Interactions of Protein with Proteins:
H.I. Chen and M. Sudol, Identification and Characterization of Protein Ligands to the WW Domain by Western Ligand Blotting.
X. Cheng, S.A. Hofstadler, J.E. Bruce, A.C. Harms, R. Chen, T.C. Terwilliger, R.D. Smith, and P.N. Goudreau, Electrospray Ionization with High Performance Fourier Transform Ion Cyclotron Resonance Mass Spectrometry for the Study of Noncovalent Biomolecular Complexes.
J.Wen, T. Arakawa, J. Talvenheimo, A.A. Welcher, T. Horan, Y. Kita, J. Tseng, M. Nicolson, and J.S. Philo, A Light Scattering/Size Exclusion Chromatography Method for Studying the Stoichiometry of a Protein-Protein Complex.
J. Li and R.M. Weis, Measurements of Protein-Protein Interaction by Isothermal Titration Calorimetry with Applications to the Bacterial Chemotaxis Systems.
Z. Wu, K.W. Johnson, B. Goldstein, T.M. Laue, and T.L. Ciardelli, Solution Assembly of Cytokine Receptor Ectodomain Complexes.
K.P.Williams, D.M. Evans, S. Rosenberg, and S.Jindal, Use of a Peptide Library to Characterize Differential Peptide Binding Specificities of Bacterial and Mammalian Hsp70.
E. Perez-Paya, R.A. Houghten, and S.E. Blondelle, The Design of Self-Assembling Peptide Complexes Using Conformationally Defined Libraries.
Interactions of Proteins with Ligands:
K. Hollfelder, F. Wang, and Y.-C.E. Pan, "Fishing Out" Ligand Binding Proteins from Protein Mixtures by a Two-Dimensional Gel ElectrophoresisSystem Utilizing Native PAGE Followed by SDS-PAGE.
W. Moore and J.D. Lambris, Mass Spectrometric Analyses of the Activation Products of the Third Component of Complement.
D. Stanojevic and G.L. Verdine, Site-Specific Reversible Conjugation: A Novel Concept in Peptide-DNA Interactions.
J.E. Scheffler, S.E. Kiefer, K. Prinzo, and E. Bekesi, Scintillation Proximity Assay to Measure the Binding of Ras-GTP to the Ras-Binding Domain of c-Raf-1.
Behavior of Proteins at Surfaces: P.L.Derby, K.H. Aoki, V. Katta, M.F. Rohde, Asparagine Rearrangements in Two Isoforms of Erythropoietin Receptor.
M. Monette, H. Gratkowski, S.J. Opella, J. Greenwood, A.E. Willis, and R.N. Perham, Initial Characterization of a Peptide Epitope Displayed on the Surface of fd Bacteriophage by Solution and Solid-State NMR Spectroscopy.
J.D. Baleja, S.J. Freedman, B.C. Furie, and B. Furie, NMR Structures for the Membrane Binding Gla Domain of Blood Coagulation Factor IX.
L. Niu, C. Grewer, and G.P. Hess, Chemical Kinetic Investigations of Neurotransmitter Receptors on a Cell Surface in the gh us Time Region.
S. Sonar, C.-P. Lee, C.F.C. Ludlam, X.-M. Liu, M. Coleman, T. Marti, U.L. RajBhandary, and K.J. Rothschild, Site-Directed IsotopeLabeling of Membrane Proteins: A New Tool for Spectroscopists.
Modifications to Proteins in Vivo:
J. Hofsteenge, A. Loffler, D.R. Muller, W.J. Richter, T. de Beer, and F.G. Vliegenthart, Protein C-Glycosylation.
C.A. Settineri, Y.D. Chen, K. Jiang, S.Z. Zhang, A.L. Burlingame, Characterization of the N- and O- Linked Oligosaccharides from Glucoamylase E4 from Monascus rubiginosus using Electrospray Mass Spectrometry and Glycosidase Digestion.
F. Barry, R. Maciewicz, and M.T. Bayliss, Post-Translational Changes in the Protein Core of the Proteoglycan, Aggrecan, in Human Articular Cartilage.
K.F. Geoghegan, C.A. Strick, S. Guhan, M.E. Kelly, A.J. Lanzetti, K.E. Cole, S.B. Jones, D.A. Cole, K.J. Rosnack,R.M. Guinn, A.R. Goulet, T.-P. I, L.W. Blocker, D.W. Melvin, and J.A. Funes, In Vivo Dipeptidylation of the Amino Terminus of Recombinant Glucagon-like Peptide-1(7-37) Produced in the Yeast Yarrowia lipolytica as a Fusion Protein.
F. Ross, T.Zamborelli, A.C. Herman, C.-H. Yeh, N.I. Tedeschi, and E.S. Luedke, Detection of Acetylated Lysine Residues Using Sequencing by Edman Degradation and Mass Spectrometry.
I. Lascu, S. Morera, M. Chiadmi, J. Cherfils, J. Janin, and M. Veron, Mechanism of the Nucleoside Diphosphate Kinase Reaction: X-Ray Structure of the Phosphohistidine Intermediate.
Manipulation of Sulfur in Proteins:
R. Singh, Selenol-Catalyzed Reduction of Disulfide Bonds in Peptides and Proteins.
D.C. Brune, D.G.Hartzfeld, and T.W. Johnson, Cysteine Modification with Acrylonitrile for Amino Acid Analysis and Protein Sequencing.
N.D. Denslow and H.P. Nguyen, Specific Cleavage of Blotted Proteins at Cysteine Residues after Cyanylation: Analysis of Products by Maldi-Tof.
J.H. Robinson, M.D. McGinley, J.C. Leidli, D.E. Lyons, C.-H. Lin, B. Karan-Tamir, M.M. Zukowski, and M.F. Rohde, Disulfide Characterization of CD31 (PECAM).
R.H. Angeletti, L. Bibbs, L.F. Bonewald, G.B. Fields, J.S. McMurray, W.T.Moore, and John T. Stults, Formation of a Disulfide Bond in an Octreotide-Like Peptide: A Multicenter Study.
F.J. Shen, M.Y. Kwong, R.G. Keck, and R.J. Harris, The Application of tert-Butylhydroperoxide Oxidation to Study Sites of Potential Methionine Oxidation in a Recombinant Antibody.
Methods Used in Primary Structural Analysis:
M. Kirchner, J. Fernandez, Q.A. Shakey, F. Gharahdaghi, and S.M. Mische, Enzymatic Digestion of PVDF-Bound Proteins: A Survey of Sixteen Nonionic Detergents.
M.R. Schlittler, B.A. Foy, J.J. Triska, B.N. Violand, and G.L. Bachman, Development and Optimization of a SE-HPLC Method for Proteins using Organic Mobile Phases.
R.R. Ogorzalek Loo, C. Mitchell, T. Stevenson, J.A. Loo, and P.C. Andrews, Interfacing Polyacrylamide Gel Electrophoresis with Mass Spectrometry.
A.G. Craig, S.W. Sutton, J. Vaughan, and W.H. Fischer, Immunoprecipitation as a Means of Purification for Analysis with Mass Spectrometry.
A.M. Mahrenholz, N.D. Denslow, T.T. Andersen, K.M. Schegg, K. Mann, S.A. Cohen, J.W. Fox, and K.U. Yuksel, Amino Acid Analysis--Recovery from PVDF Membranes: ABRF-95AAA Collaborative Trial.
D.J. Strydom, Amino Acid Analysis Using Various Carbamate Reagents for PreColumn Derivatization.
W.J. Henzel, J.T. Stults, S.C. Wong, A. Namenuk, J. Yashio, and C. Watanabe, Analysis of Mixture Sequences Derived from Edman Degradation Data.
K.S. DeJongh, J. Fernandez, J.E. Gambee, G.A. Grant, B. Merrill, K.L. Stone, and J. Rush, Design and Analysis of ABRF-95SEQ, a Recombinant Protein with Sequence Heterogeneity.
Three Dimensional Protein Structure:
Q. Han and S.-X. Lin, A Technique of Protein Addition for Repeated Enlargement of Protein Crystals in Solution.
J.K.M. Rao, M. Gribskov, J. Lubkowski, M. Miller, A.L. Swain, and A. Wlodawer, A Comparison of the Crystal Structures of Bacterial L-Asparaginases.
G. Bujacz, M. Jaskolski, J. Alexandratos, A, Wlodawer, G. Merkel, R.A. Katz, and A.M. Skalka, Crystal Structure of the Catalytic Domain of Avian Sarcoma Virus Integrase.
E.A. Komives, M.J. Hunter, D.P. Meininger, L.R. White, and C.E. White, Structure/Function of the Fourth and Fifth EGF Domains of Thrombomodulin.
P.J. Neame and R.E. Boynton, The Structure of a C-type Lectin Isolated from Bovine Cartilage.
D.N. Woolfson and T. Alber, Sequence Determinants of Oligomer Selection in Coiled Coils.
C.-J. Tsai, S.L. Lin, H.J. Wolfson, and R. Nussinov, Techniques for Searching for Structural Similarities Between Protein Cores, Protein Surfaces, and Between Protein-Protein Interfaces.
Folding and Stability of Proteins:
K.E. Prehoda, S.N. Loh, and J.L. Markley, Modeling Volume Changes in Proteins Using Partial Molar Volumes of Model Compounds.
C.V. Gegg, K.E. Bowers, and C.R. Matthews, A General Approach for the Design and Isolation of Protein Fragments: The Molecular Dissection of Dihydrofolate Reductase.
J.M. Matthews, L.D. Ward, J.-G. Zhang, and R.J. Simpson, The Association of Unfolding Intermediates during the Equilibrium Unfolding of Recombinant Murine Interleukin-6.
C.R. Johnson and E. Freire, Structural Stability of Small Oligomeric Proteins.
S.L. Kazmirski, D.O.V. Alonso, F.E. Cohen, S.B. Prusiner, and V. Daggett, The Conformational Consequences of Mutations to the H1 Helix of the Prion Protein Explored by Molecular Dynamics Simulations.
Methods and Uses for Synthetic Proteins:
R.J. Simpson, J.-G. Zhang, D.S. Dorow, G.E. Reid, R.L. Moritz,and G.-F. Tu, Identification of Truncated E. coli-Expressed Proteins with a Novel C-Terminal 10Sa RNA Decapeptide Extension.
C.J.A. Wallace, A.C. Woods, and J.G. Guillemette, Simplifying the Fragment Condensation Semisynthesis of Protein Analogs.
C.J.A. Wallace and I. Clark-Lewis, Using Semisynthesis to Insert Heavy-Atom Labels in Functional Proteins.
G. Barany, C.M. Gross, M. Ferrer, E. Barbar, H. Pan, and C. Woodward, Optimized Methods for Chemical Synthesis of Bovine Pancreatic Trypsin Inhibitor (BPTI) Analogues.
S.A. Kates, E. Diekmann, A. El-Faham, L.W. Herman, D. Ionescu, B.F. McGuiness, S.A. Triolo, F. Albericio, L.A. Carpino, On the Use of Novel Coupling Reagents for Solid-Phase Peptide Synthesis. Subject Index.
Techniques in Protein Chemistry VII, a valuable bench-top reference tool for protein chemists, features the most up-to-date advances in protein methodologies.
@introbul:Key Features @bul:* Protein sequencing and amino acid analysis
- Mass spectral analysis of peptides and proteins
- Posttranslational processing
- High-sensitivity protein and peptide separations
- Protein folding and NMR
- Functional domain analysis
- Protein design and engineering
Biochemists, molecular biologists, biophysicists, and biotechnologists in academia and industry. Also of interest to graduate students in these disciplines.
- No. of pages:
- © Academic Press 1996
- 16th May 1996
- Academic Press
- Paperback ISBN:
@qu:"The mainly sharp scientific focus of this set of snapshots is a credit to both the contributors and the editorial team." @source:--BIOTECHNOLOGY AND APPLIED BIOCHEMISTRY
Osiris Therapeutics, Inc., Baltimore, Maryland, U.S.A.