Journal of molecular biology.
Molecular Biology
Bacteriology
Biochemistry
Biology
Publisher:
Academic Press. Amsterdam : Elsevier
Frequency: Twenty-four no. a year, 2013-
Country: Netherlands
Language: English
Start Year:1959 -
ISSN:
0022-2836 (Print)
1089-8638 (Electronic)
0022-2836 (Linking)
1089-8638 (Electronic)
0022-2836 (Linking)
Impact Factor
5.6
2022
| NLM ID: | 257956 |
| (DNLM): | J30320000(s) |
| (OCoLC): | 01782923 |
| Coden: | JMOBAK |
| Classification: | W1 JO773 |
Proton magnetic resonance study of the histidine residues of sperm whale and horse myoglobins.
Journal of molecular biology
November 14, 1972
Volume 71, Issue 2 513-519 doi: 10.1016/0022-2836(72)90367-1
Cohen JS, Hagenmaier H, Pollard H, Schechter AN.No abstract available Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
Journal of molecular biology
May 28, 1971
Volume 58, Issue 1 69-77 doi: 10.1016/0022-2836(71)90232-4
Simon SR, Arndt DJ, Konigsberg WH.No abstract available Structure and functional properties of chemically modified horse hemoglobin. II. X-ray studies.
Journal of molecular biology
May 28, 1971
Volume 58, Issue 1 79-88 doi: 10.1016/0022-2836(71)90233-6
Moffat JK.No abstract available Comparison of protein structure in the crystal and in solution. V. Solubility of horse methemoglobin and azide binding.
Journal of molecular biology
August 14, 1968
Volume 35, Issue 3 477-481 doi: 10.1016/s0022-2836(68)80007-5
Rupley JA, Gates V.No abstract available Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution.
Journal of molecular biology
April 14, 1968
Volume 33, Issue 1 283-297 doi: 10.1016/0022-2836(68)90294-5
Bolton W, Cox JM, Perutz MF.No abstract available Comparative analysis of the IgG heavy chain carbohydrate peptide.
Journal of molecular biology
December 28, 1967
Volume 30, Issue 3 555-558 doi: 10.1016/0022-2836(67)90369-5
Howell JW, Hood L, Sanders BG.No abstract available Identity of structure of horse deoxy- and oxyhaemoglobin after reaction with bis(N-maleidomethyl)ether.
Journal of molecular biology
September 28, 1967
Volume 28, Issue 3 451-454 doi: 10.1016/s0022-2836(67)80094-9
Simon SR, Konigsberg WH, Bolton W, Perutz MF.No abstract available [Electronic Structure of the Prosthetic Groups and Tertiary Structure in Hemoproteins: I. Magnetic and Optical Properties of Divalent Horse Hemoglobin and Myoglobin under Reversible Detergent Action].
Journal of molecular biology
December 1, 1964
Volume 10 475-487 doi: 10.1016/s0022-2836(64)80067-x
GERSONDE K, NETTER H.No abstract available The Immunochemical Difference Between Horse Oxy- and Deoxyhaemoglobin.
Journal of molecular biology
September 1, 1964
Volume 9 785-788 doi: 10.1016/s0022-2836(64)80184-4
REICHLIN M, BUCCI E, ANTONINI E, WYMAN J, ROSSI-FANELLI A.No abstract available Three-dimensional structure of horse liver alcohol dehydrogenase at 2-4 A resolution.
Journal of molecular biology
March 25, 1976
Volume 102, Issue 1 27-59 doi: 10.1016/0022-2836(76)90072-3
Eklund H, Nordström B, Zeppezauer E, Söderlund G, Ohlsson I, Boiwe T, Söderberg BO, Tapia O, Brändén CI, Akeson A.No abstract available Read More
94
The DNA sequence of equine herpesvirus 2.
Journal of molecular biology
June 9, 1995
Volume 249, Issue 3 520-528 doi: 10.1006/jmbi.1995.0314
Telford EA, Watson MS, Aird HC, Perry J, Davison AJ.The complete DNA sequence of equine herpesvirus 2 (EHV-2) strain 86/67 was determined. The genome is 184,427 bp in size and has a base composition of 57.5% G + C. Unusually for a herpesvirus, about a third of the sequence distributed in several large blocks appears not to encode proteins. The 79 open reading frames that were identified as probably polypeptide-coding are predicted to encode 77 distinct proteins. Amino acid sequence comparisons confirmed that EHV-2 is a gamma-herpesvirus that is genetically collinear with herpesvirus saimiri (HVS; a gamma 2-herpesvirus) and Epstein-Barr virus (E... Read More
65
Horse prion protein NMR structure and comparisons with related variants of the mouse prion protein.
Journal of molecular biology
May 8, 2010
Volume 400, Issue 2 121-128 doi: 10.1016/j.jmb.2010.04.066
Pérez DR, Damberger FF, Wüthrich K.The NMR structure of the horse (Equus caballus) cellular prion protein at 25 degrees C exhibits the typical PrP(C) [cellular form of prion protein (PrP)] global architecture, but in contrast to most other mammalian PrP(C)s, it contains a well-structured loop connecting the beta2 strand with the alpha2 helix. Comparison with designed variants of the mouse prion protein resulted in the identification of a single amino acid exchange within the loop, D167S, which correlates with the high structural order of this loop in the solution structure at 25 degrees C and is unique to the PrP sequences of e... Read More
61
Fine and domain-level epitope mapping of botulinum neurotoxin type A neutralizing antibodies by yeast surface display.
Journal of molecular biology
October 3, 2006
Volume 365, Issue 1 196-210 doi: 10.1016/j.jmb.2006.09.084
Levy R, Forsyth CM, LaPorte SL, Geren IN, Smith LA, Marks JD.Botulinum neurotoxin (BoNT), the most poisonous substance known, causes naturally occurring human disease (botulism) and is one of the top six biothreat agents. Botulism is treated with polyclonal antibodies produced in horses that are associated with a high incidence of systemic reactions. Human monoclonal antibodies (mAbs) are under development as a safer therapy. Identifying neutralizing epitopes on BoNTs is an important step in generating neutralizing mAbs, and has implications for vaccine development. Here, we show that the three domains of BoNT serotype A (BoNT/A) can be displayed on the... Read More
60
High-resolution study of the three-dimensional structure of horse heart metmyoglobin.
Journal of molecular biology
June 20, 1990
Volume 213, Issue 4 885-897 doi: 10.1016/S0022-2836(05)80270-0
Evans SV, Brayer GD.The three-dimensional structure of horse heart metmyoglobin has been refined to a final R-factor of 15.5% for all observed data in the 6.0 to 1.9 A resolution range. The final model consists of 1242 non-hydrogen protein atoms, 154 water molecules and one sulfate ion. This structure has nearly ideal bonding and bond angle geometry. A Luzzati plot of the variation in R-factor with resolution yields an estimated mean co-ordinate error of 0.18 A. An extensive analysis of the pattern of hydrogen bonds formed in horse heart metmyoglobin has been completed. Over 80% of the polypeptide chain is involv... Read More
47
The structure of horse methaemoglobin at 2-0 A resolution.
Journal of molecular biology
August 15, 1977
Volume 114, Issue 3 385-414 doi: 10.1016/0022-2836(77)90256-x
Ladner RC, Heidner EJ, Perutz MF.No abstract available Read More
41
Reconstituted and native iron-cores of bacterioferritin and ferritin.
Journal of molecular biology
December 5, 1987
Volume 198, Issue 3 405-416 doi: 10.1016/0022-2836(87)90290-7
Mann S, Williams JM, Treffry A, Harrison PM.The structural and magnetic properties of the iron-cores of reconstituted horse spleen ferritin and Azotobacter vinelandii bacterioferritin have been investigated by high-resolution transmission electron microscopy, electron diffraction and Mossbauer spectroscopy. The structural properties of native horse spleen ferritin, native Az. vinelandii, and native and reconstituted Pseudomonas aeruginosa bacterioferritins have also been determined. Reconstitution in the absence of inorganic phosphate at pH 7.0 showed sigmoidal behaviour in each protein but was approximately 30% faster in initial rate f... Read More
24
Amyloid protofilaments from the calcium-binding protein equine lysozyme: formation of ring and linear structures depends on pH and metal ion concentration.
Journal of molecular biology
July 10, 2003
Volume 330, Issue 4 879-890 doi: 10.1016/s0022-2836(03)00551-5
Malisauskas M, Zamotin V, Jass J, Noppe W, Dobson CM, Morozova-Roche LA.The calcium-binding equine lysozyme has been found to undergo conversion into amyloid fibrils during incubation in solution at acidic pH. At pH 4.5 and 57 degrees C, where equine lysozyme forms a partially unfolded molten globule state, the protein forms protofilaments with a width of ca. 2 nm. In the absence of Ca(2+) the protofilaments are present as annular structures with a diameter of 40-50 nm. In the presence of 10 mM CaCl(2) the protofilaments of equine lysozyme are straight or curved; they can assemble into thicker threads, but they do not appear to undergo circularisation. At pH 2.0, ... Read More
22
Structure of horse carbonmonoxyhaemoglobin.
Journal of molecular biology
July 5, 1976
Volume 104, Issue 3 707-722 doi: 10.1016/0022-2836(76)90130-3
Heidner EJ, Ladner RC, Perutz MF.No abstract available Read More
21
Binding of equine infectious anemia virus matrix protein to membrane bilayers involves multiple interactions.
Journal of molecular biology
March 15, 2000
Volume 296, Issue 3 887-898 doi: 10.1006/jmbi.1999.3482
Provitera P, Bouamr F, Murray D, Carter C, Scarlata S.Human immunodeficiency virus (HIV) and equine infectious anemia virus (EIAV) are closely related lentiviruses that infect immune cells, but their pathogenesis differ. Localization to the cytosolic leaflet of the plasma membrane is critical for replication of both viruses. This localization is accomplished through the matrix (MA) domain of the Gag precursor protein. In HIV-1, association of MA to anionic membranes appears to be primarily driven by a linear cluster of basic residues in the MA domain and an N-myristoylation signal. Interestingly, the MA protein of EIAV does not contain either of ... Read More
19
Three-dimensional structure of mare diferric lactoferrin at 2.6 A resolution.
Journal of molecular biology
June 15, 1999
Volume 289, Issue 2 303-317 doi: 10.1006/jmbi.1999.2767
Sharma AK, Paramasivam M, Srinivasan A, Yadav MP, Singh TP.Lactoferrin is a monomeric glycoprotein with a molecular mass of approximately 80 kDa. The three-dimensional structure of mare diferric lactoferrin (mlf) has been determined at 2.6 A resolution. The protein crystallizes in the space group P 212121with a=85.2 A, b=99.5 A, c=103.1 A with a solvent content of 55 % (v/v). The structure was solved by the molecular replacement method using human diferric lactoferrin as the model. The structure has been refined using XPLOR to a final R -factor of 0.194 for all data in the 15-2.6 A resolution range. The amino acid sequence of mlf was determined using ... Read More
18
The unfolding thermodynamics of c-type lysozymes: a calorimetric study of the heat denaturation of equine lysozyme.
Journal of molecular biology
September 29, 1995
Volume 252, Issue 4 447-459 doi: 10.1006/jmbi.1995.0510
Griko YV, Freire E, Privalov G, van Dael H, Privalov PL.The energetics of the temperature-induced unfolding of equine lysozyme was studied calorimetrically and compared with that of two structurally homologous proteins: hen egg white lysozyme and alpha-lactalbumin. The structure of each of these proteins is characterized by the presence of a deep cleft that divides the molecule into two regions called the alpha and beta domains. In equine lysozyme and alpha-lactalbumin the latter domain specifically binds Ca2+. It is shown that, in contrast to hen egg white lysozyme in which the alpha and beta domains unfold as a single cooperative unit, in equine ... Read More
14
The interaction of equine lysozyme:oleic acid complexes with lipid membranes suggests a cargo off-loading mechanism.
Journal of molecular biology
March 19, 2010
Volume 398, Issue 2 351-361 doi: 10.1016/j.jmb.2010.03.012
Nielsen SB, Wilhelm K, Vad B, Schleucher J, Morozova-Roche LA, Otzen D.The normal function of equine lysozyme (EL) is the hydrolysis of peptidoglycan residues of bacterial cell walls. EL is closely related to alpha-lactalbumins with respect to sequence and structure and further possesses the calcium binding site of alpha-lactalbumins. Recently, EL multimeric complexes with oleic acids (ELOAs) were shown to possess tinctorial and morphological properties, similar to amyloidal aggregates, and to be cytotoxic. ELOA's interactions with phospholipid membranes appear to be central to its biological action, similar to human alpha-lactalbumin made lethal to tumor cells. ... Read More
12
Role of heme axial ligands in the conformational stability of the native and molten globule states of horse cytochrome c.
Journal of molecular biology
February 16, 1996
Volume 256, Issue 1 172-186 doi: 10.1006/jmbi.1996.0075
Hamada D, Kuroda Y, Kataoka M, Aimoto S, Yoshimura T, Goto Y.One unique aspect of cytochrome c folding concerns the involvement of the covalently attached heme group and its axial ligands. To elucidate the role of the ligands in stabilizing the native and molten globule states, we studied the conformational and thermodynamic features of the iron-free derivative of horse cyctochrome c (porphyrin-cytochrome c). At neutral pH, far-UV circular dichroism suggested that porphyrin-cytochrome c has native-like alpha-helices, whereas near-UV CD suggested that the side-chains are flexible. Its stability against heat or denaturants was much less than that of the i... Read More
11
Crystal structure of cleaved equine leucocyte elastase inhibitor determined at 1.95 A resolution.
Journal of molecular biology
August 20, 1992
Volume 226, Issue 4 1207-1218 doi: 10.1016/0022-2836(92)91062-t
Baumann U, Bode W, Huber R, Travis J, Potempa J.The crystal structure of active-site cleaved equine leucocyte elastase inhibitor, a member of the serpin superfamily, has been solved and refined to a crystallographic R-factor of 17.6% at 1.95 A resolution. Despite being an intracellular inhibitor with rather low sequence homology of 30% to human alpha 1-antichymotrypsin and alpha 1-proteinase inhibitor, the three-dimensional structures are very similar, with deviations only at the sites of insertions and few mobile secondary structure elements. The better resolution in comparison with the structures of other cleaved serpins allows a more pre... Read More
11
Independent nucleation and heterogeneous assembly of structure during folding of equine lysozyme.
Journal of molecular biology
June 17, 1999
Volume 289, Issue 4 1055-1073 doi: 10.1006/jmbi.1999.2741
Morozova-Roche LA, Jones JA, Noppe W, Dobson CM.The refolding of equine lysozyme from guanidinium chloride has been studied using hydrogen exchange pulse labelling in conjunction with NMR spectroscopy and stopped flow optical methods. The stopped flow optical experiments indicate that extensive hydrophobic collapse occurs rapidly after the initiation of refolding. Pulse labelling experiments monitoring nearly 50 sites within the protein have enabled the subsequent formation of native-like structure to be followed in considerable detail. They reveal that an intermediate having persistent structure within three of the four helices of the alph... Read More
11
Mechanism of translesion synthesis past an equine estrogen-DNA adduct by Y-family DNA polymerases.
Journal of molecular biology
June 9, 2007
Volume 371, Issue 5 1151-1162 doi: 10.1016/j.jmb.2007.06.009
Yasui M, Suzuki N, Liu X, Okamoto Y, Kim SY, Laxmi YR, Shibutani S.4-Hydroxyequilenin (4-OHEN)-dC is a major, potentially mutagenic DNA adduct induced by equine estrogens used for hormone replacement therapy. To study the miscoding property of 4-OHEN-dC and the involvement of Y-family human DNA polymerases (pols) eta, kappa and iota in that process, we incorporated 4-OHEN-dC into oligodeoxynucleotides and used them as templates in primer extension reactions catalyzed by pol eta, kappa and iota. Pol eta inserted dAMP opposite 4-OHEN-dC, accompanied by lesser amounts of dCMP and dTMP incorporation and base deletion. Pol kappa promoted base deletions as well as ... Read More
10
Structural characterisation and comparison of the native and A-states of equine lysozyme.
Journal of molecular biology
May 23, 1997
Volume 268, Issue 5 903-921 doi: 10.1006/jmbi.1997.0996
Morozova-Roche LA, Arico-Muendel CC, Haynie DT, Emelyanenko VI, Van Dael H, Dobson CM.Native state 1H NMR resonance assignments for 125 of the 129 residues of equine lysozyme have enabled measurement of the hydrogen exchange kinetics for over 60 backbone amide and three tryptophan indole hydrogen atoms in the native state. Native holo equine lysozyme hydrogen exchange protection factors are as large as 10(6), the most protected residues being located in elements of secondary structure. High exchange protection in the domain interface correlates with the binding of Ca2+ in this region. Equine lysozyme differs from most non-Ca2+ binding lysozymes in forming a highly populated par... Read More
10
Molten globule structure of equine beta-lactoglobulin probed by hydrogen exchange.
Journal of molecular biology
June 3, 2000
Volume 299, Issue 3 757-770 doi: 10.1006/jmbi.2000.3761
Kobayashi T, Ikeguchi M, Sugai S.The molten globule structure of equine beta-lactoglobulin has been inferred from the hydrogen exchange protection of the backbone amide protons. In order to make it possible to measure the hydrogen exchange kinetics of the individual backbone amide protons, the uniformly (15)N-labeled recombinant protein was expressed in Escherichia coli and the NMR peak assignment was obtained for most of the backbone protons. The chemical shift and NOE results obtained under the condition where the protein assumes the native structure are fully consistent with the known secondary structure of bovine beta-lac... Rate of intrachain contact formation in an unfolded protein: temperature and denaturant effects.
Journal of molecular biology
February 13, 2001
Volume 305, Issue 5 1161-1171 doi: 10.1006/jmbi.2000.4366
Hagen SJ, Carswell CW, Sjolander EM.We have measured the effect of temperature and denaturant concentration on the rate of intrachain diffusion in an unfolded protein. After photodissociating a ligand from the heme iron of unfolded horse cytochrome c, we use transient optical absorption spectroscopy to measure the time scale of the diffusive motions that bring the heme, located at His18, into contact with its native ligand, Met80. Measuring the rate at which this 62 residue intrachain loop forms under both folding and unfolding conditions, we find a significant effect of denaturant on the chain dynamics. The diffusion of the cha... Equilibrium and kinetics of the folding of equine lysozyme studied by circular dichroism spectroscopy.
Journal of molecular biology
October 8, 1998
Volume 283, Issue 1 265-277 doi: 10.1006/jmbi.1998.2100
Mizuguchi M, Arai M, Ke Y, Nitta K, Kuwajima K.The equilibrium unfolding and the kinetics of unfolding and refolding of equine lysozyme, a Ca2+-binding protein, were studied by means of circular dichroism spectra in the far and near-ultraviolet regions. The transition curves of the guanidine hydrochloride-induced unfolding measured at 230 nm and 292.5 nm, and for the apo and holo forms of the protein have shown that the unfolding is well represented by a three-state mechanism in which the molten globule state is populated as a stable intermediate. The molten globule state of this protein is more stable and more native-like than that of alp... Comparative analysis of the IgG heavy chain carbohydrate peptide.
Journal of molecular biology
December 28, 1967
Volume 30, Issue 3 555-558 doi: 10.1016/0022-2836(67)90369-5
Howell JW, Hood L, Sanders BG.No abstract available Structure and functional properties of chemically modified horse hemoglobin. I. Determination of the functional properties.
Journal of molecular biology
May 28, 1971
Volume 58, Issue 1 69-77 doi: 10.1016/0022-2836(71)90232-4
Simon SR, Arndt DJ, Konigsberg WH.No abstract available Identification and description of beta-structure in horse muscle acylphosphatase by nuclear magnetic resonance spectroscopy.
Journal of molecular biology
May 20, 1989
Volume 207, Issue 2 405-415 doi: 10.1016/0022-2836(89)90263-5
Saudek V, Wormald MR, Williams RJ, Boyd J, Stefani M, Ramponi G.Nuclear magnetic resonance spectra of acylphosphatase were searched for signs of beta-structure, i.e. characteristic nuclear Overhauser enhancement patterns displayed in the two-dimensional spectra, typical chemical shifts, coupling constants and slow 2H-H exchange. The results provided identification of the main-chain resonances of amino acid residues involved in the beta-structure. The full sequential assignment of this region was gained by identification of some amino acid spin systems and their alignment with the primary sequence. The assignment of the side-chains was virtually completed s... Structure and functional properties of chemically modified horse hemoglobin. II. X-ray studies.
Journal of molecular biology
May 28, 1971
Volume 58, Issue 1 79-88 doi: 10.1016/0022-2836(71)90233-6
Moffat JK.No abstract available The Immunochemical Difference Between Horse Oxy- and Deoxyhaemoglobin.
Journal of molecular biology
September 1, 1964
Volume 9 785-788 doi: 10.1016/s0022-2836(64)80184-4
REICHLIN M, BUCCI E, ANTONINI E, WYMAN J, ROSSI-FANELLI A.No abstract available Structure and function of haemoglobin. IV. A three-dimensional Fourier synthesis of horse deoxyhaemoglobin at 5.5 A resolution.
Journal of molecular biology
April 14, 1968
Volume 33, Issue 1 283-297 doi: 10.1016/0022-2836(68)90294-5
Bolton W, Cox JM, Perutz MF.No abstract available Interaction of GroEL with conformational states of horse cytochrome c.
Journal of molecular biology
October 4, 1996
Volume 262, Issue 4 575-587 doi: 10.1006/jmbi.1996.0536
Hoshino M, Kawata Y, Goto Y.GroEL interacts with proteins in denatured states and promotes their efficient folding. To understand the conformational features required for the substrate, we studied the interactions of GroEL with various derivatives of horse cytochrome c including porphyrin-cytochrome c, apo-cytochrome c, and the three fragments containing the heme group, i.e. fragments 1-65, 1-38 and 11-21. Size-exclusion chromatography was performed, taking advantage of the heme absorption of the fluorescence label. Under low-salt conditions, significant binding to GroEL was observed for porphyrin-cytochrome c, apo-cytoc... Interactions responsible for secondary structure formation during folding of equine beta-lactoglobulin.
Journal of molecular biology
January 25, 2007
Volume 367, Issue 4 1205-1214 doi: 10.1016/j.jmb.2007.01.053
Nakagawa K, Yamada Y, Fujiwara K, Ikeguchi M.Equine beta-lactoglobulin forms a compact intermediate at an acidic pH (A state). It also forms an expanded and helical conformation at low temperatures (C state). The structure of a single disulfide mutant C66A/C160A is similar to the A state in the presence of salts, while it is similar to the C state at low anion concentrations. We have investigated the temperature-dependent change in the secondary structure using circular dichroism and proline scanning mutagenesis. At low anion concentrations, the helical content increased linearly as temperature decreased. In the presence of salts, the A ... Identification and description of alpha-helical regions in horse muscle acylphosphatase by 1H nuclear magnetic resonance spectroscopy.
Journal of molecular biology
January 5, 1989
Volume 205, Issue 1 229-239 doi: 10.1016/0022-2836(89)90377-x
Saudek V, Atkinson RA, Williams RJ, Ramponi G.It has been proposed that combination of intraresidue, sequential and longer range nuclear Overhauser enhancements occurring in 1H nuclear magnetic resonance spectra of protein chains folded in a helix show a regular characteristic pattern. As a test case the spectra of horse muscle acylphosphatase were searched for this pattern together with other typical signs of a helical conformation (i.e. chemical shift, coupling constants and slow 2H-H exchange). Two amino acid sequences complying with these requirements were found. Just a few amino acid spin system assignments were then sufficient to lo...