The Ramachandran diagram.

Slides:



Advertisements
Similar presentations
Protein Structure Basics Presented by Alison Fraser, Christine Lee, Pradhuman Jhala, Corban Rivera.
Advertisements

PROTEINS Proteins are the most complex and most diverse group of biological compounds. If you weigh about 70 kg: About 50 of your 70 kg is water. Many.
Protein Structure C483 Spring 2013.
Protein Structure – Part-2 Pauling Rules The bond lengths and bond angles should be distorted as little as possible. No two atoms should approach one another.
©CMBI 2001 The amino acids in their natural habitat.
The amino acids in their natural habitat. Topics: Hydrogen bonds Secondary Structure Alpha helix Beta strands & beta sheets Turns Loop Tertiary & Quarternary.
S ASC Answer to Practice Problem
Lecture 11 Test next week in class Protein structure.
The Structure and Functions of Proteins BIO271/CS399 – Bioinformatics.
Introduction to Protein Structure
Protein-a chemical view A chain of amino acids folded in 3D Picture from on-line biology bookon-line biology book Peptide Protein backbone N / C terminal.
Proteins Dr Una Fairbrother. Dipeptides u Two amino acids are combined as in the diagram, to form a dipeptide. u Water is the other product.
Protein Secondary Structure : Kendrew Solves the Structure of Myoglobin “Perhaps the most remarkable features of the molecule are its complexity.
Protein Basics Protein function Protein structure –Primary Amino acids Linkage Protein conformation framework –Dihedral angles –Ramachandran plots Sequence.
Globular Proteins Proteins with a compact folded structure (with an interior and exterior), generally containing different types of secondary structure.
Proteins Structures Primary Structure.
Fundamentals of Biochemistry
(Foundation Block) Dr. Ahmed Mujamammi Dr. Sumbul Fatma
Protein Structure Lecture 2/26/2003. beta sheets are twisted Parallel sheets are less twisted than antiparallel and are always buried. In contrast, antiparallel.
Lecture 3. α domain structures Coiled-coil, knobs and hole packing Four-helix bundle Donut ring large structure Globin fold Ridges and grooves model CS882,
Proteins account for more than 50% of the dry mass of most cells
Proteins Dr. Sumbul Fatma Clinical Chemistry Unit
The structural organization within proteins Kevin Slep June 13 th, 2012.
Types of Proteins Proteomics - study of large sets of proteins, such as the entire complement of proteins produced by a cell E. coli has about 4000 different.
Supersecondary structures. Supersecondary structures motifs motifs or folds, are particularly stable arrangements of several elements of the secondary.
Lecture 10: Protein structure
Introduction to Protein Structure
The most important secondary structural elements of proteins are: A. α-Helix B. Pleated-sheet structures C. β Turns The most common secondary structures.
Proteins. Proteins? What is its How does it How is its How does it How is it Where is it What are its.
Proteins: Amino Acid Chains DNA Polymerase from E. coli Standard amino acid backbone: Carboxylic acid group, amino group, the alpha hydrogen and an R group.
STRUCTURAL ORGANIZATION
BD2ZdVSe2vQ&feature=related.
The three important structural features of proteins: a. Primary (1 o ) – The amino acid sequence (coded by genes) b. Secondary (2 o ) – The interaction.
BRANDI AND ZAK. Secondary Structure Can fold and align them selves and the repeating pattern is called a secondary structure. Common structures are the.
Paul D. Adams University of Arkansas Mary K. Campbell Shawn O. Farrell Chapter Four The Three-Dimensional.
AP Biology Proteins. AP Biology Proteins  Most structurally & functionally diverse group of biomolecules  Function:  involved in almost everything.
Protein Folding & Biospectroscopy F14PFB David Robinson Mark Searle Jon McMaster
Amino acids and proteins … for AS Biology. Amino acids Proteins are macromolecules consisting of long unbranched chains of amino acids. All amino acids.
Chapter 14 Proteins. Peptides and Proteins Proteins behave as zwitterions. isoelectric point, pI Proteins also have an isoelectric point, pI. ◦ At its.
CS790 – BioinformaticsProtein Structure and Function1 Review of fundamental concepts  Know how electron orbitals and subshells are filled Know why atoms.
AP Biology Proteins. AP Biology Proteins  Most structurally & functionally diverse group of biomolecules  Function:  involved in.
MCC BP Based on work by K. Foglia Proteins.
Tertiary structure combines regular secondary structures and loops (coil) Bovine carboxypeptidase A.
Protein Structure 1 Primary and Secondary Structure.
©CMBI 2001 Step 5: The amino acids in their natural habitat.
The α-helix forms within a continuous strech of the polypeptide chain 5.4 Å rise, 3.6 aa/turn  1.5 Å/aa N-term C-term prototypical  = -57  ψ = -47 
Protein Structure (Foundation Block) What are proteins? Four levels of structure (primary, secondary, tertiary, quaternary) Protein folding and stability.
Protein Structure (Foundation Block) What are proteins? Four levels of structure (primary, secondary, tertiary, quaternary) Protein folding and stability.
Proteins Dr. Sumbul Fatma Clinical Chemistry Unit Department of Pathology Tel
3-D Structure of Proteins
W-H Based on work by K. Foglia Proteins. W-H Based on work by K. Foglia Proteins  Most structurally & functionally diverse group of biomolecules  Function:
Protein Structure and Bioinformatics. Chapter 2 What is protein structure? What are proteins made of? What forces determines protein structure? What is.
Proteins: 3D-Structure Chapter 6 (9 / 17/ 2009)
Sections 14.9, 14.10, 14.11, and Hannah Nowell and Jenny Sulouff.
Protein backbone Biochemical view:
AP Biology Proteins AP Biology Proteins Multipurpose molecules.
Doug Raiford Lesson 14.  Reminder  Involved in virtually every chemical reaction ▪ Enzymes catalyze reactions  Structure ▪ muscle, keratins (skin,
Enzymes SADIA SAYED. Enzymes are proteins  All enzymes are proteins  Strings of amino acids folding up into distinct structures  The properties of.
Peptides. Structure and functions of proteins Department of General Chemistry Poznań University of Medical Sciences MD 2015/16.
Structural organization of proteins
Mir Ishruna Muniyat. Primary structure (Amino acid sequence) ↓ Secondary structure ( α -helix, β -sheet ) ↓ Tertiary structure ( Three-dimensional.
19.5 Protein Structure: Tertiary and Quaternary Levels
Protein Structure and Properties
The heroic times of crystallography
Protein Structure September 7,
The Peptide Bond Amino acids are joined together in a condensation reaction that forms an amide known as a peptide bond.
The Peptide Bond Amino acids are joined together in a condensation reaction that forms an amide known as a peptide bond.
Biochem Block Handout #6: Protein Structure
ACTIVE FIGURE 6.4 A Ramachandran diagram showing the sterically reasonable values of the angles  and . The shaded regions indicate particularly favorable.
The Three-Dimensional Structure of Proteins
Presentation transcript:

The Ramachandran diagram.

Allowed phi and psi torsion angles in proteins.

The Ramachandran diagram of Gly residues in a polypeptide chain.

Interconversion catalyzed by peptidyl prolyl cis-trans isomerases Cis/Trans Isomerization: Proline trans cis Energy difference between these forms is small. Nearly all Xaa-Pro linkages are biosynthesized in the trans form. ~10% of these peptide bonds are in the cis form in globular proteins. Interconversion catalyzed by peptidyl prolyl cis-trans isomerases

Stereo space-filling representation of an a helical segment of sperm whale myoglobin (its E-helix) as determined by X-ray crystal structure analysis.

The hydrogen bonding pattern of several polypeptide helices.

Comparison of the two polypeptide helices that occasionally occur in proteins with the commonly occurring a helix.

b pleated sheet: antiparallel orientation

b pleated sheets: parallel orientation

A two-stranded b antiparallel pleated sheet drawn to emphasize its pleated appearance.

Stereo space-filling representation of the 6-stranded antiparallel b pleated sheet in jack bean concanavalin A as determined by crystal X-ray analysis.

Polypeptide chain folding in proteins illustrating the right-handed twist of b sheets: bovine carboxypeptidase A.

Polypeptide chain folding in proteins illustrating the right-handed twist of b sheets: chicken muscle triose phosphate isomerase. (b barrel)

Connections between adjacent polypeptide strands in b pleated sheets. hairpin out-of-plane crossovers Connections between adjacent polypeptide strands in b pleated sheets.

Origin of a right-handed crossover connection.

Reverse turns in polypeptide chains.

Space-filling representation of an Ω loop comprising residues 40 to 54 of cytochrome c.

The structure of a keratin.

The two-stranded coiled coil: view down the coil axis showing the interactions between the nonpolar edges of the a helices.

The two-stranded coiled coil: side view in which the polypeptide back bone is represented by skeletal (left) and space-filling (right) forms.

The amino acid sequence at the C-terminal end of the triple helical region of the bovine a1(I) collagen chain.

The triple helix of collagen.

X-Ray structure of the triple helical collagen model peptide (Pro-Hyp-Gly)10 in which the fifth Gly is replaced by Ala. (a) Ball and stick representation.

X-Ray structure of the triple helical collagen model peptide (Pro-Hyp-Gly)10 in which the fifth Gly is replaced by Ala. (b) View along helix axis.

X-Ray structure of the triple helical collagen model peptide (Pro-Hyp-Gly)10 in which the fifth Gly is replaced by Ala. (c) A schematic diagram.

A biosynthetic pathway for cross-linking Lys, Hyl, and His side chains in collagen.

X-Ray diffraction photograph of a single crystal of sperm whale myoglobin.

Electron density maps of proteins (heme of sperm whale myoglobin) (2 angstrom resolution)

Electron density maps of proteins (sperm whale myoglobin) (2 Electron density maps of proteins (sperm whale myoglobin) (2.4 angstrom resolution)

Sections through the electron density map of diketopiperazine calculated at the indicated resolution.

The 2D proton NMR structures of proteins: a NOESY spectrum of a protein presented as a contour plot with two frequency axes w1 and w2.

The 2D proton NMR structures of proteins: NMR structure of a 64-residue polypeptide comprising the Src protein SH3 domain.

Representations of the X-ray structure of sperm whale myoglobin: the protein and its bound heme are drawn in stick form.

8 helices Representations of the X-ray structure of sperm whale myoglobin: a diagram in which the protein is represented by its computer-generated Ca backbone.

Representations of the X-ray structure of sperm whale myoglobin: a computer-generated cartoon drawing.

The X-ray structure of jack bean protein concanavalin A.

Human carbonic anhydrase.

The x-ray structure of horse heart cytochrome c The x-ray structure of horse heart cytochrome c. (hydrophobic residues in red)

The x-ray structure of horse heart cytochrome c The x-ray structure of horse heart cytochrome c. (hydrophilic residues in green)

H-helix Representations of the x-ray structure of sperm whale myoglobin: a diagram in which the protein is represented by its computer-generated Ca backbone.

The H helix of sperm whale myoglobin The H helix of sperm whale myoglobin. (a) A helical wheel representation in which the side chain positions about the a helix are projected down the helix axis onto a plane.

The H helix of sperm whale myoglobin: a skeletal model The H helix of sperm whale myoglobin: a skeletal model. (orange = nonpolar; purple = polar)

The H helix of sperm whale myoglobin: a space-filling model. orange = nonpolar purple = polar The H helix of sperm whale myoglobin: a space-filling model.

A space-filling model of an antiparallel b sheet from concanavalin A. red = nonpolar purple = polar A space-filling model of an antiparallel b sheet from concanavalin A.

two domains One subunit of the enzyme glyceraldehyde-3-phosphate dehydrogenase from Bacillus stearothermophilus.

Schematic diagrams of supersecondary structures. aa bab b-hairpin Schematic diagrams of supersecondary structures.

Schematic diagrams of supersecondary structures. Greek key motif Schematic diagrams of supersecondary structures.

X-ray structures of 4-helix bundle proteins: E. coli cytochrome b562. directionality of helices X-ray structures of 4-helix bundle proteins: E. coli cytochrome b562.

X-ray structures of 4-helix bundle proteins: human growth hormone. directionality of helices X-ray structures of 4-helix bundle proteins: human growth hormone.

X-ray structure of the immunoglobulin fold. stacked 4-stranded and 3-stranded antiparallel b-sheets X-ray structure of the immunoglobulin fold.

X-ray structure of retinol binding protein. Up-down b-barrel X-ray structure of retinol binding protein.

X-ray structure of the C-terminal domain of bovine g-b crystallin: a topological diagram showing how its two Greek key motifs are arranged in a b barrel.

X-ray structure of the C-terminal domain of bovine g-b crystallin: the 83-residue peptide backbone displayed in ribbon form.

X-ray structure of the enzyme, peptide-N4-(N-acetyl-b-D-glucosaminyl)asparagine amidase F from Flavobacterium meningosepticum.

X-ray structure of the enzyme, peptide-N 4-(N-acetyl-b-D-glucosaminyl)asparagine amidase F from Flavobacterium meningosepticum.

The X-ray structure of the 247-residue enzyme triose phosphate isomerase (TIM) from chicken muscle.

Topological diagrams of (a) carboxypeptidase A and (b) the N-terminal domain of glyceraldehyde-3-phosphate dehydrogenase.

X-ray structures of open b sheet-containing enzymes: dogfish lactate dehydrogenase, N-terminal domain (residues 20-163 of this 330-residue protein).

X-ray structures of open b sheet-containing enzymes: porcine adenylate kinase (195 residues).

Doubly wound sheets.

Graphical Representation and Analysis of Surface Properties A GRASP diagram of human growth hormone (helps predict protein interactions with charged molecules)

Thermodynamic changes for transferring hydrocarbons from water to nonpolar solvents at 25°C.

Hydropathy Scale for Amino Acid Side Chains

Hydropathic index plot for bovine chymotrypsinogen.

Protein denaturation curve

strengthen hydrophobic interactions Hofmeister series chaotropic Weaken hydrophobic interactions Melting temperature of RNase A as a function of the concentration of various salts.

The structural hierarchy in proteins.

The quaternary structure of hemoglobin

Some possible symmetries of proteins with identical protomers Some possible symmetries of proteins with identical protomers. (a) Assemblies with the cyclic symmetries C2, C3, and C5.

Some possible symmetries of proteins with identical protomers Some possible symmetries of proteins with identical protomers. (b) Assemblies with the dihedral symmetries D2, D4, and D3.

Some possible symmetries of proteins with identical protomers Some possible symmetries of proteins with identical protomers. (c) Assemblies with T, O, and I symmetries.

A dimer of transthyretin as viewed down its twofold axis (red lenticular symbol).

X-ray structure of glutamine synthetase from Salmonella typhimurium - view down 6-fold symmetry axis

X-ray structure of glutamine synthetase from Salmonella typhimurium - view down one of the 2-fold symmetry axes

A helical structure composed of a single kind of subunit. actin, tubulin A helical structure composed of a single kind of subunit.

Chemical cross-linking agents.

Structural Bioinformatics Websites (URLs)

Structural Bioinformatics Websites (URLs)

Structural Bioinformatics Websites (URLs)