Journal Issue - Volume 6 Issue 1 (January 1997)
Protein science in 1996
- Hans Neurath
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060101 (p 1-4)
Friends and relations of the cystatin superfamily—new members and their evolution
- W.M. Brown, K.M. Dziegielewska
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060102 (p 5-12)
Abstract The cystatin “superfamily” encompasses proteins that contain multiple cystatin‐like sequences. Some of the members are active cysteine protease inhibitors, while others have lost or perhaps never aquired this inhibitory activity. In recent years, several new members of the superfamily have been characterized, including proteins from insects and plants. Based on partial amino acid homology, new members, such as the invariant...
Structure of the vibrio harveyi : X‐ray analysis of a kinetic protein folding trap
- James B. Thoden, Hazel M. Holden, Andrew J. Fisher, James F. Sinclair, Gary Wesenberg, Thomas O. Baldwin, Ivan Rayment
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060103 (p 13-23)
Abstract Luciferase, as isolated from Vibrio harveyi, is an aβ heterodimer. When allowed to fold in the absence of the α subunit, either in vitro or in vivo, the β subunit of the enzyme will form a kinetically stable homodimer that does not unfold even after prolonged incubation in 5 M urea at pH 7.0 and 18 °C. This form of the β subunit, arising via kinetic partitioning on the folding pathway, appears to constitute a kinetically ...
Hydrophobic folding units derived from dissimilar monomer structures and their interactions
- Chung‐Jung Tsai, Ruth Nussinov
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060104 (p 24-42)
Abstract We have designed an automated procedure to cut a protein into compact hydrophobic folding units. The hydrophobic units are large enough to contain tertiary non‐local interactions, reflecting potential nucleation sites during protein folding. The quality of a hydrophobic folding unit is evaluated by four criteria. The first two correspond to visual characterization of a structural domain, namely, compactness and extent of...
Probing the active site of α‐class rat liver glutathione S‐transferases using affinity labeling by monobromobimane
- Longqin Hu, Barbara L. Borleske, Roberta F. Colman
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060105 (p 43-52)
Abstract Monobromobimane (mBBr) is a substrate of both μ‐ and α‐class rat liver glutathione S‐transferases, with Km values of 0.63 μM and 4.9 μM for the μ‐class isozymes 3–3 and 4–4, respectively, and 26 μM for the α‐class isozymes 1–1 and 2–2. In the absence of substrate glutathione, mBBr acts as an affinity label of the 1–1 as well as μ‐class isozymes, but not of the α‐class 2–2 isozyme. Incubation of rat liver isozyme 1–1 with mBBr at pH 7.5...
Studies of protein‐protein interfaces: A statistical analysis of the hydrophobic effect
- Chung‐Jung Tsai, Shuo Liang Lin, Haim J. Wolfson, Ruth Nussinov
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060106 (p 53-64)
Abstract Data sets of 362 structurally nonredundant protein‐protein interfaces and of 57 symmetry‐related oligomeric interfaces have been used to explore whether the hydrophobic effect that guides protein folding is also the main driving force for protein‐protein associations. The buried nonpolar surface area has been used to measure the hydrophobic effect. Our analysis indicates that, although the hydrophobic effect plays a...
Solution structure of a unique C5a semi‐synthetic antagonist: Implications in receptor binding
- Xiaolu Zhang, William Boyar, Nina C. Gonnella, Nicholas Galakatos
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060107 (p 65-72)
Abstract The tertiary structure of a unique C5a receptor antagonist was determined by two‐dimensional NMR spectroscopy. The core domain of this 8‐kDa antagonist exists as an antiparallel helical bundle, similar to recombinant human (rh)‐C5a. However, unlike C5a, the antagonist's C terminus was found to be conformationally restricted along a groove between helices one and four in the core domain. This conformational restriction...
Molecular modeling of the structures of human and rat pancreatic cholesterol esterases
- Shawn R. Feaster, Daniel M. Quinn, Bobby L. Barnett
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060108 (p 73-79)
Abstract Structural models have been generated for rat and human cholesterol esterases by molecular modeling. For rat cholesterol esterase, three separate models were generated according to the following procedure: (1) the cholesterol esterase sequence was aligned with those of three template enzymes: Torpedo californica acetylcholinesterase, Geotrichum candidum lipase and Candida rugosa lipase; (2) the X‐ray structure coordinates of the three...
The crystal structure of the designed trimeric coiled coil coil‐V d : Implications for engineering crystals and supramolecular assemblies
- Nancy L. Ogihara, Manfred S. Weiss, David Eisenberg, William F. Degrado
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060109 (p 80-88)
Abstract The three‐dimensional structure of the 29‐residue designed coiled coil having the amino acid sequence acetyl‐E VEALEKK VAALESK VQALEKK VEALEHG‐amide has been determined and refined to a crystallographic R‐factor of 21.4% for all data from 10‐Å to 2.1‐Å resolution. This molecule is called coil‐VaLd because it contains valine in the a heptad positions and leucine in the d heptad positions. In the trigonal crystal, three molecules, related by a...
Importance of the release of strand 1C to the polymerization mechanism of inhibitory serpins
- Wun‐Shaing W. Chang, James Whisstock, Paul C.R. Hopkins, Arthur M. Lesk, Robin W. Carrell, Mark R. Wardell
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060110 (p 89-98)
Abstract Serpin polymerization is the underlying cause of several diseases, including thromboembolism, emphysema, liver cirrhosis, and angioedema. Understanding the structure of the polymers and the mechanism of polymerization is necessary to support rational design of therapeutic agents. Here we show that polymerization of antithrombin is sensitive to the addition of synthetic peptides that interact with the structure. A 12‐mer...
Conformation of P22 tailspike folding and aggregation intermediates probed by monoclonal antibodies
- Margaret A. Speed, Timothy Morshead, Daniel I.C. Wang, Jonathan King
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060111 (p 99-108)
Abstract The partitioning of partially folded polypeptide chains between correctly folded native states and off‐pathway inclusion bodies is a critical reaction in biotechnology. Multimeric partially folded intermediates, representing early stages of the aggregation pathway for the P22 tailspike protein, have been trapped in the cold and isolated by nondenaturing polyacrylamide gel electrophoresis (PAGE) (Speed MA, Wang DIC, King J....
Recombinant hirustasin: Production in yeast, crystallization, and interaction with serine proteases
- Stefania Di Marco, Gabriele Fendrich, Rene Knecht, Andre Strauss, Gabriele Pohlig, Jutta Heim, John P. Priestle, Markus G. Grütter, Christian P. Sommerhoff
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060112 (p 109-118)
Abstract A synthetic gene coding for the 55‐amino acid protein hirustasin, a novel tissue kallikrein inhibitor from the leech Hirudo medicinalis, was generated by polymerase chain reaction using overlapping oligonucleotides, fused to the yeast α‐factor leader sequence and expressed in Saccharomyces cerevisiae. Recombinant hirustasin was secreted mainly as incompletely processed fusion protein, but could be processed in vitro using a soluble variant of the...
Crystal structure of the reduced Schiff‐base intermediate complex of transaldolase B from escherichia coli : Mechanistic implications for class I aldolases
- Jia Jia, Ylva Lindqvist, Gunter Schneider, Ulrich Schörken, Georg A. Sprenger
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060113 (p 119-124)
Abstract Transaldolase catalyzes transfer of a dihydroxyacetone moiety from a ketose donor to an aldose acceptor. During catalysis, a Schiff‐base intermediate between dihydroxyacetone and the ϵ‐amino group of a lysine residue at the active site of the enzyme is formed. This Schiff‐base intermediate has been trapped by reduction with potassium borohydride, and the crystal structure of this complex has been determined at 2.2 Å...
Identification of the cap binding domain of human recombinant eukaryotic protein synthesis initiation factor 4E using a photoaffinity analogue
- Diana E. Friedland, Dixie J. Goss, Michael T. Shoemaker, Yiping Xie, Yuhuan Wang, Curt H. Hagedorn
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060114 (p 125-131)
Abstract Binding of eIF‐4E to the 5′ m7G cap structure of eukaryotic mRNA signals the initiation of protein synthesis. In order to investigate the moiecular basis for this recognition, photoaffinity labeling with [γ‐32P]8‐N3GTP was used in binding site studies of human recombinant cap binding protein reIF‐4E. Competitive inhibition of this cap analogue by m7GTP and capped mRNA indicated probe specificity for interaction at the protein binding site....
Nonenzymatic anticoagulant activity of the mutant serine protease Ser360Ala‐activated protein C mediated by factor Va
- Andrew J. Gale, Xi Sun, Mary J. Heeb, John H. Griffin
- Published in Wiley Interscience on Dec 31, 2008
- DOI: 10.1002/pro.5560060115 (p 132-140)
Abstract The human plasma serine protease, activated protein C (APC), primarily exerts its anticoagulant function by proteolytic inactivation of the blood coagulation cofactors Va and Villa. A recombinant active site Ser 360 to Ala mutation of protein C was prepared, and the mutant protein was expressed in human 293 kidney cells and purified. The activation peptide of the mutant protein C zymogen was cleaved by a snake venom...




