement using energy function (GROMOS) 6.model evalution (PROCHECK & WHAT IF) • Has been observed that even proteins with 30% sequence identity fold into similar structures • Does not work for remote homologs (< 30% pairwise identity)
  • 9. Threading • Given: – sequence of protein 'P 'with unknown structure – Database of known folds • Find: – Most plausible fold for 'P' – Evaluate quality of such arrangement • Places the residues of unknown 'P' along the backbone of a known structure and determines stability of side chains in that arrangement
  • 10. Threading and fold recognition • predicts the structural fold of unknown protein sequences by fitting the sequence into a structural database and selecting the best fitting fold. • we can identify structurally similar proteins even without detectablesequence similarity. • two algorithms:- 1.pairwise energy based method 2.profile based method
  • 11. Protein Sequence Database Searching Multiple Sequence Alignment Homologue in PDB Homology Modelling Secondary Structure Prediction No Yes 3-D Protein Model Fold Recognition Predicted Fold Sequence-Structure Alignment Ab-initio Structure Prediction No Yes Overall Approach