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Made for 3rd year Protein Engineering class
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This presentation covers the basics and introduction to Ramachandran plot. It also enlights limitations for secondary structure forming in protein.
Ramachandran plot
Ramachandran plot
Sushant Balasaheb Jadhav
protein engineering
Alpha/beta domains
Alpha/beta domains
Mirra09
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein Folding-biophysical and cellular aspects, protein denaturation
AnishaMukherjee5
Describes various aspects of Ramachandran plot. Different torsion angles are described with clear figures. How protein folding is affected by torsion angles is also explained.
Ramachandran plot
Ramachandran plot
Radhakrishna Gopala Pillai
Includes basic and the main topic....wholly covered
The Ramachandran plot
The Ramachandran plot
K Tanay
BIOCHEMISTRY
Secondary Structure Of Protein (Repeating structure of protein)
Secondary Structure Of Protein (Repeating structure of protein)
Amrutha Hari
covalent and non-covalent bonds
Forces stabilising structure of proteins
Forces stabilising structure of proteins
Raviz Prathyusha
Describes Ramachandran plot at Graduate level with figures and explanations in simple language
Ramachandran plot
Ramachandran plot
Radhakrishna Gopala Pillai
Empfohlen
This presentation covers the basics and introduction to Ramachandran plot. It also enlights limitations for secondary structure forming in protein.
Ramachandran plot
Ramachandran plot
Sushant Balasaheb Jadhav
protein engineering
Alpha/beta domains
Alpha/beta domains
Mirra09
Protein folding is the physical process by which a protein chain acquires its native 3-dimensional structure, a conformation that is usually biologically functional, in an expeditious and reproducible manner.
Protein Folding-biophysical and cellular aspects, protein denaturation
Protein Folding-biophysical and cellular aspects, protein denaturation
AnishaMukherjee5
Describes various aspects of Ramachandran plot. Different torsion angles are described with clear figures. How protein folding is affected by torsion angles is also explained.
Ramachandran plot
Ramachandran plot
Radhakrishna Gopala Pillai
Includes basic and the main topic....wholly covered
The Ramachandran plot
The Ramachandran plot
K Tanay
BIOCHEMISTRY
Secondary Structure Of Protein (Repeating structure of protein)
Secondary Structure Of Protein (Repeating structure of protein)
Amrutha Hari
covalent and non-covalent bonds
Forces stabilising structure of proteins
Forces stabilising structure of proteins
Raviz Prathyusha
Describes Ramachandran plot at Graduate level with figures and explanations in simple language
Ramachandran plot
Ramachandran plot
Radhakrishna Gopala Pillai
Introduction Definition Levinthal’s Paradox Relation between folding & amino acid sequence Factors affecting protein folding Biophysical aspects -Hierarchy in protein structure -Thermodynamic consideration Conclusion References
Protein folding by KK Sahu
Protein folding by KK Sahu
KAUSHAL SAHU
here the modifications of protein i.e co and post are described .
Co and post translationational modification of proteins
Co and post translationational modification of proteins
Sukirti Vedula
Protein are amino acids chains that acquire their biological properties by folding in to unique 3 D structure
Protein folding slids
Protein folding slids
anam tariq
Ramachandran plot for structural validation of protein will give information whether your protein or model protein is allowed or not in three dimensional point of view.
Ramachandran plot by Krunal Chodvadiya
Ramachandran plot by Krunal Chodvadiya
chodvadiyakrunal
Quaternary structure of protein
Quaternary structure of protein
Arjun K Gopi
In this presentation i have explained about all the super secondary structure their types and their functions . The ppt has been made in such a way that it will clear out our basic concepts first and then it will go higher. I hope you like it
Super secondary structure of protein
Super secondary structure of protein
SatvikSharma29
supersecondary structures types of supersecondary structures
Supersecondary structure ppt
Supersecondary structure ppt
Mary Theresa
This ppt will help you get through the complete topic for RAMACHANDRAN PLOT in detail . for detailed explanation , watch the lecture on my youtube channel - BOTANY INSIDER
Ramachandran plot
Ramachandran plot
Kajal Jain
Chaperones are a functionally related group of proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
Chaperones
Chaperones
Hadeeqa Aiman
Hydrogen bonding Base stacking Hydrophobic interaction Ionic bonding
Forces stabilizing nucleic acid structure
Forces stabilizing nucleic acid structure
Gaurav Aggarwal
Proteins are dynamic molecules whose functions almost invariably depend on interactions with other molecules. A molecule bound reversibly by a protein is called a ligand. A ligand binds at a site on the protein called the binding site, which is complementary to the ligand in size, shape, charge, and hydrophobic or hydrophilic character.
PROTIEN LIGAND INTERACTIONS
PROTIEN LIGAND INTERACTIONS
National Institute of Pharmaceutical Education and Research (NIPER), Hyderabad
folding of proteins
Protein folding @ sid
Protein folding @ sid
sidjena70
Great Slide by Ghafran Ali Biotechnology
Protein folding
Protein folding
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plzz leave your comments.... Publisher Aamer al zaman..Contact no:+923438853008
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This contains DNA Supercoiling , relation between Linking no,Twist and Writhe and a brief explanation of Topoisomerase
DNA Supercoiling
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For protein Engineering
Beta
Beta
Nithin Chandran
Proteins are complex molecules made up of long chains of amino acids. The secondary structure of a protein refers to the local folding patterns that occur within these chains. The two most common types of secondary structures are alpha helices and beta sheets. In an alpha helix, the polypeptide chain is coiled in a right-handed spiral, with hydrogen bonds forming between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid three residues down the chain. This structure gives the alpha helix a rod-like shape, which is stabilized by these hydrogen bonds. In contrast, beta sheets consist of extended strands of amino acids that are held together by hydrogen bonds between adjacent strands. These strands can be either parallel, with the amino acids in each strand oriented in the same direction, or antiparallel, with the amino acids in each strand oriented in opposite directions. Beta sheets can form flat, sheet-like structures, or can be twisted to form a more compact structure. Other secondary structures, such as beta turns and loops, also play important roles in protein structure and function. These structures help to stabilize the overall three-dimensional shape of the protein, which is critical for its function.
Secondary structure of proteins- Sonal Singh Shrivas.pptx
Secondary structure of proteins- Sonal Singh Shrivas.pptx
SonalShrivas
Weitere ähnliche Inhalte
Was ist angesagt?
Introduction Definition Levinthal’s Paradox Relation between folding & amino acid sequence Factors affecting protein folding Biophysical aspects -Hierarchy in protein structure -Thermodynamic consideration Conclusion References
Protein folding by KK Sahu
Protein folding by KK Sahu
KAUSHAL SAHU
here the modifications of protein i.e co and post are described .
Co and post translationational modification of proteins
Co and post translationational modification of proteins
Sukirti Vedula
Protein are amino acids chains that acquire their biological properties by folding in to unique 3 D structure
Protein folding slids
Protein folding slids
anam tariq
Ramachandran plot for structural validation of protein will give information whether your protein or model protein is allowed or not in three dimensional point of view.
Ramachandran plot by Krunal Chodvadiya
Ramachandran plot by Krunal Chodvadiya
chodvadiyakrunal
Quaternary structure of protein
Quaternary structure of protein
Arjun K Gopi
In this presentation i have explained about all the super secondary structure their types and their functions . The ppt has been made in such a way that it will clear out our basic concepts first and then it will go higher. I hope you like it
Super secondary structure of protein
Super secondary structure of protein
SatvikSharma29
supersecondary structures types of supersecondary structures
Supersecondary structure ppt
Supersecondary structure ppt
Mary Theresa
This ppt will help you get through the complete topic for RAMACHANDRAN PLOT in detail . for detailed explanation , watch the lecture on my youtube channel - BOTANY INSIDER
Ramachandran plot
Ramachandran plot
Kajal Jain
Chaperones are a functionally related group of proteins that assist the covalent folding or unfolding and the assembly or disassembly of other macromolecular structures.
Chaperones
Chaperones
Hadeeqa Aiman
Hydrogen bonding Base stacking Hydrophobic interaction Ionic bonding
Forces stabilizing nucleic acid structure
Forces stabilizing nucleic acid structure
Gaurav Aggarwal
Proteins are dynamic molecules whose functions almost invariably depend on interactions with other molecules. A molecule bound reversibly by a protein is called a ligand. A ligand binds at a site on the protein called the binding site, which is complementary to the ligand in size, shape, charge, and hydrophobic or hydrophilic character.
PROTIEN LIGAND INTERACTIONS
PROTIEN LIGAND INTERACTIONS
National Institute of Pharmaceutical Education and Research (NIPER), Hyderabad
folding of proteins
Protein folding @ sid
Protein folding @ sid
sidjena70
Great Slide by Ghafran Ali Biotechnology
Protein folding
Protein folding
Facebook
ALL BASIC AND IMPORTANT CONTENT REGARDING HELIX LOOP HELIX AND HELIX TURN HELIX.. ALL ITS FUNCTION AND SUMMARY. HOPE YOU WILL FIND IT EASY..
HELIX-LOOP-HELIX, HELIX-TURN-HELIX
HELIX-LOOP-HELIX, HELIX-TURN-HELIX
naren
plzz leave your comments.... Publisher Aamer al zaman..Contact no:+923438853008
Bacterial gene mapping
Bacterial gene mapping
Aamer Al Zaman Chaudhary
melting temperature of DNA Chargaff's rule on DNA & RNA denaturation renaturation hyperchromism hypochromism
Tm of DNA - melting temperature of DNA
Tm of DNA - melting temperature of DNA
Mandira bhosale
DNA Histones Non histones helix turn helix motif zinc finger leucine zipper
Dna binding proteins
Dna binding proteins
Hari Sharan Makaju
biochemistry
Abzymes
Abzymes
jeeva raj
expalins about detailed mechanism of the trp operon and its attenuation
Trp operon
Trp operon
Neerajkalyan Gandholi
This contains DNA Supercoiling , relation between Linking no,Twist and Writhe and a brief explanation of Topoisomerase
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Was ist angesagt?
(20)
Protein folding by KK Sahu
Protein folding by KK Sahu
Co and post translationational modification of proteins
Co and post translationational modification of proteins
Protein folding slids
Protein folding slids
Ramachandran plot by Krunal Chodvadiya
Ramachandran plot by Krunal Chodvadiya
Quaternary structure of protein
Quaternary structure of protein
Super secondary structure of protein
Super secondary structure of protein
Supersecondary structure ppt
Supersecondary structure ppt
Ramachandran plot
Ramachandran plot
Chaperones
Chaperones
Forces stabilizing nucleic acid structure
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PROTIEN LIGAND INTERACTIONS
PROTIEN LIGAND INTERACTIONS
Protein folding @ sid
Protein folding @ sid
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HELIX-LOOP-HELIX, HELIX-TURN-HELIX
Bacterial gene mapping
Bacterial gene mapping
Tm of DNA - melting temperature of DNA
Tm of DNA - melting temperature of DNA
Dna binding proteins
Dna binding proteins
Abzymes
Abzymes
Trp operon
Trp operon
DNA Supercoiling
DNA Supercoiling
Ähnlich wie Alpha domain structurs
For protein Engineering
Beta
Beta
Nithin Chandran
Proteins are complex molecules made up of long chains of amino acids. The secondary structure of a protein refers to the local folding patterns that occur within these chains. The two most common types of secondary structures are alpha helices and beta sheets. In an alpha helix, the polypeptide chain is coiled in a right-handed spiral, with hydrogen bonds forming between the carbonyl oxygen of one amino acid and the amide hydrogen of an amino acid three residues down the chain. This structure gives the alpha helix a rod-like shape, which is stabilized by these hydrogen bonds. In contrast, beta sheets consist of extended strands of amino acids that are held together by hydrogen bonds between adjacent strands. These strands can be either parallel, with the amino acids in each strand oriented in the same direction, or antiparallel, with the amino acids in each strand oriented in opposite directions. Beta sheets can form flat, sheet-like structures, or can be twisted to form a more compact structure. Other secondary structures, such as beta turns and loops, also play important roles in protein structure and function. These structures help to stabilize the overall three-dimensional shape of the protein, which is critical for its function.
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