slides
... These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. Such methods were typically ~60% accurate in predicting which of the three states (helix/sheet/coil) a ...
... These methods were based on the helix- or sheet-forming propensities of individual amino acids, sometimes coupled with rules for estimating the free energy of forming secondary structure elements. Such methods were typically ~60% accurate in predicting which of the three states (helix/sheet/coil) a ...
THE CENTRAL DOGMA THE CENTRAL DOGMA
... residues close to each other in the primary sequence • Tertiary – non-covalent or covalent interactions between secondary structural elements • Quaternary – non-covalent or covalent interactions between different polypeptide chains ...
... residues close to each other in the primary sequence • Tertiary – non-covalent or covalent interactions between secondary structural elements • Quaternary – non-covalent or covalent interactions between different polypeptide chains ...
LectureIV
... • A centralized database (PDB) contains all solved protein structures – XYZ coordinate of atoms within specified precision – ~19,000 solved structures ...
... • A centralized database (PDB) contains all solved protein structures – XYZ coordinate of atoms within specified precision – ~19,000 solved structures ...
PowerPoint Slides
... • Proteins which have >~50% of their secondary structure elements arranged the in the same order in the protein chain and in three dimensions are classified as having the same fold • No evolutionary relation between proteins *confusingly also called fold classes ...
... • Proteins which have >~50% of their secondary structure elements arranged the in the same order in the protein chain and in three dimensions are classified as having the same fold • No evolutionary relation between proteins *confusingly also called fold classes ...
Reading Guide: Pratt and Cornely, Chapter 4, pp 87
... 8. Draw the structure of MSG (monosodium glutamate.) What is its role in taste perception. 9. Assuming all conventions, draw the oligopeptide: WACPR. What is its net charge at pH 7? What is its net charge at pH 8.4? (Use Table 4.1 for pKa values.) 10. Describe the four levels of protein structure. 1 ...
... 8. Draw the structure of MSG (monosodium glutamate.) What is its role in taste perception. 9. Assuming all conventions, draw the oligopeptide: WACPR. What is its net charge at pH 7? What is its net charge at pH 8.4? (Use Table 4.1 for pKa values.) 10. Describe the four levels of protein structure. 1 ...
Answers
... CLUSTALW 1.8 was used for multiple alignment of the three sequences. Areas where there were difference between the sequences were identified using Boxshade version 3.21 – these are shown in the file “Boxshade results”. It can be see that the VEGA sequence has an extra 22 amino acids at the N terminu ...
... CLUSTALW 1.8 was used for multiple alignment of the three sequences. Areas where there were difference between the sequences were identified using Boxshade version 3.21 – these are shown in the file “Boxshade results”. It can be see that the VEGA sequence has an extra 22 amino acids at the N terminu ...
de novo Protein Design
... chemical denaturation is characteristic of the twostate unfolding expected for small, two-state, monomeric single-domain protein ...
... chemical denaturation is characteristic of the twostate unfolding expected for small, two-state, monomeric single-domain protein ...
Visualization: A New Dimension to Research
... making proteins Protein = molecules of (20) amino acids that perform much of life’s function Proteome = set of all proteins in a cell ...
... making proteins Protein = molecules of (20) amino acids that perform much of life’s function Proteome = set of all proteins in a cell ...
Membrane Proteins Integral membrane proteins often contain
... Integral membrane proteins often contain helical segments of appropriate length to span the lipid bilayer. In a protein that has a single segment that spans the membrane, the helix usually only contains hydrophobic residues and is called a single-span membrane protein. In transmembrane proteins with ...
... Integral membrane proteins often contain helical segments of appropriate length to span the lipid bilayer. In a protein that has a single segment that spans the membrane, the helix usually only contains hydrophobic residues and is called a single-span membrane protein. In transmembrane proteins with ...
Faraday Discussion Meeting September 2002
... The effect of applied force on the energy landscape that describes protein conformation is an exciting and challenging topic in molecular biophysics. Recently it has become possible to use nanotechnology tools such as the atomic force microscope and laser tweezers to manipulate individual molecules ...
... The effect of applied force on the energy landscape that describes protein conformation is an exciting and challenging topic in molecular biophysics. Recently it has become possible to use nanotechnology tools such as the atomic force microscope and laser tweezers to manipulate individual molecules ...
Blast and Database Searches
... Alignment is used to determine if a sequence is like another sequence, uncovering identical or similar regions. ...
... Alignment is used to determine if a sequence is like another sequence, uncovering identical or similar regions. ...
Biological Databases - University of Alberta
... • Classification of proteins based on domain structures • Each protein chopped into individual domains and assigned into homologous superfamilies. • Hierarchial domain classification of PDB entries. ...
... • Classification of proteins based on domain structures • Each protein chopped into individual domains and assigned into homologous superfamilies. • Hierarchial domain classification of PDB entries. ...
Interaction Site Evolution
... DNA is the blueprint for generating strings of amino acids which fold into proteins. The interactions these proteins form with each other are primary components of organismal physiology. Proteins assume very specific shapes, and the amino acids on their surface involved in protein interactions are s ...
... DNA is the blueprint for generating strings of amino acids which fold into proteins. The interactions these proteins form with each other are primary components of organismal physiology. Proteins assume very specific shapes, and the amino acids on their surface involved in protein interactions are s ...
Structural Studies of Sgt2, a Component of the GET Pathway that
... Structural Studies of Sgt2, a Component of the GET Pathway that Mediates the Sorting of Tail-anchored Proteins to the ER Membrane. Nuri Sung, Sukyeong Lee, Amadeo B. Biter, and Francis T.F. Tsai Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One ...
... Structural Studies of Sgt2, a Component of the GET Pathway that Mediates the Sorting of Tail-anchored Proteins to the ER Membrane. Nuri Sung, Sukyeong Lee, Amadeo B. Biter, and Francis T.F. Tsai Verna and Marrs McLean Department of Biochemistry and Molecular Biology, Baylor College of Medicine, One ...
Slide 1
... • Because the positions of all database word matches are indexed and stored prior to the blast search, the relevant parts of search space are reached quickly. • Tradeoff is in accuracy and certainty – occasionally matches will be missed (when they are distant enough and dispersed enough that no loca ...
... • Because the positions of all database word matches are indexed and stored prior to the blast search, the relevant parts of search space are reached quickly. • Tradeoff is in accuracy and certainty – occasionally matches will be missed (when they are distant enough and dispersed enough that no loca ...
Chemotaxis pahtway How can physics help?
... • The same organism has several CheA, CheW and MCP. ...
... • The same organism has several CheA, CheW and MCP. ...
Ivy Mead 24 February 2011 Bioinformatics Lab report 3 The analysis
... less closely related for reasons stated in the former paragraph. A middle range alignment is best for a component that is more likely to differ, although the standard should not be so low as to not align the binding site. It is also important to note that the default gap penalty is not ideal for all ...
... less closely related for reasons stated in the former paragraph. A middle range alignment is best for a component that is more likely to differ, although the standard should not be so low as to not align the binding site. It is also important to note that the default gap penalty is not ideal for all ...
Document
... between conserved domains. • In known sequences, gaps are preferentially found between secondary structure elements (alpha helices, beta strands). ...
... between conserved domains. • In known sequences, gaps are preferentially found between secondary structure elements (alpha helices, beta strands). ...
Pfam
... • A common usage is that superfamilies contain families which contain sub-families. • Many proteins comprise multiple independent structural and functional units or domains. Due to evolutionary shuffling, different domains in a protein have evolved independently. This has led, in recent years, to a ...
... • A common usage is that superfamilies contain families which contain sub-families. • Many proteins comprise multiple independent structural and functional units or domains. Due to evolutionary shuffling, different domains in a protein have evolved independently. This has led, in recent years, to a ...
Teaching Notes
... proteins) may have protein chains with interfaces that have hydrophobic amino acids. These proteins chains seek out and bind to partner proteins with complimentary interfaces and form functional assemblies. 5. In proteins that are composed of multiple domains, connected with flexible linker regions, ...
... proteins) may have protein chains with interfaces that have hydrophobic amino acids. These proteins chains seek out and bind to partner proteins with complimentary interfaces and form functional assemblies. 5. In proteins that are composed of multiple domains, connected with flexible linker regions, ...
BY 330 Spring 2015Worksheet 3 Draw a protein made up of two
... 1. Draw a protein made up of two amino acids. Label the peptide bonds and indicate the N and C termini. What kind of reaction links amino acids together? ...
... 1. Draw a protein made up of two amino acids. Label the peptide bonds and indicate the N and C termini. What kind of reaction links amino acids together? ...
Structural alignment
Structural alignment attempts to establish homology between two or more polymer structures based on their shape and three-dimensional conformation. This process is usually applied to protein tertiary structures but can also be used for large RNA molecules. In contrast to simple structural superposition, where at least some equivalent residues of the two structures are known, structural alignment requires no a priori knowledge of equivalent positions. Structural alignment is a valuable tool for the comparison of proteins with low sequence similarity, where evolutionary relationships between proteins cannot be easily detected by standard sequence alignment techniques. Structural alignment can therefore be used to imply evolutionary relationships between proteins that share very little common sequence. However, caution should be used in using the results as evidence for shared evolutionary ancestry because of the possible confounding effects of convergent evolution by which multiple unrelated amino acid sequences converge on a common tertiary structure.Structural alignments can compare two sequences or multiple sequences. Because these alignments rely on information about all the query sequences' three-dimensional conformations, the method can only be used on sequences where these structures are known. These are usually found by X-ray crystallography or NMR spectroscopy. It is possible to perform a structural alignment on structures produced by structure prediction methods. Indeed, evaluating such predictions often requires a structural alignment between the model and the true known structure to assess the model's quality. Structural alignments are especially useful in analyzing data from structural genomics and proteomics efforts, and they can be used as comparison points to evaluate alignments produced by purely sequence-based bioinformatics methods.The outputs of a structural alignment are a superposition of the atomic coordinate sets and a minimal root mean square deviation (RMSD) between the structures. The RMSD of two aligned structures indicates their divergence from one another. Structural alignment can be complicated by the existence of multiple protein domains within one or more of the input structures, because changes in relative orientation of the domains between two structures to be aligned can artificially inflate the RMSD.