Chapter 9

11/16/04

Click here to start

Table of Contents

Reductive denaturation and oxidative renaturation of RNase A

Plausible mechanism for the thiol- or enzyme-catalyzed disulfide interchange reaction in a protein

Primary structure of porcine proinsulin

Hierarchical organization of globular proteins (subdomains)

NMR structure of protein GB1

X-ray structure of Rop protein, a homodimer of aa motifs that associate to form a 4-helix bundle

A stopped-flow device: 40 ms dead-times

UV absorbance spectra of the three aromatic amino acids, phenylalanine, tryptophan, and tyrosine

Circular dichroism (CD) spectra of polypeptides

Folding funnels: An idealized funnel landscape

Folding funnels: The Levinthal "golf course" landscape

Folding funnels: Classic folding landscape

Folding funnels: Rugged energy surface

Polypeptide backbone and disulfide bonds of native BPTI (58 residues, three disulfide bonds)

Renaturation of BPTI: protein primary structures evolved to specify efficient folding pathways as well as stable native conformations

Reactions catalyzed by protein disulfide isomerase (PDI). (a) Reduced PDI catalyzes the rearrangement of the non-native disulfide bonds.

Reactions catalyzed by protein disulfide isomerase (PDI). (b) The oxidized PDI-dependent synthesis of disulfide bonds in proteins.

NMR structure of the a domain of human protein disulfide isomerase (PDI-a) in its oxidized form. (a) The polypeptide backbone is shown in ribbon form.

NMR structure of the a domain of human protein disulfide isomerase (PDI-a) in its oxidized form. (b) The molecular structure as viewed from the bottom.

Electron micrograph-derived 3D image of the Hsp60 (GroEL) chaperonin from the photosynthetic bacterium Rhodobacter sphaeroides.

X-ray structure of GroEL. (a) Side view perpendicular to the 7-fold axis.

X-ray structure of GroEL. (b) Top view along the 7-fold axis.

X-ray structure of GroES as viewed along its 7-fold axis.

X-ray structure of the GroEL-GroES-(ADP)7 complex.

X-ray structure of the GroEL-GroES-(ADP)7 complex.

X-ray structure of the GroEL-GroES-(ADP)7 complex.

Domain movements in GroEL. (a) Ribbon diagram of a single subunit of GroEL in the X-ray structure of GroEL alone.

Domain movements in GroEL. (b) A GroEL subunit in the
X-ray structure of GroEL-GroES-(ADP)7.

Domain movements in GroEL. (c) Schematic diagram indicating the conformational changes in GroEL when it binds GroES.

Apical domain of GroEL in complex with a tight-binding 12-residue polypeptide (SWMTTPWGFLHP).

Movements of the polypeptide-binding helices of GroEL.

Reaction cycle of
the GroEL/ES
chaperonin system
in protein folding.

Rate of hydrogen-tritium exchange of tritiated RuBisCO.

Schematic diagram of the mechanism of stretch-induced hydrogen exchange by the GroEL/ES system.

Propensities and classifications of amino acid residues for a helical and b sheet conformations.

Secondary structure prediction in adenylate kinase ( N-terminal 24 residues)

Structures of the second zinc finger motif of Zif268 (DNA-binding protein): X-ray structure.

Structure of de novo designed peptide, FSD-1: NMR structure (a bba motif; 28 residues)

Comparison of the structures of the second zinc finger motif of Zif268 and FSD-1: best-fit superpositions of their backbones.

Conformational fluctuations (breathing motions) in the oxygen binding protein, myoglobin.

The mobility of the GroEL subunit in the X-ray structure of GroEL alone.

The mobility of the GroEL subunit in the X-ray structure of the GroEL-GroES-(ADP)7 complex.

The internal motions of myoglobin as determined by a molecular dynamics simulation: the Ca backbone and the heme group.

The internal motions of myoglobin as determined by a molecular dynamics (MD) simulation: an a helix.

The hydrogen-tritium "exchange-out" curve for hemoglobin that has been pre-equilibrated with tritiated water.

Amyloid fibrils: an electron micrograph of amyloid fibrils of the protein PrP 27-30.

Amyloid fibrils (PrP 27-30): Model (a) and isolated (b) b sheet.

Superposition of wild-type human lysozyme and its D67H mutant.

Evidence that the scrapie agent is a protein: scrapie agent is inactivated by treatment with diethylpyrocarbonate, which reacts with His sidechains.

Evidence that the scrapie agent is a protein: scrapie agent is unaffected by treatment with hydroxylamine, which reacts with cytosine residues.

Evidence that the scrapie agent is a protein: hydroxylamine rescues diethylpyrocarbonate-inactivated scrapie reagent.

Prion protein conformations: NMR structure of human prion protein (PrPC). Note the disordered N-terminal tail residues (dots). PrP may be a cell-surface signal receptor.

Prion protein conformations: a plausible model for the structure of PrPSc (very insoluble)

Figure 9-36 Molecular formula for iron-protoporphyrin IX (heme).

Figure 9-37 Primary structures of some representative c-type cytochromes.

Figure 9-38 Three-dimensional structures of the c-type cytochromes whose primary structures are displayed in Fig. 9-37.

Figure 9-39 The two-structurally similar domains of rhodanese.

Author: Anthony S. Serianni

Download presentation source