Journal Issue - Volume 10 Issue 11 (November 2001)
Electrostatic contributions to protein–protein interactions: Fast energetic filters for docking and their physical basis
- Raquel Norel, Felix Sheinerman, Donald Petrey, Barry Honig
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.12901 (p 2147-2161)
Abstract The methods of continuum electrostatics are used to calculate the binding free energies of a set of protein–protein complexes including experimentally determined structures as well as other orientations generated by a fast docking algorithm. In the native structures, charged groups that are deeply buried were often found to favor complex formation (relative to isosteric nonpolar groups), whereas in nonnative complexes...
Reconstitution of a native‐like SH2 domain from disordered peptide fragments examined by multidimensional heteronuclear NMR
- Deanna Dahlke Ojennus, Mark R. Fleissner, Deborah S. Wuttke
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.18701 (p 2162-2175)
Abstract The N‐terminal SH2 domain from the p85α subunit of phosphatidylinositol 3′ kinase is cleaved specifically into 9‐ and 5‐kD fragments by limited proteolytic digestion with trypsin. The noncovalent SH2 domain complex and its constituent tryptic peptides have been investigated using high‐resolution heteronuclear magnetic resonance (NMR). These studies have established the viability of the SH2 domain as a fragment...
Influence of a sulfhydryl cross‐link across the allosteric‐site interface of E. coli phosphofructokinase
- Jason L. Johnson, Mauricio D. Lasagna, Gregory D. Reinhart
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.02401 (p 2186-2194)
Abstract To assess the role of quaternary stability on the properties of Escherichia coli phosphofructokinase (PFK), a disulfide bond has been introduced across the subunit interface containing the allosteric binding sites in E. coli phosphofructokinase by changing N288 to cysteine. N288 is located in close proximity to the equivalent residue on an adjacent subunit. Although SDS‐PAGE of oxidized N288C indicates monomeric protein, blocking the...
Solvent‐induced collapse of α‐synuclein and acid‐denatured cytochrome c
- Artemiza S. Morar, Alina Olteanu, Gregory B. Young, Gary J. Pielak
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.24301 (p 2195-2199)
Abstract The effects of solution conditions on protein collapse were studied by measuring the hydrodynamic radii of two unfolded proteins, α‐synuclein and acid‐denatured ferricytochrome c, in dilute solution and in 1 M glucose. The radius of α‐synuclein in dilute solution is less than that predicted for a highly denatured state, and adding 1 M glucose causes further collapse. Circular dichroic data show that α‐synuclein lacks organized ...
Structural features underlying selective inhibition of protein kinase CK2 by ATP site‐directed tetrabromo‐2‐benzotriazole
- Roberto Battistutta, Erika De Moliner, Stefania Sarno, Giuseppe Zanotti, Lorenzo A. Pinna
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.19601 (p 2200-2206)
Abstract Two novel crystal structures of Zea mays protein kinase CK2α catalytic subunit, one in complex with the specific inhibitor 4,5,6,7‐tetrabromobenzotriazole (TBB) and another in the apo‐form, were solved at 2.2 Å resolution. These structures were compared with those of the enzyme in presence of ATP and GTP (the natural cosubstrates) and the inhibitor emodin. Interaction of TBB with the active site of CK2α is mainly due to van...
Characterization of ostrich ( Struthio camelus ) β‐microseminoprotein (MSP): Ideication of homologous sequences in EST databases and analysis of their evolution during speciation
- Claude Lazure, Michéle Villemure, Dany Gauthier, Ryno J. Naudé, Majambu Mbikay
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.06501 (p 2207-2218)
Abstract β‐Microseminoprotein, alternatively called prostatic secretory protein of 94 amino acids, is a hydrophilic, unglycosylated, small protein rich in conserved half‐cystine residues. Originally found in human seminal plasma and prostatic fluids, its presence was later shown in numerous secretions and its homologs were described in many vertebrate species. These studies showed that this protein had rapidly evolved, but they...
Peptide‐plane flipping in proteins
- Steven Hayward
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.23101 (p 2219-2227)
Abstract A peptide‐plane flip is a large‐scale rotation of the peptide plane that takes the ϕ,ψ angles at residues i and i + 1 to different structural regions in the Ramachandran plot with a comparatively small effect on the relative orientation of their side chains. This phenomenon, which is expected to play an important role during the early stages of protein folding, has been investigated using 76 proteins for which two high‐resolution X‐ray...
Key interactions in the immunoglobulin‐like structure of apo‐neocarzinostatin: Evidence from nuclear magnetic resonance relaxation data and molecular dynamics simulations
- Nadia Izadi‐Pruneyre, Éric Quiniou, Yves Blouquit, Javier Perez, Philippe Minard, Michel Desmadril, Joël Mispelter, Élisabeth Adjadj
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.12201 (p 2228-2240)
Abstract The three‐dimensional structure of apo‐neocarzinostatin (apo‐NCS, MW: ca.11000, antitumoral chromophore carrier protein) is based on a seven‐stranded antiparallel β‐sandwich, very similar to the immunoglobulin folding domain. We investigated the backbone dynamics of apo‐NCS by 13C‐NMR relaxation measurements and molecular dynamics simulation. Model‐free parameters determined from the experimental data are compared with a...
Structure of the transmembrane region of the M2 protein H + channel
- Junfeng Wang, Sanguk Kim, Frank Kovacs, Timothy A. Cross
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.17901 (p 2241-2250)
Abstract The transmembrane domain of the M2 protein from influenza A virus forms a nearly uniform and ideal helix in a liquid crystalline bilayer environment. The exposure of the hydrophilic backbone structure is minimized through uniform hydrogen bond geometry imposed by the low dielectric lipid environment. A high‐resolution structure of the monomer backbone and a detailed description of its orientation with respect to the bilayer...
Ideication of disulfide‐linked peptides by isotope profiles produced by peptic digestion of proteins in 50% 18 O water
- Tristan P. Wallis, James J. Pitt, Jeffrey J. Gorman
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.15401 (p 2251-2271)
Abstract Determination of the disulfide‐bond arrangement of a protein by characterization of disulfide‐linked peptides in proteolytic digests may be complicated by resistance of the protein to specific proteases, disulfide interchange, and/or production of extremely complex mixtures by less specific proteolysis. In this study, mass spectrometry has been used to show that incorporation of 18O into peptides during peptic digestion of...
E. coli methionine sulfoxide reductase with a truncated N terminus or C terminus, or both, retains the ability to reduce methionine sulfoxide
- Sandrine Boschi‐Muller, Saïd Azza, Guy Branlant
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.10701 (p 2272-2279)
Abstract The monomeric peptide methionine sulfoxide reductase (MsrA) catalyzes the irreversible thioredoxin‐dependent reduction of methionine sulfoxide. The crystal structure of MsrAs from Escherichia coli and Bos taurus can be described as a central core of about 140 amino acids that contains the active site. The core is wrapped by two long N‐ and C‐terminal extended chains. The catalytic mechanism of the E. coli enzyme has been recently...
Proteins of circularly permuted sequence present within the same organism: The major serine proteinase inhibitor from Capsicum annuum seeds
- Nikolinka Antcheva, Alessandro Pintar, András Patthy, András Simoncsits, Endre Barta, Bojidar Tchorbanov, Sándor Pongor
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.21701 (p 2280-2290)
Abstract The major serine proteinase inhibitor from bell pepper (Capsicum annuum, paprika) seeds was isolated, characterized, and sequenced, and its disulfide bond topology was determined. PSI‐1.2 is a 52‐amino‐acid‐long, cysteine‐rich polypeptide that inhibits both trypsin (Ki = 4.6 × 10−9 M) and chymotrypsin (Ki = 1.1 × 10−8 M) and is a circularly permuted member of the potato type II inhibitor family. Mature proteins of this family are produced ...
Implications of secondary structure prediction and amino acid sequence comparison of class I and class II phosphoribosyl diphosphate synthases on catalysis, regulation, and quaternary structure
- Britta N. Krath, Bjarne Hove‐Jensen
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.11801 (p 2317-2324)
Abstract Spinach 5‐phospho‐d‐ribosyl α‐1‐diphosphate (PRPP) synthase isozyme 4 was synthesized in Escherichia coli and purified to near homogeneity. The activity of the enzyme is independent of Pi; it is inhibited by ADP in a competitive manner, indicating a lack of an allosteric site; and it accepts ATP, dATP, GTP, CTP, and UTP as diphosphoryl donors. All of these properties are characteristic for class II PRPP synthases. Km values for ATP and ribose...
Salt‐dependent monomer–dimer equilibrium of bovine β‐lactoglobulin at pH 3
- Kazumasa Sakurai, Motohisa Oobatake, Yuji Goto
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.17001 (p 2325-2335)
Abstract Although bovine β‐lactoglobulin assumes a monomeric native structure at pH 3 in the absence of salt, the addition of salts stabilizes the dimer. Thermodynamics of the monomer–dimer equilibrium dependent on the salt concentration were studied by sedimentation equilibrium. The addition of NaCl, KCl, or guanidine hydrochloride below 1 M stabilized the dimer in a similar manner. On the other hand, NaClO4 was more effective than...
Structural comparison of recombinant human macrophage colony stimulating factor β and a partially reduced derivative using hydrogen deuterium exchange and electrospray ionization mass spectrometry
- Y. Heidi Zhang, Xuguang Yan, Claudia S. Maier, Michael I. Schimerlik, Max L. Deinzer
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1110/ps.16701 (p 2336-2345)
Abstract Hydrogen deuterium exchange, monitored by electrospray ionization mass spectrometry, has been employed to characterize structural features of a derivative of recombinant human macrophage colony stimulating factor beta (rhm‐CSFβ) in which two of the nine disulfide bridges (Cys157/Cys159–Cys′157/Cys′159) were selectively reduced and alkylated. Removal of these two disulfide bridges did not affect the biological activity of...




