Subcellular location of PKCalphaII-GFP (green) in Green Monkey COS-7 cells using laser scanning confocal microscopy two days after transfection. The actin cytoskeleton is stained with Texas Red-phalloidin and the endoplasmic reticulum (purple) identified with an antibody to calreticulin.   By Lorene Langeberg, Scott Lab Manager at the Howard Hughes Medical Institute, Portland, OR.
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The Protein and Peptide Science Group

The Protein and Peptide Science Group has set up an email discussion group. Click on the link to sign up for discussions and queries on topics related to protein and peptide science.

Prizewinners for the Young Investigators Awards
Forthcoming Events
Committee Members
Past Meetings
Links

The Protein and Peptide Science Group The Group is both a special interest group of the Biochemical Society and a subject group of the Perkin division of the Royal Society of Chemistry. With a historic basis in peptide chemistry, the interests of the Group has enlarged in recent years to cover protein structure determination, structure prediction, molecular modelling and dynamics, protein separation and characterisation, protein biosynthesis, protein expression, combinatorial synthesis, protein design and engineering, drug-protein interactions and protein structure-function. The Group is also committed to paving the way forward into functional genomics and bioinformatics. The Group's mission is to maintain the logical progression of molecular science through chemistry into biochemistry, biology and medicine. Thus, it has an interdisciplinary approach, representing the protein science interests of chemists, molecular biologists, structural biologists, peptide chemists and biologists and members of the biotechnology, food and pharmaceutical industries.


Forthcoming Events:

Harden Conference

September 10th-12th 2003
St John's College, Oxford
More details on http://www.biochemsoc.org/meetings/harden.htm
Talks in the conference will include:

The biochemistry and cell biology of metalloproteinase activation
G. Murphy

Proteosomes
A.J. Rivett

Optimisation of the P'-region of Peptide Inhibitors of Hepatitis C virus NS3 Protease
A. Pessi

Synthesis of Proteinase Inhibitors
D. Fairlie

Receptor mediated regulation of plasminogen activator function - a paradigm for proteolytic remodelling of the extracellular matrix.
V. Ellis

Natural and Synthetic Tryptase Inhibitors as Diagnostic Tools and for Therapeutic Approaches
C. Sommerhoff

Adams Proteinases
A.J. Turner

Scripps phage display library for protease screening
Ed Madison

Neuropeptide processing
D. Coates, Leeds UK

Genetics of haemophilia
Lillicrap D, Canada

Cloning and gene family of kallikreins in cancer
Diamandis

Aposome for caspase activation
Cain K, Leicester UK



Past Meetings:

Protein-Protein Interactions in London

This meeting was organised jointly by Simon Edwards of the Chemical Biology Forum and Brian Austen of the PPSG group at the convenient location of the Scientific Society Lecture Theatre in Saville Row, London, on Tuesday May 7th, 2002. It was attended by about 70 registrants from industry and academia, with representatives from funding bodies.

Sequencing genomes of a number of species, has identified many thousands of open reading frames, which represent many millions of potential protein-protein contacts. It is now a priority in research to establish the identity of the actual functional protein-protein interactions that take place in cells. Protein interactions involved in disease processes may potentially be targeted by pharmaceutical chemists to develop novel drugs.

The meeting covered a variety of approaches for identifying functional interactions between proteins. Sarah Teichmann (LMB-MRC Cambridge) described how bioinformatics is used to identify partners of multi-domain proteins, stable protein complexes or transiently interacting components. Classification of interacting domains among families and superfamilies of proteins provide useful ways of predicting interactions. Biosensors which detect protein-protein-interactions by surface plasmon resonance or evanescent wave-resonance have been used to purify protein complexes containing the adenomatous polyposis coli tumor suppressor protein (Bruce Catimel, Ludwig Institute, Melbourne, Australia) by virtue of specific interactions with an immobilised peptide. A firm basis for establishing the kinetics of interactions of proteins at biosensor surfaces was described by Robin Leatherborrow (Imperial College, London). Migyue He (Discerna Ltd, Babraham, Cambridge) described methods of preparing protein arrays directly on DNA array chips, using in vitro transcription-translation. By removing termination codons, the polypeptides are conveniently analysed still attached to ribosomes. Steve Cleverley (Ciphergen, Camberley, Surrey) described surface-enhanced protein arrays consisting of chemically and biologically-active surfaces on Maldi plates; applications include capture and mass spectrometry identification of crk SH2-binding domain proteins from whole cell lysates.

The meeting finished with a detailed analysis of interactions functioning among the protein components in the Raf-MEK-ERK pathway, using classical techniques of immunoprecipitation and kinase activity (Walter Kolch, Glasgow). The concluding discussion expressed the need for increased collaborations in chemical biology to develop methods for establishing topography of protein complexes in whole cells, and achieving automation in the preparation and use of protein-array chips

Heriot Watt Meeting

Amyloidogenic Proteins involved in neurodegeneration, and therapeutic implications
8-9 April 2002

Speakers and Organisers at the Colloquium on "Amyloidogenic Proteins and their roles in Neurodegenerative Disease" at Heriot-Watt.



L. Serpell, B. Austen, B. Irvine, B. Caughey, D. Beher, E. Zerovnik, S. Cleverley, L. Masino, A. Doig, T. Wisniewski.

Monday 8th April 2002  
9.00-9.40Pathology of amyloid diseases
Nigel Cairns, University of London
9.40-10.20Protein folding and aggregation
Chris Dobson, Cambridge University
10.20-11.00Three-dimensional structure of amyloid fibrils
Louise Serpell, Molecular Biology Laboratory, Cambridge
14.00-14.40 Beta-Secretase inhibition
Jordan Tang, Oklahoma Medical Research Foundation
14.40-15.20Gamma-Secretase inhibition
Mark Shearman, Merck Sharp & Dohme
15.20-16.00The prospect of a vaccine for Alzheimer's: recent behavioural studies in mouse models of the disease
Richard Morris, Edinburgh
16.00-16.40Cholesterol and Alzheimer's Disease
Benjamin Wolozin, Loyola University
16.40-17.30Poster Sessions


Tuesday 9th April 2002  
9.00-9.40The role of oligomeric forms of Ab in Alzheimer's disease.
Dominic Walsh, Harvard University, Boston
9.40-10.20The oligomerisation and toxicity of the ABri and ADan, products of the BRI gene
Brian Austen, St Georges Hospital, University of London
10.20-11.00Oligomerisation and toxicity of alpha-synuclein
Omar El-Agnaf, University of Lancaster
14.00-14.40Prion interconversions
Byron Caughey, NIAID, USA
14.40-15.20Anti-prion peptides
Claudio Soto, , Serono Pharmaceutical Research Institute, Geneva
15.20-16.00The role of poly-glutamine sequences in Huntington's disease
Stephen Davies, University of London
16.00-16.40Quantitative detection and identification of amyloid beta peptides directly from crude biological samples using the SELDI ProteinChip® Biology System
Steve Cleverley, Ciphergen
16.40 - 18.00Poster Sessions



Membrane Active Peptides

Colloquium organised at the University of Bristol in April 2001
Organisers: Brian Austen (London), Parvez Haris (De Montfort)
Wednesday 11 April 2001
De novo design, synthesis and characterization of membrane active Peptides
Jim D. Lear (Philadelphia, USA)

Simulations studies of peptide/bilayer interactions
Mark Sansom (Oxford, UK)

Peptaibols: models for ion channels
Bonnie Wallace (London, UK)

Structural implications for the transformation of the Bacillus thuringiensis delta-endotoxins from water soluble to membrane inserted form
Jade Li (Cambridge, UK)

Developing structural models of K+ channels and their relatives based on analyses of distantly related sequences
H. Robert Guy (Bethesda, USA)

Insertion of transmembrane helices into the ER membrane
Gunnar von Heijne (Stockholm, Sweden)

Self-assembly of membrane protein monolayers on gold
Jeremy Lakey (Newcastle, UK)

Application of electron spin resonance for investigating peptide-lipid interactions
Derek Marsh (Gottingen, Germany)

Conformational analysis of synthetic potassium ion-channel peptides
Parvez I. Haris (Leicester, UK)
Thursday 12 April 2001
Binding of a signal sequence peptide: role of bilayer properties
Tom McIntosh (Duke, USA)

Why and how are peptide-lipid interactions utilized for self-defence?
Katsumi Matsuzaki (Kyoto, Japan)

Membrane properties and amyloid fibril formation of lung surfactant protein C
Jan Johansson (Stockholm, Sweden)

Connexin mimetic peptides; specific inhibitors of gap junctional communication
W. Howard Evans (Cardiff, Wales)

Tethered bilayer lipid membranes as a support for membrane active peptides
Bruce Cornell (NSW, Australia)

Membrane disordering effects of beta-amyloid peptides
Walter E. Mueller (Frankfurt, Germany)

Influenza fusion peptides
John Skehel (London, UK)


Protein Aggregation in Birmingham

Parvez Haris and Brian Austen, from the Protein and Peptide special interest group organised a symposium on Protein Folding and Aggregation at the RSC annual convention held at the ICC,Birmingham at the beginning of August.

As the formation of insoluble aggregates is a Phenomenon associated with, and perhaps causing, a number of human diseases, there is a need to understand, control and eliminate the pathways leading to aggregation both to alleviate these diseases and to obtain improved yields of useful correctly-folded recombinant proteins. Intermediates in folding may convert to correctly folded forms, or into protein aggregates (Radford, Leeds).

Stephen Davies (UCL) brought us up to date on the aggregation of polyglutamine repeat sequences expressed in the N-terminal region of the protein Huntingtin in patients with Huntington's Disease, his electron micrographs showed clearly the formation of cytoplasmic and intranuclear inclusions in neuronal cells in Huntington's patients and transgenic animal models. A number of other proteins, such as transcription factors, become trapped in these inclusions, but the mechanisms that damage the neurons, and lead to non-apoptotic cell death remain to be fully elucidated.

Human genetics suggest that aggregation of alpha- synuclein may be a cause of the neurodegeneration seen in Parkinson's Disease, Toxic oligomers and fibrils, seen by em, are produced from alpha-synuclein, its mutant forms and from shorter fragments released from alpha-synuclein by proteolysis (El-Agnaf, Lancaster), The region of alpha-synuclein important for aggregation and toxicity has been tracked down to residues 68-78 (Irvine, Belfast).

Soluble oligomers of cyclic peptides ABri and ADan, released by proteolysis of mutant forms of the BRI-proteins in familial dementias are shown to be apoptotic to neuronal cells in culture, and are prime examples of the amyloid hypothesis normally attached to Alzheimer's Disease (Austen, London). Human cystatin B is an intracellular protease inhibitor that is prone to form fibrils connected to signs of epilepsy. (Zerovnic, Slovenia).

There is a pressing need for techniques capable of detecting oligomerisation and fibril formation, atomic force spectroscopy reveals interesting annular-shaped aggregates formed from alpha-synucleins at impressive resolution (Ding, Harvard), and FT-IR holds great promise for the detection of secondary structure in partially-soluble aggregated proteins (Haris, Leicester).

The high resolving power of Fourier-transform ion cyclotron resonance mass spectrometry shows great promise for studying calcium-bonding proteins (Hoxha, Warwick), whereas there are difficulties in detecting poly-Gln interactions by NMR (Pastore, NIMR). Optimised conditions for folding proteins expressed initially as inclusion bodies in E.coli were formulated by Lilie (Halle), and the conditions required for solving the complex problem of providing a lipid-rich environment for optimal folding of membrane proteins was rationalised by Paula Booth (Bristol).

The prion protein, still continues to fascinate audiences, its copper-binding properties are now firmly established (Brown, Cambridge), whereas the mysterious way in which it contorts itself into an infective and potentially fatal, conformation, is still under computation (Warwicker, UMIST). Post-translational modifications undergone by crystallins, are known to result in aggregation of lens proteins, and the formation of cataracts (Harding, Oxford).

Altogether, this was an exciting meeting in which ideas flowed freely, The group welcome the resurgence of interest in biology, and proteomics, by the RSC in evidence throughout this conference at the ICC.

Transcripts from the symposium should appear in the journal Spectroscopy later this year.



7th International Symposium & Exhibition Solid phase synthesis & Combinatorial Chemical Libraries

Peptides, Glycopeptides, Oligonucleotides, DNA, RNA, PNA, Proteins, etc.
Small Molecule Organic Chemical Diversity, Drug Design, etc
Under the Auspices of Mayflower Trust and the European Peptide Society.
Session 1

Alternative Methods Enabling Native Chemical Ligation Assembly of Proteins
Dr Derek Hudson (Biosearch Technologies Inc, Novato, CA, USA)

Non-peptide Mimics of Helical Structures: Synthesis of Artificial Peptides and Proteins
M. Amblard, N. Raynald, D. Maux, G. Bergé, M. Calmes and Prof Jean Martinez (LAPP, Faculté de Pharmacie, Montpellier, France)

Synthesis of Peptide and Reporter Conjugates of Oligonucleotide Analogues
Dr Mike Gait (MRC Laboratory of Molecular Biology, Cambridge, England, UK)
Session 2A: Solid Phase Synthesis Supports: Handling, Design, Linkers and Spacers

Revolutionising Resin Handling for Solid Phase Synthesis
Prof Mark Bradley (University of Southampton, Southampton, England, UK)

Synthesis and Application of a Novel Perfluoroalkylsulfonyl (PFS) Linker for the Traceless Synthesis of Aromatics
Dr Chris Holmes (Affymax Research, Palo Alto, CA, USA)

Recent Advances in Synthesis and Use of High Load Spacer-modified Supports in SPS
Dr Wolfgang Rapp (Rapp Polymere GmbH, Tuebingen, Germany)

Session 2B: Solid Phase Peptide and Protein Synthesis (I)

Solid Phase Synthesis of Cyclic Peptides from Marine Source: Kahalahide F and Trunkamide A
Prof Fernando Albericio (University of Barcelona, Spain)

Solid Phase Synthesis, Purification and Characterization of Some Biologically Active Peptides and their Fragments Containing Difficult Sequences
Prof Lajos Baláspiri (Inst. of Chemistry, Hungarian Academy of Sciences, Budapest)

Extending Synthetic Access to Proteins with a Complementary Peptide bond Ligation
Dr John L. Offer and Philip E. Dawson (The Scripps Research Institute and The Skaggs Institute for Chemical Biology, La Jolla, CA, USA)
Session 3A: New Polymer Development and Combinatorial Strategies

Combinatorial Approach to the Design of New Grafted Polymeric Surfaces
Dr Nick Ede (Mimotopes Pty, Ltd., Clayton, Vic, Australia)

Combinatorial Strategies for Biomedical Polymer Development
Dr Steve Brocchini (The School of Pharmacy, University of London, England, UK)

Preparation of New Multi-Modal Ion Exchange Media -A Combinatorial Approach
Dr Nicolas Thevenin and Jean-Luc Maloisel (Amersham Pharmacia Biotech, Uppsala, Sweden)

Combinatorial Chemistry is Scintillating
Dr Andrew J Sutherland (Aston University, Birmingham, England, UK)
Session 3B: Solid Phase Peptide and Protein Synthesis (II)

Improved Synthesis, Biological Evaluation and Conformational Analysis of New h/r CRH Peptide Analogues
Prof Paul Cordopatis (Department of Pharmacy, University of Patras, Greece)

Solid Phase Incorporation of Lipidic Side-chains on Peptides
Dr Jean-Alain Fehrentz (LAPP, Faculté de Pharmacie, Montpellier, France)

Amino Acid and Peptide Diols and their Application in Ligation
Robert J Broadbridge and Dr Ram P Sharma (University of Southampton, England, UK)

Chemical Ligation of Multiple Peptide Fragments Using Thiazolidine-4-Carboxylic Acid as Cysteine Precursor
Dr Matteo Villain*, Jean Vizzavona‡ and Hubert Gaertner* (* GeneProt Inc., Swiss Branch, Meyrin, Switzerland; ‡ University of Geneva, Switzerland)
Session 3C: Oligonucleotide Synthesis and Modifications

Linker Phosphoramidites for the Synthesis of Oligonucleotides on Underivatized Supports either Singly or in Tandem
Dr Richard T. Pon, Shuyuan Yu, and Fady Girgis (University of Calgary, Calgary, AB, Canada)

Inoffensive Chemistry for Labelling, Immobilisations and Conjugations of Oligonucleotides
Dr Duncan Graham (University of Strathclyde, Glasgow, Scotland,UK)

Amide Group Assisted 3'-Dephosphorylation of Oligonucleotides Synthesized on Universal A Supports
Prof Alex Azhayev (University of Kuopio, Finland)

Doubly Labeled Oligonucleotides Through Aqeous Diels-Alder Reactions
Dr Andreas Wolter (Proligo Biochemie GmbH, Hamburg, Germany)
Session 4 - (Plenary): Combinatorial Chemistry, Spacial Diversity, Combinatorial Scaffolds

Two Decades in Combinatorial Chemistry
Prof Dr Arpad Furka (Eotvos Lorand University, Budapest, Hungary)

Chemical Libraries with Spacial Diversity and Their Use for the Discovery of Peptido- and Proteinomimetics
Prof Chaim Gilon (Hebrew University of Jerusalem, Israel

Rapid Generation of Heterocyclic Scaffolds on Solid Support: The Concept, Strategy and Practice
Dr Hossain Saneii (Advanced SymTech Inc., Louisville, KY, USA)

Session 5A: Instrumentation for Combinatorial Synthesis

Construction of a Flexible and Highly Efficient System for Compound Library Production: Consisting of Robotic Arm with Modular Reactors and Work-up Stations
Prof Kiyoshi Nokihara (Shimadzu Scientific Research, Tokyo, Japan)

Workbench Automation in Synthesis: From Preparation to a Final Substance
Werner Zinsser (Zinsser Analytic GmbH, Rodelheim, Germany)

Multistep Parallel Solution-phase Synthesis of Urea and Amide Libraries on the TridentTM System
Dr Francesco Spadola, Juergen Swienty-Busch, Sukanta Bhattacharyya and Jeff Labadie (Argonaut Technologies AG, CH-4132 Muttenz-Swizerland)
Session 5B: Genetic Analysis/ High Throughput Synthesis (I)

Duplex Scorpion Primers in SNP Analysis and FRET Applications"
A. Solinas§, L.J. Brown‡, C. McKeen‡, J.M. Mellor§, J. Nicol§, N. Thelwell‡ and Prof Tom Brown (§University of Southampton, England, UK; ‡Oswel Research Products Ltd, Southampton, England, UK)

Matrix-induced DNA Fragmentation for High Throughput MALDI-TOF Analysis of Genomic Sequence Polymorphisms
Dr Mikhail S. Shchepinov, M.F. Denissenko, K.J. Smylie, R.J. Wörl, A. L. Leppin, C.R. Cantor and C.P. Rodi (Sequenom, Inc., San Diego, CA, USA)

Randomly Assembled Arrays, SNP Analysis, and High Throughput Oligonucleotide Synthesis
Dr Michal Lebl (Illumina, Inc, and Spyder Instruments, Inc., San Diego, CA, USA)
Session 5C: Analytical Methods for Combinatorial Libraries

Applications of a New Mass Spectrometry Tagging Strategy to Focussed Peptide Libraries
Dr Corinne Kay (GlaxoSmithKline, Chemical and Analytical Technologies, Stevenage, England, UK)

Using Mass Spectrometry for Identifying Novel Substrates for Proteases
Dr Stephen C McKeown (GlaxoSmith Kline, Chemical and Analytical Technologies, Stevenage, England, UK)

Towards Analysis of Diverse Post-translational Modification of Proteins Using High Performance Mass Spectrometry
Prof Yasatsugu Shimonishi (Protein Research Foundation, Osaka University, Japan)

High Resolution Biopolymer Mass Spectrometry: New Perspectives for Analysis of Complex Biological mixtures and Combinatorial Libraries
Prof Dr Michael Przybylski (University of Konstanz, Germany)
Session 6A: Solid Phase Synthesis and Application of Peptides for Biosensor Systems

Solid Phase Synthesis of Regioselectively-labelled Peptides for Biorecognition Analyses via Biosensors
Dr John D. Wade (Howard Florey Institute, University of Melbourne, Vic, Australia)

Biosensors and Proteomics: the Role of Large Chemically Synthesized Peptides as Sensor Surfaces
Prof Ed Nice (Ludwig Institute of Cancer Research, Melbourne, Vic, Australia)
Session 6B: High Throughput Synthesis (II)

High Throughput Antisense - From 96-Well Plate Synthesis of Modified Antisense Oligonucleotides to Cell-based Screening
Dr François Natt (Novartis Pharma AG, Basel, Switzerland)

High Throughput Thematic Library Development and Production
Dr Christopher B Cooper (Bristol-Myers Squibb Pharmaceutical Research Institute, Princeton, New Jersey, USA)
Session 7A: Biomedically-significant Peptides/ Peptide Interactions

Combinatorial Search of High Structural Propensity Oligopeptides
Dr Saul Gdanski Jacchieri (A.C. Camargo Cancer Hospital, Sao Paulo, Brazil)

Chemical Modification of 'Dimerization Inhibitors' of HIV-1 Protease
S. König, Prof Dr H.J. Schramm, W. Schramm, T. Wenger, René Loic§* and B. Badet§ (Kliniken Innenstadt, Universität München, and MPI Biochemie, Martinsried, Germany; §ICSN-CNRS, Gif-sur-Yvette, France; [*deceased] )

A Peptide that Binds and Stabilises p53 Core Domain
Dr Assaf Friedler, Lars O. Hansson, Dmitry B. Veprintsev, Stefan M.V. Freund and Alan R. Fersht (Cambridge University Chemical Laboratory and Cambridge Centre for Protein Engineering, MRC Centre, Cambridge, UK)

The Structure and Neurotoxicity of the Abri Peptide an Amyloid Involved in Familial British Dementia
Prof Brian M Austen, Omar El-Agnaf, Joseph Sheridan, Christina Sidera, Giuliano Siligardi‡, Rohanna Hussain‡, Parvez L Haris§, Sidhara Nagala, Maria Lee (St George's Hospital Medical School, London, England, UK; ‡King's College, London, England, UK; §De Montfort University, Leicester, England, UK)
Session 7B: Microwave-assisted Synthesis/ Novel Intermediates and Reagents

A One-pot Three-step Solution Phase Syntheses of Thiohydantoins using Microwave Heating
Liselotte Öhberg* and Dr Jacob Westman‡ (*SIK AB, Uppsala Science Park, Uppsala, Sweden; ‡Personal Chemistry AB, Uppsala, Sweden)

Alpha Amino Aldehydes: Protection as N,O-Acetals for Use as Novel Building Blocks in the Solid Phase Synthesis of Heterocyclic Compounds"
Dr J. Beyer and Prof M. Meldal (Carlsberg Laboratory, Valby, Denmark )

Novel Polymer-supported Reagents for Organic Transformations in Solution and for Postmodification of Compound Collections Obtained by Solid Phase Synthesis
Dr Jörg Rademan and Prof Dr Guenther Jung (Institute of Organic Chemistry, University of Tuebingen, Germany)

EVOblueTM30 as New Red Excitable High Performance Fluorescence Dye for Assay Development and HTS Applications"
Dr Eloisa Lopez-Calle, Joachim R. Fries, Annett Müller and Dirk Winkler (Evotec OAI , Hamburg, Germany)

Solid Phase Synthesis of Heterocyclic Ketene Aminals (I)
Prof Mei-Xiang Wang, Tao Peng, Chan-Ping Du and Zhi-Tang Huang (Institute of Chemistry, Chinese Academy of Sciences, Beijing , China)

Solid Phase Synthesis of Heterocyclic Ketene Aminals (II)
Prof Zhi-Tang Huang, Zhen-Dong Liu, Li-Ping Xing and Mei-Xiang Wang (Institute of Chemistry, Chinese Academy of Sciences, Beijing , China)


Prizewinners for the Young Investigators Awards



Prizewinners for the Young Investigators Awards at Southampton (left to right) Sharon Gazal (Israel), Rebecca Maille [Second Prize](Southampton), Sean Monaghan(Southampton),Hazel Street[First prize] (Southampton), Oliver Schon(Cambridge).


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