2000
Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne
Senes A, Gerstein M, Engelman D. Statistical analysis of amino acid patterns in transmembrane helices: the GxxxG motif occurs frequently and in association with β-branched residues at neighboring positions11Edited by G. von Heijne. Journal Of Molecular Biology 2000, 296: 921-936. PMID: 10677292, DOI: 10.1006/jmbi.1999.3488.Peer-Reviewed Original ResearchAmino Acid MotifsAmino Acid SubstitutionAmino Acids, Branched-ChainBiasBinding SitesCell MembraneDatabases, FactualDimerizationGlycineGlycophorinsIsoleucineMathematicsMembrane ProteinsModels, MolecularMolecular WeightOdds RatioPliabilityProtein FoldingProtein Structure, SecondaryThermodynamicsValine
1993
Mutations can cause large changes in the conformation of a denatured protein.
Flanagan J, Kataoka M, Fujisawa T, Engelman D. Mutations can cause large changes in the conformation of a denatured protein. Biochemistry 1993, 32: 10359-70. PMID: 8399179, DOI: 10.1021/bi00090a011.Peer-Reviewed Original ResearchConceptsAmino acid substitutionsPolypeptide chainSecondary structureCoil-like polymerAcid substitutionsCircular dichroism spectroscopySmall-angle X-ray scatteringSingle amino acid substitutionCarboxyl-terminal deletionsPersistent secondary structureResidual secondary structureX-ray scatteringUseful model systemDelta polypeptideSolvent conditionsDichroism spectroscopyConformational distributionCarboxyl terminusNative nucleaseRandom polymersAmino acidsSingle substitutionPolymersStaphylococcal nucleaseGlobular proteins
1984
Neutron Scattering and the 30 S Ribosomal Subunit of E. coli
Moore P, Engelman D, Langer J, Ramakrishnan V, Schindler D, Schoenborn B, Sillers I, Yabuki S. Neutron Scattering and the 30 S Ribosomal Subunit of E. coli. Basic Life Sciences 1984, 27: 73-91. PMID: 6370225, DOI: 10.1007/978-1-4899-0375-4_4.Peer-Reviewed Original ResearchInelastic Neutron Scattering Studies of Hexokinase in Solution
Engelman D, Dianoux A, Cusack S, Jacrot B. Inelastic Neutron Scattering Studies of Hexokinase in Solution. Basic Life Sciences 1984, 27: 365-380. PMID: 6712571, DOI: 10.1007/978-1-4899-0375-4_22.Peer-Reviewed Original ResearchConceptsNeutron scatteringInelastic Neutron Scattering StudyInelastic neutron scatteringInstitute Laue-LangevinNeutron Scattering StudyBiological macromoleculesMolecular dynamicsInelastic scatteringExcited modesScattering StudyScatteringSuch measurementsSuch experimentsDynamic propertiesMacromoleculesSolutionProperties
1983
Assignment of segments of the bacteriorhodopsin sequence to positions in the structural map
Trewhella J, Anderson S, Fox R, Gogol E, Khan S, Engelman D, Zaccai G. Assignment of segments of the bacteriorhodopsin sequence to positions in the structural map. Biophysical Journal 1983, 42: 233-241. PMID: 6871370, PMCID: PMC1329232, DOI: 10.1016/s0006-3495(83)84391-4.Peer-Reviewed Original Research
1981
Cholesteryl myristate conformation in liquid crystalline mesophases determined by neutron scattering.
Burks C, Engelman D. Cholesteryl myristate conformation in liquid crystalline mesophases determined by neutron scattering. Proceedings Of The National Academy Of Sciences Of The United States Of America 1981, 78: 6863-6867. PMID: 6947261, PMCID: PMC349152, DOI: 10.1073/pnas.78.11.6863.Peer-Reviewed Original ResearchMeSH KeywordsCholesterol EstersCrystallizationMathematicsMolecular ConformationNeutronsScattering, RadiationConceptsLiquid crystalline mesophasesTerminal methyl groupSpecific molecular modelsCrystalline mesophasesEster moleculesConformational rangeCholesterol moietyPure phaseCholesteryl ester moleculesExtended conformationMethyl groupNeutron scatteringMolecular modelConformationIsotropic phaseThree-carbonMoleculesPersistence of atherosclerosisEstersCholesteryl myristateMesophasesMoietyConformation of liquid N-alkanes
Goodsaid-Zalduondo F, Engelman D. Conformation of liquid N-alkanes. Biophysical Journal 1981, 35: 587-594. PMID: 7272453, PMCID: PMC1327550, DOI: 10.1016/s0006-3495(81)84814-x.Peer-Reviewed Original ResearchMeSH KeywordsAlkanesMathematicsMolecular ConformationNeutronsScattering, RadiationStructure-Activity Relationship
1979
[49] On the feasibility and interpretation of intersubunit distance measurements using neutron scattering
Moore P, Engelman D. [49] On the feasibility and interpretation of intersubunit distance measurements using neutron scattering. Methods In Enzymology 1979, 59: 629-638. PMID: 440089, DOI: 10.1016/0076-6879(79)59118-6.Peer-Reviewed Original Research
1978
X‐Ray and Neutron Small‐Angle Scattering Studies of the Complex between Protein S1 and the 30‐S Ribosomal Subunit
LAUGHREA M, ENGELMAN D, MOORE P. X‐Ray and Neutron Small‐Angle Scattering Studies of the Complex between Protein S1 and the 30‐S Ribosomal Subunit. The FEBS Journal 1978, 85: 529-534. PMID: 348475, DOI: 10.1111/j.1432-1033.1978.tb12268.x.Peer-Reviewed Original Research
1976
Protein pair distance determination in the 30 S ribosomal subunit of E. coli.
Engelman D, Moore P, Schoenborn B. Protein pair distance determination in the 30 S ribosomal subunit of E. coli. Brookhaven Symposia In Biology 1976, iv20-iv37. PMID: 786445.Peer-Reviewed Original Research
1975
Neutron scattering measurements of separation and shape of proteins in 30S ribosomal subunit of Escherichia coli: S2-S5, S5-S8, S3-S7.
Engelman D, Moore P, Schoenborn B. Neutron scattering measurements of separation and shape of proteins in 30S ribosomal subunit of Escherichia coli: S2-S5, S5-S8, S3-S7. Proceedings Of The National Academy Of Sciences Of The United States Of America 1975, 72: 3888-3892. PMID: 1105567, PMCID: PMC433101, DOI: 10.1073/pnas.72.10.3888.Peer-Reviewed Original ResearchDetermination of Quaternary Structure by Small Angle Neutron Scattering
Engelman D, Moore P. Determination of Quaternary Structure by Small Angle Neutron Scattering. Annual Review Of Biophysics And Bioengineering 1975, 4: 219-241. PMID: 1098555, DOI: 10.1146/annurev.bb.04.060175.001251.Peer-Reviewed Original ResearchA neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli
Moore P, Engelman D, Schoenborn B. A neutron scattering study of the distribution of protein and RNA in the 30 S ribosomal subunit of Escherichia coli. Journal Of Molecular Biology 1975, 91: 101-120. PMID: 1102695, DOI: 10.1016/0022-2836(75)90374-5.Peer-Reviewed Original Research