LIST OF PUBLICATIONS OF M.F. PERUTZ, OM, CH, CBE, PhD, FRS

Hemoglobin Papers

M.F. Perutz. Umkristallisieren von kleinen Mengen.
Z. Kristallogr. (A) 96, 328-329, 1937.

J.D. Bernal, I. Fankuchen & M.F. Perutz. An X-ray study of chymotrypsin and haemoglobin. Nature, 141, 523-524, 1938.

M.F. Perutz. Absorption spectra of single crystals of haemoglobin in polarized light.
Nature, 143, 731-734, 1939.

M.F. Perutz. X-ray analysis of haemoglobin. Nature, 149, 491-496, 1942.

M.F. Perutz. Crystal structure of oxyhaemoglobin. Nature, 150, 324-329, 1942

J. Boyes-Watson & M.F. Perutz. X-ray analysis of haemoglobin. Nature, 151, 714-720, 1943.

M.F. Perutz. The composition and swelling properties of haemoglobin crystals. Trans. Faraday Soc. Vol.XLII B, 187-195, 1946.

M.F. Perutz & G.L. Rogers. A vacuum tank for use with a single crystal X-ray goniometer.
J. Sci. Intruments, 23, 1946.

J. Boyes-Watson, E. Davidson & M.F. Perutz. An X-ray study of horse methaemoglobin. I.
Proc. Roy. Soc. A. 191, 83-132,1947.

M.F. Perutz. An X-ray study of horse methaemoglobin. II. Proc. Roy. Soc. A 195, 474-499, 1949.

M.F. Perutz & O. Weisz. Crystal structure of human carboxyhaemoglobin. Nature, 160, 786-788, 1947.

M.F. Perutz. Submicroscopic structure of the red cell. Nature, 161, 204-206, 1948.

J.C.Kendrew & M.F.Perutz. A comparative X-ray study of foetal and adult sheep haemoglobins. Proc. Roy. Soc. A. 194, 375-398, 1948.

M.F. Perutz. Polarizing attachment for the microscope of a single crystal X-ray goniometer.
J. Sci. Instruments and of Physics in Industry, 26, 1949.

M.F. Perutz &J.M. Mitchison. State of haemoglobin in sickle-cell anaemia. Nature, 166, 677-682, 1950.

M.F. Perutz, M. Jope & R. Barer. Observations of proteins in polarized ultra-violet light.
Trans. Faraday Soc. 9, 423-427, 1950.

L. Bragg, J.C. Kendrew & M.F. Perutz. Polypeptide chain configurations in crystalline proteins. Proc. Roy. Sco. A, 203, 321-357, 1950.

M.F. Perutz, A.M. Liquori & F. Eirich. X-ray and solubility studies of the haemoglobin of sickle-cell anaemia patients. Nature, 167, 929-936, 1951.

M.F. Perutz. New X-ray evidence on the configuration of polypeptide chains. Nature, 167, 1053-1058, 1951.

M.F. Perutz. The 1.5Å reflexion from proteins and polypeptides. Nature, 168, 653-656, 1951

W.L. Bragg, E.R, Howells & M.F. Perutz. Arrangement of polypeptide chains in horse methaemoglobin. Acta Cryst. 5, 136-141, 1952.

W.L. Bragg & M.F. Perutz. The external form of the haemoglobin molecule. I Acta Cryst. 5, 277-283, 1952.

W.L. Bragg & M.F. Perutz. The external form of the haemoglobin molecule. II Acta Cryst. 5, 323-328, 1952.

W.L. Bragg & M.F. Perutz. The structure of haemoglobin. Proc. Roy. Soc. A, 213, 425-435, 1952

W.L. Bragg, E.R. Howells & M.F. Perutz. The structure of haemoglobin. II, Proc. Roy. Soc., A, 222, 33-44, 1954.

M.F. Perutz. The structure of haemoglobin III. Direct determination of the molecular transform. Proc. Roy. Soc., A, 225, 264-286, 1954.

D.W. Green, V.M. Ingram & M.F. Perutz. The structure of haemoglobin IV. Sign determination by the isomorphous replacement method. Proc. Roy. Soc, A, 225, 287-307, 1954.

E.R. Howells & M.F. Perutz. The structure of haemoglobin V. Imidazole-methaemoglobin: a further check of the signs. Proc. Roy. Soc., A, 225, 308-314, 1954.

W.L. Bragg & M.F. Perutz. The structure of haemoglobin VI. Fourier projections on the 010 plane. Proc. Roy. Soc., A, 225, 315-329, 1954.

M.F. Perutz. An optical method for finding the molecular orientation in different forms of crystalline haemoglobin; changes in dichroism accompanying oxygenation and reduction. Proc. Roy. Soc. B, 141, 69-71, 1953.

M.F. Perutz. Polarization dichroism, form birefringence, and molecular orientation in crystalline haemoglobins. Acta Cryst. 6, 859-864, 1953.

M.F. Perutz & V. Scatturin. A test of the usefulness of direct mathematical methods in the structure analysis of a protein. Acta Cryst. 7, 799-800, 1954.

M.F. Perutz, I.F. Trotter, E.R. Howells & D.W. Green. An X-ray study of reduced human haemoglobin. Acta Cryst. 8, 241-245, 1955.

M.F. Perutz. Isomorphous replacement and phase determination in non-centrosymmetric space groups. Acta Cryst. 9, 867-873, 1956

D.J.E. Ingram, J.F. Gibson & M.F. Perutz. Orientation of the four haem groups in haemoglobin. Nature, 178, 905-910, 1956.

A.F. Cullis, H.M. Dintzis and M.F. Perutz. X-ray analysis of haemoglobin. Nat. Acad. Sci. Wash. Conference of Haemoglobin. pp.50-65, 1958.

M.F. Perutz, L.K. Steinrauf, A. Stockell & A.D. Bangham, Chemical and crystallographic study of the two fractions of adult horse haemoglobin. J. Mol. Biol. 1, 402-404, 1959.

M.F. Perutz, M.G. Rossmann, A.F. Cullis, H. Muirhead, G. Will & A.C.T. North. Structure of haemoglobin. A three-dimensional Fourier synthesis at 5.5Å resolution, obtained by X-ray analysis. Nature, 185, 416-422, 1960.

D.B. Smith & M.F. Perutz. Identification of the black sub-unit of the crystallographic model of horse haemoglobin with the valyl-glutaminyl polypeptide chain. Nature, 188, 406-407, 1960.

M.F. Perutz. Structure of hemoglobin. Brookhaven Symposia in Biology No.13. 1960.

A. Stockell, M.F. Perutz, H. Muirhead & S.G. Glauser, A comparison of adult and foetal horse haemoglobins. J. Mol. Biol. 3, 112-116, 1961.

A.F. Cullis, H. Muirhead, M.F. Perutz, M.G. Rossmann & A.C.T. North. The Structure of haemoglobin VIII. A three-dimensional Fourier synthesis at 5.5Å resolution determination of the phase angles. Proc. Roy. Soc., A, 265, 15-38, 1961.

A.F. Cullis, H. Muirhead, M.F. Perutz, M.G. Rossmann & A.C.T. North. The structure of haemoglobin IX. A three-dimensional Fourier synthesis at 5.5Å resolution: description of the structure. Proc. Roy. Soc, A, 265, 161-187, 1962.

M.F. Perutz. Relation between structure and sequence of haemoglobin. Nature, 194, 914-917, 1962.

M.F. Perutz. X-ray analysis of haemoglobin. Nobel lecture. Dec. 1962.

M.F. Perutz. Proteins and Nucleic Acids. Elsevier Amsterdam, 1962.

H. Muirhead & M.F. Perutz. Structure of haemoglobin. A three-dimensional Fourier synthesis of reduced human haemoglobin at 5.5Å resolution. Nature, 199, 633-639, 1963.

M.F. Perutz, W. Bolton, R. Diamond, H. Muirhead & H.C. Watson. Structure of haemoglobin. An X-ray examination of reduced horse haemoglobin. Nature, 203, 687-690, 1964.

M.F. Perutz. Structure and function of haemoglobin. I. A tentative atomic model of horse oxyhaemoglobin. J. Mol. Biol. 13, 646-668, 1965.

M.F. Perutz, J.C. Kendrew & H.C. Watson. Structure and function of haemoglobin II. Some relations between polypeptide chain configuration and amino acid sequence. J. Mol. Biol. 13, 669-678, 1965.

H. Muirhead, J.M. Cox, L. Mazzarella & M.F. Perutz, Structure and function of haemoglobin III. A three-dimensional Fourier symthesis of human deoxyhaemoglobin at 5.5Å resolution. J. Mol. Biol. 28, 117-156, 1967.

W. Bolton, J.M. Cox & M.F. Perutz. Structure and function of haemoglobin IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5Å resolution. J. Mol. Biol. 33, 283-297, 1968.

J. Greer, M.F. Perutz & N. Rumen. Lattice constants of lamprey haemoglobin. J. Mol. Biol. 18, 547-548, 1966.

M.F. Perutz & F.S. Mathews. An X-ray study of azide methaemoglobin. J. Mol. Biol. 21, 199-202, 1966.


S.R. Simon, W.H. Konigsberg, W. Bolton and M.F. Perutz. Identity of structure of horse deoxy- and oxyhaemoglobin after reaction with bis(N-maleidomethyl)ether. J. Mol. Biol. 28, 451-454, 1967.

M.F. Perutz. Preparation of haemoglobin crystals. J. Crystal Growth, 2, 54-56, 1968.

H. Muirhead, J. Cox, L. Mazzarella & M.F. Perutz. A comparison of the structures of horse oxy- and human deoxyhaemoglobin. Journal de Chimie Physique, 65, p.188, 1968.

M.F. Perutz, H. Muirhead, J.M. Cox, L.C.G. Goaman, F.S. Mathews, E.L. McGandy & L.E Webb. Three-dimensional Fourier synthesis of horse oxyhaemoglobin at 2.8Å resolution: (1) X-ray analysis. Nature, 219, 29-32, 1968.

M.F. Perutz, H. Muirhead, J.M. Cox & L.C.G. Goaman. Three-dimensional Fourier Synthesis of Horse Oxyhaemoglobin at 2.8Å Resolution: II - The Atomic Model. Nature, 219, 131-139, 1968.

M.F. Perutz & H. Lehmann. Molecular pathology of human haemoglobin.
Nature, 219, 902-909, 1968.

M.F. Perutz. The haemoglobin molecule. The Croonian Lecture 1968. Proc. Roy. Soc. B., 173, 113-140, 1969.

M.F. Perutz, H. Muirhead, L. Mazzarella, R.A. Crowther, J. Greer & J.V. Kilmartin. Identification of residues responsible for the alkaline Bohr effect in haemoglobin. Nature, 222, 1240-1243, 1969.

J.V. Kilmartin & L. Rossi-Bernardi. Inhibition of CO2 combination and reduction of the Bohr effect in haemoglobin chemically modified at its a-amino groups. Nature, 222, 1243-1246, 1969.

H. Muirhead & J. Greer. Three-dimensional Fourier synthesis of human deoxyhaemoglobin at 3.5Å resolution. Nature 228, 516-519, 1970.

W. Bolton & M.F. Perutz. Three dimensional Fourier synthesis of horse deoxyhaemoglobin at 2.8Å resolution. Nature 228, 551-552, 1970.

M.F. Perutz Stereochemistry of cooperative effects in haemoglobin. Nature, 228, 726-739, 1970.

J. Greer & M.F. Perutz. Three dimensional structure of haemoglobin Rainier. Nature New Biology, 230, 261-264, 1971.

H. Morimoto, H. Lehmann & M.F. Perutz. Molecular Pathology of Human Haemoglobin: stereochemical interpretation of abnormal oxygen affinities. Nature, 232, 408-413, 1971.

M.F. Perutz, P. del Pulsinelli, L. Ten Eyck, J.V. Kilmartin, S. Shibata, I. Iuchi, T Miyaji & H.B. Hamilton. Haemoglobin Hiroshima and the mechanism of the alkaline Bohr effect. Nature New Biology, 232, 147-149, 1971.

M.F. Perutz & L.F. Ten Eyck. Stereochemistry of cooperative effects in hemoglobin.
Cold Spring Harbor Symposia on Quantitative Biology Vol XXXVI, 295-310, 1971.

J.A. Hewitt, J.V. Kilmartin, L.F. Ten Eyck & M.F. Perutz. Noncooperativity of the ab dimer in the reaction of hemoglobin with oxygen. Proc. Nat. Acad. Sci., 69, 203-207, 1972.

M.F. Perutz, P.D. Pulsinelli & H.M. Ranney. Structure and subunit interaction of haemoglobin M. Milwaukee. Nature New Biology, 237, 259-264, 1972.

M.F. Perutz. Nature of haem-haem interaction. Nature New Biology, 237. 495-499, 1972.

N.L. Anderson & M.F. Perutz. Site of the amino-acid substitution in haemoglobin Seattle (aA2 b702 Asp). Nature New Biology, 243, 274-275, 1973.

J.T. Finch, M.F. Perutz, J.F. Bertles & J. Döbler. Structure of sickled erythrocytes and of sickle-cell hemoglobin fibers. Proc. Nat. Acad. Sci., 70, 718-722, 1973.

M.F. Perutz. Methaemoglobin and the problem of haem-haem interaction. Biochemical Soc. Trans. pp42-43, 1973.

M.F. Perutz. Stereochemical interpretation of high oxygen affinity of haemoglobin Little Rock (a2b2143HisÆGln). Nature New Biology, 243, 180-181, 1973.

P.D. Pulsinelli, M.F. Perutz & R.L. Nagel. Structure of hemoglobin M Boston, a variant with a five-coordinated ferric heme. Proc.Nat.Acad.Sci, USA, 70, 3870-3874, 1973.

M.F. Perutz. Mechanism of denaturation of hameoglobin by alkali. Nature, 247, 341-344, 1974.

A. Arnone & M.F. Perutz. Structure of inositol hexaphosphate-human deoxyhaemoglobin complex. Nature, 249, 34-36, 1974.

M.F. Perutz, J.E. Ladner, S.R. Simon & Chien Ho. Influence of globin structure on the state of the heme. I. Human Deoxyhaemoglobin. Biochemistry, 13, 2163-2173, 1974.

M.F. Perutz, A.R. Fersht, S.R. Simon & G.C.K. Roberts. Influence of globin structure on the state of the heme. II. Allosteric transitions in methemoglobin. Biochemistry, 13, 2174-2186, 1974.

M.F. Perutz, E.J. Heidner, J.E. Ladner, J.G. Beetlestone, C. Ho & E.F. Slade. Influence of globin structure on the state of the heme. III. Changes in heme spectra accompanying allosteric transitions in methemoglobin and their implications for heme-heme interaction. Biochemistry, 13, 2187-2200, 1974.

M.F. Perutz & H. Raidt. Stereochemical basis of heat stability in bacterial ferredoxins and in haemoglobin A2. Nature, 255, 256-259, 1975.

E.J. Heidner, R.C. Ladner & M.F. Perutz. Structure of horse carbonmonoxyhaemoglobin.
J. Mol. Biol., 104, 707-722, 1976.

M.F. Perutz, J.V. Kilmartin, K. Nagai, A. Szabo & S.R. Simon. Influence of globin structures on the state of the heme. Ferrous low spin derivatives. Biochemistry, 15, 378-387, 1976.

T. Asakura, K. Adachi, J.S. Wiley, L.W.M. Fung, C. Ho, J.V. Kilmartin & M.F. Perutz. Structure and function of haemoglobin Philly (TyrC1(35)bÆPhe). J. Mol. Biol., 104, 185-195, 1976.

A. Szabo & M.F. Perutz. Equilibrium between six- and five-coordinated hemes in nitrosylhemoglobin: Interpretation of electron spin resonance spectra. Biochemistry, 15, 4427-4428, 1976.

D.J. Weatherall, J.B. Clegg, S.T. Callender, R.M.G. Wells, R.E. Gale, E.R. Huehns, M.F. Perutz, G. Viggiano & C. Ho. Haemoglobin Radcliffe (a2b299(G1)Ala): A high oxygen affinity variant causing familial polycythaemia. Brit. J. Haematology, 35, 177-191, 1977.

J.A. Frier & M.F. Perutz. Structure of human foetal deoxyhaemoglobin. J. Mol. Biol. 112, 97-112, 1977.

R.C. Ladner, E.J. Heidner & M.F. Perutz. The structure of horse methaemoglobin at 2.0Å resolution. J. Mol. Biol. 114, 385-414, 1977.

P.W. Tucker & M.F. Perutz. Mechanism of charge compensation and impairment of co-operative functions in haemoglobin Tacoma (ArgB12(20)bÆSer). J. Mol. Biol. 114, 415-420, 1977.

G. Fermi & M.F. Perutz. Structure of human fluoromethaemoglobin with inositol hexaphosphate. J. Mol. Biol., 114. 421-431, 1977.

M.F. Perutz. The role of bound water in haemoglobin and myoglobin. BioSystems, 8, 261-263, 1977.

M.F. Perutz. Hemoglobin structure and respiratory transport. Sci.Am. 239, 92-125, 1978.

P.W. Tucker, S.E.V. Phillips, M.F. Perutz, R. Houtchens & W.S. Caughey. Structure of hemoglobins Zürich (His E7(63)bÆArg) and Sydney (Val E11(67)bÆAla])and role of the distal residues in ligand binding. Proc. Natl. Acad. Sci. USA, 75, 1076-1080, 1978.

M.F. Perutz. Electrostatic effects in proteins. Science, 201, 1187-1191, 1978.

N. Alberding, S.S. Chan, L. Eisenstein, H. Frauenfelder, D. Good, I.C. Gunsalus, T.M. Nordlund, M.F. Perutz, A.H. Reynolds & L.B. Sorensen. Binding of Carbon Monoxide to Isolated Hemoglobin Chains. Biochemistry, 17, 43-51, 1978

M.F. Perutz, J.K.M. Sanders, D.H. Chenery, R.W. Noble, R.R. Pennelly, L.W.-M. Fung, C. Ho, I. Giannini, D. Porschke & H. Winkler. Interactions between the quaternary structure of the globin and the spin state of the heme in ferric mixed spin derivatives of hemoglobin. Biochemistry, 17, 3640-3652, 1978.

C. Messana, M. Cerdonio, P. Shenkin, R.W. Noble, G. Fermi, R.N. Perutz & M.F. Perutz. Influence of quaternary structure of the globin on thermal spin equilibria in different methemoglobin derivatives. Biochemistry, 17, 3652-3662, 1978.

M.F. Perutz. Molecular adaptation in haemoglobin and thermophile bacteria.
Differentiation 13, 47-50, 1979.

M.F. Perutz. Regulation of oxygen affinity of hemoglobin. Influence of structure of the globin on the heme iron. Ann. Rev. Biochem. 48, 327-386, 1979.

M.F. Perutz & K. Imai. Regulation of oxygen affinity of mammalian haemoglobins.
J. Mol. Biol., 136, 183-191, 1980.

M.F. Perutz. What the abnormal haemoglobins teach us about the folding problem.
Elsevier/North Holland Biomedical Press 1980. Ed. Rainer Jaenicke.

J.V. Kilmartin, J.H. Fogg & M.F. Perutz. Role of C-terminal histidine in the alkaline Bohr effect of human hemoglobin. Biochemistry, 19, 3189-3193, 1980.
M.F. Perutz, J.V. Kilmartin, K. Nishikura, J.H. Fogg, P.J.G. Butler & H.S. Rollema Identification of Residues contributing to the Bohr effect of human Haemoglobin. J.Mol.Biol. 138, 649-670, 1980.

M.F. Perutz. State of methaemoglobin in normal adults and in patients with hereditary methaemoglobinaemia. Biochem. J., 195, 519-520, 1981.

M.F. Perutz, C. Bauer, G. Gros, F. Leclerq, C. Vandecasserie, A.G. Schnek, G. Braunitzer, A. E. Friday and K.A. Joysey. Allosteric regulation of crocodilian haemoglobin.
Nature, 291, 682-684, 1981.

G. Fermi & M.F. Perutz. Atlas of molecular structures in biology: haemoglobin and myoglobin. Clarendon Press, Oxford, 1981.

S.E.V. Phillips, D. Hall & M.F. Perutz. Structure of deoxyhaemoglobin Zürich (HisE7(63b)ÆArg). J. Mol. Biol., 150, 137-141, 1981.

G. Fermi, M.F. Perutz, L.C. Dickinson & J.C.W. Chien. Structure of human deoxy cobalt haemoglobin J. Mol. Biol., 155, 495-505, 1982.

M.F. Perutz, S.S. Hasnain, P.J. Duke, J.L. Sessler & H.E. Hahn. Stereochemistry of iron in deoxyhaemoglobin. Nature, 295, 535-538, 1982.

M.F. Perutz & M. Brunori. Stereochemistry of cooperative effects in fish and amphibian haemoglobins. Nature, 299, 421-426, 1982.

S.E.V. Phillips, M.F. Perutz, C. Poyart & H. Wajcman. Structure and function of haemoglobin Barcelona Asp FG1(94)bÆHis. J. Mol. Biol. 164, 477-480, 1983.

D.J. Abraham, M.F. Perutz & S.E.V. Phillips. Physiological and x-ray studies of potential antisickling agents. Proc. Natl Acad. Sci. USA, 80, 324-328, 1983.

M.F. Perutz & C. Poyart. Bezafibrate lowers oxygen affinity of haemoglobin.
The Lancet, October 15, 1983.

L.J. Parkhurst, D.J. Goss & M.F. Perutz. Kinetic and equilibrium studies on the role of the b147 histidine in the Root effect and cooperativity in carp hemoglobin. Biochemistry, 22, 5401-5409, 1983.

M.F. Perutz. Species adaptation in a protein molecule. Mol. Biol. Evol., 1, 1-28, 1983
and Adv.Prot.Chem., 36, 213, 1984.

G. Fermi, M.F. Perutz, B. Shaanan & R. Fourme. The crystal structure of human deoxyhaemoglobin at 1.74Å resolution. J. Mol. Biol. 175, 159-174, 1984.

M.F. Perutz, G. Fermi & D.T-b. Shih. Structure of deoxyhemoglobin Cowtown (HisHC3(146)bÆLeu): Origin of the alkaline Bohr effect and electrostatic interactions in hemoglobin. Proc. Nat. Acad. Sci. USA 81, 4781-4784, 1984.

A.M. Gronenborn, G.M. Clore, M. Brunori, B. Giardina, G. Falcioni & M.F. Perutz. Stereochemistry of ATP and GTP bound to fish haemoglobins. J. Mol. Biol. 178, 731-742, 1984.

M.F. Perutz, A.M. Gronenborn, G.M. Clore, J.H. Fogg & D.T-b. Shih. The pKa's of two histidines in human haemoglobin, the Bohr effect, and the dipole moments of a-helices. J. Mol. Biol. 183, 491-498, 1985.

M.F. Perutz, A.M. Gronenborn, G.M. Clore, D.T-b.Shih & C.T.Craescu. Comparison of histidine proton magnetic resonances of human carbonmonoxyhaemoglobin in different buffers. J. Mol. Biol. 186, 471-473, 1985.

K. Nagai, M.F. Perutz & C. Poyart. Oxygen binding properties of human mutant hemoglobins synthesized in Escherichia coli. Proc.Nat.Acad.USA. 82, 7252-7255, Nov. 1985.

M.F. Perutz. "A clam with a difference". Nature (News & Views) 316, 210, 1985.

K. Nagai, M.F. Perutz & C. Poyart. Studies of haemoglobin functions by site-directed mutagenesis. Phil.Trans.R.Soc.Lond.A 317, 443-447, 1986.

M. F. Perutz. Concluding remarks, Royal Society Discussion Meeting on "Design, Construction and Properties of Novel Protein Molecules", 5-6 June 1985. Phil.Trans.R.Soc.Lond.A 317, 449-451 1986.

M. F. Perutz, G. Fermi, D. J. Abraham, C. Poyart & E. Burseaux. Hemoglobin as a receptor of drugs and peptides: X-ray studies of the stereochemistry of binding. J.Am.Chem.Soc. 108, 1064-1078, 1986.

M.F. Perutz. Inhibition into activation. Nature 326 (News & Views) 745, 23 April 1987.

D.T-b. Shih, M.F.Perutz, A. Gronenborn & G.M. Clore. Histidine proton resonances of carbonmonoxy-haemoglobins A and Cowtown in chloride-free buffer. J.Mol.Biol. 195, 453-455, 1987.

D.T.-b. Shih & M.F. Perutz. Influence of Anions and Protons on the Adair Coefficients of haemoglobins A and Cowtown (His HC3(146)b->Leu). J.Mol.Biol. 195, 419-422, 1987.

M. Brunori, A. Bellelli, B. Giardina, S. Condo & M.F. Perutz. Is there a root effect in Xenopus hemoglobin? FEBS Letts. 221, 1, 161-166, 1987.

M.F. Perutz, G. Fermi, B. Luisi, B. Shaanan, & R.C. Liddington. Stereochemistry of cooperative mechanisms in hemoglobin. Accs.Chem.Res. 20, 309, 1987.

M.F. Perutz. Molecular Anatomy, Physiology and Pathology of Hemoglobin.
In: Molecular Basis of Blood Diseases. Eds. G.Stamatoyannopoulos, A.W. Nienhuis, P. Leder & P.W.Majerus W.B. Saunders Company 1987.

B.F. Luisi, K. Nagai & M.F. Perutz. X-Ray crystallographic and functional studies of human haemoglobin mutants produced in Escherichia coli. Haemoglobin. Proc.Inc.Meeting, London 1986. Acta haemat. 78, 85-89, 1987.

G. Fermi, M.F. Perutz & R.G. Shulman. Iron distances in hemoglobin: Comparison of X-ray crystallographic and extended X-ray absorption fine structure studies.. Proc.Natl.Acad.Sci.USA. 84, 6167-6168, 1987.

M.F. Perutz, G. Fermi, J. Fogg & S. Rahbar. Indirect allosteric effects of a neutral mutation. Structure of deoxyhaemoglobin North Chicago (ProC2(36)bÆSer). J.Mol.Biol. 201, 459-461, 1988.

M. Levitt & M.F. Perutz. Aromatic rings act as hydrogen bond acceptors. J.Mol.Biol. 201, 751-754, 1988.

I. Lalezari, S. Rahbar, P. Lalezari, G. Fermi & M.F. Perutz. LR16, a compound with potent effects on the oxygen affinity of hemoglobin, on blood cholesterol, and on low density lipoprotein. Proc.Natl.Acad.Sci.USA 85, 6117-6121,1988.

M. F. Perutz. Control by phosphorylation. Nature (News & Views) 336, 202, 17 Nov. 1988.

M. F. Perutz & G. Fermi. Stereochemistry of salt-bridge formation in a-helices and b-strands. Proteins: Structure, Function & Genetics 4, 294-295, 1988.

M. F. Perutz. Myoglobin and haemoglobin: role of distal residues in reactions with haem ligands. Trends in Biochem.Sci. 14, 42, 1989.

M. F. Perutz. Mechanisms of cooperativity and allosteric regulation in proteins. Quarterly Reviews of Biophysics. 22, 2, 139-236, 1989. also Cambridge University Press, Cambridge, New York, Port Chester, Melbourne, Sydney, pp 101, 1990.

M. P. Kavanaugh, M.F. Perutz, G.Fermi, D.T.Shih & R. Jones. Structure and function of human hemoglobin covalently labeled with periodate-oxidized adenosine triphosphate.
J.Biol.Chem. 264, 19, 11009-11013,1989.

I. Lalezari, P. Lalezari, C. Poyart, M. Marden, J. Kister, B. Bohn, G. Fermi & M.F. Perutz. New effectors of human hemoglobin: Structure and function. Biochemistry, 29, 6, 1515-1523, 1990.

G.R. Honig, L.N. Vida, B.B. Rosenblum, M.F. Perutz & G. Fermi. Hemoglobin Warsaw (Pheb42(CD1)ÆVal), an unstable variant with decreased oxygen affinity. J.Biol.Chem. 265, 1, 126-132,1990.

Z. Derewenda, G. Dodson, P. Emsley, D. Harris, K. Nagai, M. Perutz & J.-P. Reynaud. Stereochemistry of carbon monoxide binding to normal human adult and Cowtown haemoglobins. J.Mol.Biol., 211, 515-519, 1990.

M. F. Perutz. Mechanisms regulating the reactions of human hemoglobin with oxygen and carbon monoxide. Annu. Rev.Physiol. 52, 1-25, 1990.

M. F. Perutz. Frequency of abnormal human haemoglobins caused by CÆT transitions in CpG dinucleotides. J.Mol.Biol. 213, 203-206,1990 also Biophys.Chem. 37, 25-29, 1990 and Boll. Soc. It. Biol. Sper., 66, 809-819, 1990.

Y. Huang, J. Pagnier, P. Magne, F. Baklouti, J. Kister, J. Delaunay, C. Poyart, G. Fermi & M.F. Perutz. Structure and function of hemoglobin variants at an internal hydrophobic site Consequences of mutations at the b 27 (B29) position. Biochemistry, 29, 7020-7023, 1990.

M. F. Perutz. "Molecular Inventiveness"
Nature (News & Views), 348, 583-584, 1990.

M. F. Perutz. How Lawrence Bragg invented X-ray analysis. Proc.Roy.Inst.G.B. 62, 183-198, 1990 also Acta Cryst, A46, 633-643, 1990.

M. Perutz. Physics and the Riddle of Life. In: Comprehensive Biochemistry, vol. 37,
(G. Semenza and R. Jaenicke, eds.) Elsevier Science Publishers BV., 1-20, 1990.

M. F. Perutz. Hemoglobin In: Encyclopedia of Human Biology, vol. 4. Academic Press, New York, 135-144, 1991.

T. Boehm, L. Foroni, Y. Kaneko, M.F. Perutz & T.H. Rabbits. The rhombotin family of cysteine-rich LIM-domain oncogenes: Distinct members are involved in T-cell translocations to human chromosomes 11p15 and 11p13. Proc.Nat.Acad.Sci.USA, 88, 4367-4371, 1991.

S. Bonaventura, R. Cashon, J. Bonaventura, M. Perutz, G. Fermi, D.T-b. Shih. Involvement of the distal histidine in the low affinity exhibited by Hb Chico (Lys b66ÆThr) and its isolated b chains. J.Biol.Chem., 266, 23033-23040, 1991.

G. Fermi, M.F. Perutz, D. Williamson, P. Stein & D.T-b. Shih. Structure-function relationships in the low-affinity mutant of haemoglobin Aalborg (Gly74(E18)bÆArg). J.Mol.Biol., 226, 883-888, 1992.

M.F. Perutz. Species adaptation of the allosteric regulation of hemoglobin. In: Regulation of Proteins by Ligands. Proc. The Robert A. Welch Found. Conf. Chem. Res. Vol XXXVI. 1-14, 1992.

M.F. Perutz. What are enzyme structures telling us? Roy.Soc.Chem., Faraday Discuss., 93, 1-11, 1992.

I. De Baere, L. Liu, L. Moens, J. Van Beeumen, C. Gielens, J. Richelle, C. Trotman, J. Finch, M. Gerstein & M. Perutz. Polar zipper sequence in the high affinity hemoglobin of Ascaris Suum: Amino acid sequence and structural interpretation. Proc.Natl.Acad.Sci.USA, 89, 4638-4642,1992.

L. Camardella, C. Caruso, R. D'Avino, G. di Prisco, B. Rutigliano, M. Tamburrini, G. Fermi & M.F. Perutz. Haemoglobin of the antarctic fish Pagothenia bernacchii. Amino acid sequence, oxygen Eequilibria and crystal structure of its carbonmonoxy derivative. J.Mol.Biol., 224, 449-460, 1992.

M.F. Perutz. The significance of the hydrogen bond in physiology. In: The Chemical Bond: Structure & Dynamics (A.Zewail, ed.) Academic Press, New York. 1992.

M.F. Perutz. Protein Structure: New Approaches to Disease and Therapy. W.H. Freeman and Company, New York, 1992.

M.F. Perutz. Protein function below 220 K. Nature, 358, 548, 1992.

M.F. Perutz, R. Staden, L. Moens & I. De Baer. Polar zippers. Curr. Biol., 3(5), 249-253, 1993.

M.F. Perutz. The fifth freedom; an essay review. Eur. Rev. 1(3), 243-248, 1993.
D.T.-b. Shih, B. F. Luisi, G. Miyasaki, M.F. Perutz & K. Nagai. A mutagenic study of the allosteric linkage of His(HC3) 146b in haemoglobin. J.Mol.Biol. 230, 1291-1296, 1993.

M.F. Perutz, G. Fermi, C. Poyart, J. Pagnier & J. Kister. A novel allosteric mechanism in haemoglobin: Structure of bovine deoxyhaemoglobin, absence of specific chloride-binding sites and origin of the chloride-linked Bohr effect in bovine and human haemoglobin. J.Mol.Biol. 233, 536-545, 1993.

M.F. Perutz. The role of aromatic rings as hydrogen-bond acceptors in molecular recognition.
Phil.Trans.R.Soc.A., Faraday Discuss., 345, 105-112, 1993.
M.F. Perutz. Before the double helix. Co-Chairman's remarks. Presented at the COGENE/Symposium: 'From the Double Helix to the Human Genome: 40 Years of Molecular Genetics', UNESCO, Paris. also Gene 135, 9-13, 1993.

I. De Baere, M.F. Perutz, L. Kiger, M. Marden & C. Poyart. Formation of two hydrogen bonds from the globin to the heme-linked oxygen molecule in Ascaris hemoglobin. Proc.Natl.Acad.Sci. USA. 91, 1594-1597, 1994.

M.F. Perutz, D.T.-b. Shih & D. Williamson. The chloride effect in human haemoglobin: A new kind of allosteric mechanism. J. Mol. Biol. 239, 555-560, 1994.

M.F. Perutz, T. Johnson, M. Suzuki & J.T. Finch. Glutamine repeats as polar zippers: Their possible role in inherited neurodegenerative diseases. Proc.Natl.Acad.Sci. USA. 91, 5355-5358, 1994.

M.A. Gilles-Gonzalez, G. Gonzalez, M.F. Perutz, L. Kiger, M.C. Marden & C. Poyart. Heme-based sensors, exemplified by the kinase FixL, are a new class of heme protein with distinctive ligand binding and autoxidation. Biochemistry 33, 8067-8073, 1994.

M.F. Perutz. Linus Pauling Obituary. Structural Biology 1, 667-671, 1994.

M.F. Perutz. Dorothy Hodgkin Obituary. Quarterly Review of Biophysics 27, 333-337, 1994.

M.F. Perutz. Polar zippers: Their role in human disease. Protein Science 3, 1629-1637, 1994.
and Pharmaceutica Acta Helvetiae 69, 213-224 (1995).

M.A. Gilles-Gonzalez, G. Gonzalez & M.F. Perutz. Kinase activity of oxygen sensor FixL depends on the spin state of its heme iron. Biochemistry 34, 232-236, 1995.

Stott, K., Blackburn, J.M., Butler, P.J.G. & Perutz, M. Incorporation of glutamine repeats makes protein oligomerize: Implications for inherited neurodegenerative diseases. Proc. Nat. Acad. Sci. USA 92, 6509-6513, 1995.

Haratyunyan, E.H., Sofanova, T.N., Kuranova, I.P., Popov, A.N., Teplyakov, A.V., Obmolova, G.V., Rusakov, A.A., Vainshtein, B.K., Dodson, G.G., Wilson, J.C. & Perutz, M.F. The structure of deoxy- and oxy-leghaemoglobin from Lupin. J. Mol. Biol. 251, 104-115, 1995.

Perutz, M.F. Hoppe-Seyler, Stokes and Haemoglobin (Guest Editorial). Biol. Chem. Hoppe-Seyler 376, 449-450, 1995.

Perutz, M.F. Glutamine repeats as polar zippers: Their role in inherited neurodegenerative diseases. Molecular Medicine 1(7), 718-721, 1995.

M.F. Perutz. Cause of the Root effect in fish haemoglobin. Nature Structural Biol. 3, 211-212, 1996.

M.F. Perutz.Taking the pressure off. Nature (News & Views) 380, 205-2206, 1996.

M.F. Perutz. Glutamine repeats and inherited neurodegenerative diseases: molecular aspects. Curr. Opin. Struct. Biol. 6, 848-858, 1996.

M.F. Perutz. Cause of the root effect in fish haemoglobins. Nat. Struct. Biol. 3, 211-212.

M.F. Perutz. Mutations make enzyme polymerize. Nature 385, 773-775, 1997.

M.F. Perutz. By what right do we invoke human rights? Eur. Rev. 5, 123-133, 1997.

M.F. Perutz. Bedeutung der Waserstoffbrücken für die Physiologie. Naturw. Rdsch. 49 Jahrgang. 6, 215-221, 1997.

M.F. Perutz. Verteidigung eines pioniers: Louis Pasteur. Naturw. Rdsch. 50 Jahrgang. 4, 132-136, 1997.

M.F. Perutz. Hemoglobin. Encyclopedia of Human Biology 4, 511-521, 1997.

M.F. Perutz. Lise Meitner und die Entdeckung der Kernspaltung. Naturw. Rdsch. 50 Jahrgang 12, 463-470, 1997.

M.F. Perutz. Mutations make enzymes polymerise. Nature 385, 773-774, 1997.

M.F. Perutz, Science is not a quiet life. Unravelling the atomic mechanism of haemoglobin.
Imperial College Press and World Scientific Publishing Company, 1997.

S. Bettati, A. Mozzarelli & M.F. Perutz. Allosteric Mechanism of Haemoglobin: Rupture of Salt-bridges Raises the Oxygen Affinity of the T-structure. J. Mol. Biol.281, 581-585, 1998.

M.F. Perutz, A.J. Wilkinson, M. Paoli & G.G. Dodson. The Stereochemical Mechanism of the Cooperative effects in Hemoglobin revisited. Annu. Rev. Biophysics.Biomol. Struct. 27, 1-34, 1998.

M.F. Perutz. I wish I'd made you angry earlier. Cold Spring Harbor Laboratory Press 1998.
and Oxford University Press 1999.

M.F. Perutz, M. Paoli & A.M. Lesk. Fix L, a haemoglobin that acts as an oxygen sensor: signalling mechanism and structural basis of its homology with PAS domains.
Chemistry & Biology 6, R291-R297, 1999.

M F Perutz. Glutamine repeats & neurodegenerative diseases: molecular aspects. TIBS 24, 58-63, 1999.

Y W Chen, K Stott & M F Perutz. Crystal structure of a dimeric chymotrypsin inhibitor 2 mutant containing an inserted glutamine repeat. Proc. Natl. Acad. Sci. USA 96, 1257-1261, 1999.

M.F. Perutz. Will biomedicine outgrow support? Nature 399, 299-301, 1999.

M.F. Perutz. A Woman Scientist's Role Model. Notes Rec. Re. Soc. London. Book Review 54 (3), 387-408, 2000.

M.F. Perutz, A. H. Windle. Cause of neural death in neurodengenerative disease attribute to expansion of glutamine repeats. Nature 412, 143-144, (2001).

M.F. Perutz, J.T. Finch, J. Berriman & A. Lesk. Amyloid Fibres are Water-filled Nanotubes.
PNAS In press (2002).



Studies of Minerals and Glaciers


M.F. Perutz. 'Iron-rhodonite' (from slag) and pyroxmangite and their relation to rhodonite.
Mineralogical Magazine, 24, 573-576, 1937.

M.F. Perutz. Radioactive nodules from Devon shire, England.
"Mineralogische und Petrographische Mitteilungen", 51, 141-161, 1939.

M.F. Perutz. Mechanism of glacier flow. Proc.Phys.Soc., 52, 132-135, 1940.

M.F. Perutz & G. Seligman. A crystallographic investigation of glacier structure and the mechanism of glacier flow. Proc.R.Soc. A, 172, 335-360, 1939.

J.A.F. Gerrard, M.F. Perutz & A. Roch. Measurement of the velocity distribution along a vertical line through a glacier. Proc.R.Soc. A, 213, 546-558, 1952.

M.F. Perutz. The flow of glaciers. Nature, 172, 929-938, 1953.



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