RESUMEN
It has been reported that the C-terminus of the second conserved region (C2) of the envelope glycoprotein gp120, encompassing peptide RSANFTDNAKTIIVQLNESVEIN (NTM), is important for infectivity and neutralization of the human immunodeficiency virus type 1 (HIV-1). It was also demonstrated that human natural anti-vasoactive intestinal peptide (VIP) antibodies reactive with this gp120 region play an important role in control of HIV disease progression. The bioinformatic analysis based on the time-frequency signal processing revealed non-obvious similarities between NTM and VIP. When tested against a battery of sera from 46 AIDS patients, these peptides, in spite of a significant difference in their primary structures, showed a similar reactivity profiles (r = 0.83). Presented results point out that similarity in the periodical pattern of some physicochemical properties in primary structures of peptides plays a significant role in determination of their immunological crossreactivity. Based on these findings, we propose this bioinformatic criterion be used for design of VIP/NTM peptide mimetics for prevention and treatment of HIV disease.
Asunto(s)
Proteína gp120 de Envoltorio del VIH/química , Péptidos/química , Péptidos/inmunología , Secuencia de Aminoácidos , Biología Computacional/métodos , Diseño de Fármacos , Anticuerpos Anti-VIH/sangre , Proteína gp120 de Envoltorio del VIH/genética , Infecciones por VIH/sangre , Infecciones por VIH/tratamiento farmacológico , Infecciones por VIH/prevención & control , Humanos , Imitación Molecular , Datos de Secuencia Molecular , Péptidos/genética , Alineación de Secuencia , Péptido Intestinal Vasoactivo/química , Péptido Intestinal Vasoactivo/inmunologíaRESUMEN
RBP16 is a mitochondrial Y-box protein from the parasitic protozoan Trypanosoma brucei that binds guide RNAs and ribosomal RNAs. It is comprised of an N-terminal cold-shock domain and a C-terminal domain rich in glycine and arginine residues, resembling the RGG RNA-binding motif. Arginine residues found within RGG domains are frequently asymmetrically dimethylated by a class of enzymes termed protein arginine methyltransferases (PRMTs). As Arg-93 of RBP16 exists in the context of a preferred sequence for asymmetric arginine dimethylation (G/FGGRGGG/F), we investigated whether modified arginines are present in native RBP16 by MALDI-TOF and post-source decay analyses. These analyses confirmed that Arg-93 is dimethylated. In addition, Arg-78 exists as an unmodified or as a monomethylated derivative, and Arg-85 is present in forms corresponding to the unmodified, di-, and tri-methylated state. While Arg-93 is apparently constitutively dimethylated, the methylation of Arg-78 and Arg-85 is mutually exclusive. Furthermore, whole cell extracts from procyclic form T. brucei are able to methylate bacterially expressed RBP16 (rRBP16), as well as endogenous proteins, in the presence of S-adenosyl-L-[methyl-3H]methionine. While assays of mitochondrial extracts suggest a small amount of PRMT may also be present in this subcellular compartment, the majority of trypanosome PRMT activity is extramitochondrial. We show that rRBP16 is methylated in trypanosome extracts through the action of a type I methyltransferase as well as serving as a substrate for heterologous mammalian type I PRMTs. In addition, we demonstrate the presence of type II PRMT activity in trypanosome cell extracts. These results suggest that protein arginine methylation is a common posttranslational modification in trypanosomes, and that it may regulate the function of RBP16.
Asunto(s)
Arginina/metabolismo , Mitocondrias/metabolismo , Procesamiento Proteico-Postraduccional , Proteínas Protozoarias , ARN Guía de Kinetoplastida/metabolismo , Proteínas de Unión al ARN/metabolismo , Trypanosoma brucei brucei/metabolismo , Animales , Espectrometría de Masas , Metilación , Proteína-Arginina N-Metiltransferasas/metabolismo , Edición de ARN , ARN Guía de Kinetoplastida/genética , Proteínas de Unión al ARN/genética , Trypanosoma brucei brucei/genética , Trypanosoma brucei brucei/crecimiento & desarrolloRESUMEN
The three-dimensional structure of the amaranth alpha-amylase inhibitor (AAI) adopts a knottin fold of abcabc topology. Upon binding to alpha-amylase, it adopts a more compact conformation characterized by an increased number of intramolecular hydrogen bonds, a decreased volume and in addition a trans to cis isomerization of Pro20. A systematic analysis of the 3-D structural databanks revealed that similar proteins and domains share with AAI the characteristic presence of proline residues, many of which are in a cis backbone conformation. As these proteins fulfil a variety of functional roles and are expressed in very different organisms, we conclude that the structure of the knottin fold, including the propensity of the cis bond, are the result of convergent evolution.
Asunto(s)
Amaranthus/enzimología , Cistina/química , Inhibidores Enzimáticos/metabolismo , Proteínas de Plantas/química , Proteínas de Plantas/metabolismo , alfa-Amilasas/metabolismo , Algoritmos , Sitios de Unión , Evolución Biológica , Análisis por Conglomerados , Bases de Datos de Proteínas , Disulfuros/química , Inhibidores Enzimáticos/química , Enlace de Hidrógeno , Modelos Moleculares , Proteínas de Plantas/clasificación , Proteínas de Plantas/fisiología , Prolina/química , Unión Proteica , Conformación Proteica , Pliegue de Proteína , Estructura Terciaria de Proteína , Semillas/química , Estereoisomerismo , Relación Estructura-Actividad , Inhibidores de Tripsina , alfa-Amilasas/antagonistas & inhibidores , alfa-Amilasas/clasificaciónRESUMEN
The major serine proteinase inhibitor from bell pepper (Capsicum annuum, paprika) seeds was isolated, characterized, and sequenced, and its disulfide bond topology was determined. PSI-1.2 is a 52-amino-acid-long, cysteine-rich polypeptide that inhibits both trypsin (K(i) = 4.6 x 10(-9) M) and chymotrypsin (K(i) = 1.1 x 10(-8) M) and is a circularly permuted member of the potato type II inhibitor family. Mature proteins of this family are produced from precursor proteins containing two to eight repeat units that are proteolytically cleaved within, rather than between, the repeats. In contrast, PSI-1.2 corresponds to a complete repeat that was predicted as the putative ancestral protein of the potato type II family. To our knowledge, this is the first case in which two proteins related to each other by circular permutation are shown to exist in the same organism and are expressed within the same organ. PSI-1.2 is not derived from any of the known precursors, and it contains a unique amphiphilic segment in one of its loops. A systematic comparison of the related precursor repeat-sequences reveals common evolutionary patterns that are in agreement with the ancestral gene-duplication hypothesis.
Asunto(s)
Capsicum/química , Inhibidores de Serina Proteinasa/aislamiento & purificación , Secuencia de Aminoácidos , Capsicum/genética , Quimotripsina/antagonistas & inhibidores , Disulfuros/química , Evolución Molecular , Inhibidores del Factor Xa , Cinética , Modelos Moleculares , Datos de Secuencia Molecular , Mutación , Filogenia , Alineación de Secuencia , Inhibidores de Serina Proteinasa/química , Trombina/antagonistas & inhibidores , Inhibidores de Tripsina/aislamiento & purificaciónRESUMEN
Single-chain derivatives of the 434 repressor containing one wild-type and one mutant DNA-binding domain recognize the general operator ACAA-6 base pairs-NNNN, where the ACAA operator subsite is contacted by the wild-type and the NNNN tetramer by the mutant domain. The DNA-binding specificities of several single-chain mutants were studied in detail and the optimal subsites of the mutant domains were determined. The characterized mutant domains were used as building units to obtain homo- and heterodimeric single-chain derivatives. The DNA-binding properties of these domain-shuffled derivatives were tested with a series of designed operators of NNNN-6 base pairs-NNNN type. It was found that the binding specificities of the mutant domains were generally maintained in the new environments and the binding affinities for the optimal DNA ligands were high (with K(d) values in the range of 10(-11)-10(-10) M). Considering that only certain sequence motifs in place of the six base pair spacer can support optimal contacts between the mutant domains and their subsites, the single-chain 434 repressor mutants are highly specific for a limited subset of 14 base pair long DNA targets.
Asunto(s)
Proteínas de Unión al ADN/química , Mutación , Proteínas Represoras/química , Secuencia de Bases , Sitios de Unión/genética , Proteínas de Unión al ADN/genética , Oligonucleótidos/química , Oligonucleótidos/genética , Oligonucleótidos/metabolismo , Regiones Operadoras Genéticas , Unión Proteica , Estructura Terciaria de Proteína , Proteínas Represoras/genética , Proteínas Represoras/metabolismo , Especificidad por Sustrato , Proteínas ViralesRESUMEN
The PvuII restriction endonuclease has been converted from its natural homodimeric form into a single polypeptide chain by tandemly linking the two subunits through a short peptide linker. The arrangement of the single-chain PvuII (sc PvuII) is (2-157)-GlySerGlyGly-(2-157), where (2-157) represents the amino acid residues of the enzyme subunit and GlySerGlyGly is the peptide linker. By introducing the corresponding tandem gene into Escherichia coli, PvuII endonuclease activity could be detected in functional in vivo assays. The sc enzyme was expressed at high level as a soluble protein. The purified enzyme was shown to have the molecular mass expected for the designed sc protein. Based on the DNA cleavage patterns obtained with different substrates, the cleavage specificity of the sc PvuII is indistinguishable from that of the wild-type (wt) enzyme. The sc enzyme binds specifically to the cognate DNA site under non-catalytic conditions, in the presence of Ca2+, with the expected 1:1 stoichiometry. Under standard catalytic conditions, the sc enzyme cleaves simultaneously the two DNA strands in a concerted manner. Steady-state kinetic parameters of DNA cleavage by the sc and wt PvuII showed that the sc enzyme is a potent, but somewhat less efficient catalyst; the k(cat)/K(M) values are 1.11 x 10(9) and 3.50 x 10(9) min(-1) M(-1) for the sc and wt enzyme, respectively. The activity decrease is due to the lower turnover number and to the lower substrate affinity. The sc arrangement provides a facile route to obtain asymmetrically modified heterodimeric enzymes.
Asunto(s)
Desoxirribonucleasas de Localización Especificada Tipo II/química , Desoxirribonucleasas de Localización Especificada Tipo II/metabolismo , Ingeniería de Proteínas , Proteus vulgaris/enzimología , Secuencia de Aminoácidos , Secuencia de Bases , Calcio/metabolismo , Catálisis , ADN/genética , ADN/metabolismo , Proteínas de Unión al ADN/química , Proteínas de Unión al ADN/genética , Proteínas de Unión al ADN/metabolismo , Desoxirribonucleasas de Localización Especificada Tipo II/genética , Dimerización , Escherichia coli , Cinética , Modelos Moleculares , Mutación/genética , Unión Proteica , Estructura Cuaternaria de Proteína , Subunidades de Proteína , Proteus vulgaris/genética , Solubilidad , Especificidad por Sustrato , TermodinámicaRESUMEN
An artificial neural network (ANN) solution is described for the recognition of domains in protein sequences. A query sequence is first compared to a reference database of domain sequences by use of and the output data, encoded in the form of six parameters, are forwarded to feed-forward artificial neural networks with six input and six hidden units with sigmoidal transfer function. The recognition is based on the distribution of scores precomputed for the known domain groups in a database versus database comparison. Applications to the prediction of function are discussed.
Asunto(s)
Biología Computacional/métodos , Redes Neurales de la Computación , Estructura Terciaria de Proteína/fisiología , Análisis de Secuencia de Proteína/métodos , Bases de Datos FactualesRESUMEN
We studied the interaction between a synthetic peptide (sequence Ac-GXGGFGGXGGFXGGXGG-NH(2), where X = arginine, N(omega),N(omega)-dimethylarginine, DMA, or lysine) corresponding to residues 676-692 of human nucleolin and several DNA and RNA substrates using double filter binding, melting curve analysis and circular dichroism spectroscopy. We found that despite the reduced capability of DMA in forming hydrogen bonds, N(omega),N(omega)-dimethylation does not affect the strength of the binding to nucleic acids nor does it have any effect on stabilization of a double-stranded DNA substrate. However, circular dichroism studies show that unmethylated peptide can perturb the helical structure, especially in RNA, to a much larger extent than the DMA peptide.
Asunto(s)
Arginina/metabolismo , Glicina/metabolismo , Nitroarginina/metabolismo , Ácidos Nucleicos/metabolismo , Fosfoproteínas/química , Fosfoproteínas/metabolismo , Procesamiento Proteico-Postraduccional , Proteínas de Unión al ARN/química , Proteínas de Unión al ARN/metabolismo , Secuencia de Aminoácidos , Animales , Secuencia de Bases , Dicroismo Circular , ADN/química , ADN/genética , ADN/metabolismo , Bases de Datos como Asunto , Duplicado del Terminal Largo de VIH/genética , Humanos , Enlace de Hidrógeno , Metilación , Modelos Moleculares , Datos de Secuencia Molecular , Nitroarginina/química , Conformación de Ácido Nucleico , Desnaturalización de Ácido Nucleico , Ácidos Nucleicos/química , Ácidos Nucleicos/genética , Fragmentos de Péptidos/síntesis química , Fragmentos de Péptidos/química , Fragmentos de Péptidos/metabolismo , Fosfatos/química , Fosfatos/metabolismo , Unión Proteica , ARN/química , ARN/genética , ARN/metabolismo , Termodinámica , NucleolinaRESUMEN
The degree of similarity of two protein three-dimensional structures is usually measured with the root-mean-square distance between equivalent atom pairs. Such a similarity measure depends on the dimension of the proteins, that is, on the number of equivalent atom pairs. The present communication presents a simple procedure to make the root-mean-square distances between pairs of three-dimensional structures independent of their dimensions. This normalization may be useful in evolutionary and fold classification studies as well as in simple comparisons between different structural models.
Asunto(s)
Modelos Moleculares , Proteínas/química , Algoritmos , Animales , Bases de Datos Factuales , Humanos , Conformación Proteica , Estructura Terciaria de ProteínaRESUMEN
SBASE 8.0 is the eighth release of the SBASE library of protein domain sequences that contains 294 898 annotated structural, functional, ligand-binding and topogenic segments of proteins, cross-referenced to most major sequence databases and sequence pattern collections. The entries are clustered into over 2005 statistically validated domain groups (SBASE-A) and 595 non-validated groups (SBASE-B), provided with several WWW-based search and browsing facilities for online use. A domain-search facility was developed, based on non-parametric pattern recognition methods, including artificial neural networks. SBASE 8.0 is freely available by anonymous 'ftp' file transfer from ftp.icgeb.trieste.it. Automated searching of SBASE can be carried out with the WWW servers http://www.icgeb.trieste.it/sbase/ and http://sbase.abc. hu/sbase/.
Asunto(s)
Bases de Datos Factuales , Proteínas , Sitios de Unión , Servicios de Información , Internet , Estructura Terciaria de Proteína , Proteínas/química , Alineación de SecuenciaRESUMEN
Single-chain repressor RR(Tres) is a derivative of bacteriophage 434 repressor, which contains covalently dimerized DNA-binding domains (amino acids 1-69) of the phage 434 repressor. In this single-chain molecule, the wild type domain R is connected to the mutant domain R(TRES) by a recombinant linker in a head-to-tail arrangement. The DNA-contacting amino acids of R(TRES) at the -1, 1, 2, and 5 positions of the a3 helix are T, R, E, S respectively. By using a randomized DNA pool containing the central sequence -CATACAAGAAAGNNNNNNTTT-, a cyclic,in vitro DNA-binding site selection was performed. The selected population was cloned and the individual members were characterized by determining their binding affinities to RR(Tres) The results showed that the optimal operators contained the TTAC or TTCC sequences in the underlined positions as above, and that the Kd values were in the 1 x 10(-12) mol/L-1 x 10(11) mol/L concentration range. Since the affinity of the natural 434 repressor to its natural operator sites is in the 1 x 10(-9) mol/L range, the observed binding affinity increase is remarkable. It was also found that binding affinity was strongly affected by the flanking bases of the optimal tetramer binding sites, especially by the base at the 5' position. We constructed a new homodimeric single-chain repressor R(TRES)R(TRES) and its DNA-binding specificity was tested by using a series of new operators designed according to the recognition properties previously determined for the R(TREs) domain. These operators containing the consensus sequenceGTAAGAAARNTTACN orGGAAGAAARNTTCCN (R is A or G) were recognized by R(TRES)R(TRES) specifically, and with high binding affinity. Thus, by using a combination of random selection and rational design principles, we have discovered novel, high affinity protein-DNA interactions with new specificity. This method can potentially be used to obtain new binding specificity for other DNA-binding proteins.
RESUMEN
SUMMARY: A simple heuristic scoring method is described for assigning sequences to known domain types based on BLAST search outputs. The scoring is based on the score distribution of the known domain groups determined from a database versus database comparison and is directly applicable to BLAST output processing.
Asunto(s)
Modelos Estadísticos , Estructura Terciaria de Proteína , Programas Informáticos , Biología Computacional , Bases de Datos Factuales , Internet , Proteínas/química , Proteínas/genética , Alineación de Secuencia/estadística & datos numéricosRESUMEN
UNLABELLED: A WWW server is described for creating 3D models of canonical or bent DNA starting from sequence data. Predicted DNA trajectory is first computed based on a choice of di- and tri-nucleotide models (M.G. Munteanu et al., Trends Biochem. Sci. 23, 341-347, 1998); an atomic model is then constructed and optionally energy-minimized with constrained molecular dynamics. The data are presented as a standard PDB file, directly viewable on the user's PC using any molecule manipulation program. AVAILABILITY: The model.it server is freely available at http://www.icgeb.trieste.it/dna/ CONTACT: kristian@icgeb.trieste.it; pongor@icgeb.trieste.it SUPPLEMENTARY INFORMATION: a series of help files is available at the above address.
Asunto(s)
ADN/química , Internet , Modelos Moleculares , Conformación de Ácido Nucleico , Programas Informáticos , Secuencia de Bases , Biología Computacional , ADN/genética , ADN de Plantas/química , ADN de Plantas/genética , Bases de Datos Factuales , Regiones Promotoras Genéticas , Alineación de Secuencia/estadística & datos numéricos , Zea mays/genéticaRESUMEN
SBASE 7.0 is the seventh release of the SBASE protein domain library sequences that contains 237 937 annotated structural, functional, ligand-binding and topogenic segments of proteins, cross-referenced to all major sequence databases and sequence pattern collections. The entries are clustered into over 1811 groups and are provided with two WWW-based search facilities for on-line use. SBASE 7.0 is freely available by anonymous 'ftp' file transfer from ftp.icgeb. trieste.it. Automated searching of SBASE with BLAST can be carried out with the WWW servers http://www.icgeb.trieste.it/sbase/and http://sbase.abc.hu/sbase/
Asunto(s)
Sistemas de Administración de Bases de Datos , Bases de Datos Factuales , Proteínas/química , Secuencia de Aminoácidos , InternetRESUMEN
BACKGROUND: alpha-Amylases constitute a family of enzymes that catalyze the hydrolysis of alpha-D-(1,4)-glucan linkages in starch and related polysaccharides. The Amaranth alpha-amylase inhibitor (AAI) specifically inhibits alpha-amylases from insects, but not from mammalian sources. AAI is the smallest proteinaceous alpha-amylase inhibitor described so far and has no known homologs in the sequence databases. Its mode of inhibition of alpha-amylases was unknown until now. RESULTS: The crystal structure of yellow meal worm alpha-amylase (TMA) in complex with AAI was determined at 2.0 A resolution. The overall fold of AAI, its three-stranded twisted beta sheet and the topology of its disulfide bonds identify it as a knottin-like protein. The inhibitor binds into the active-site groove of TMA, blocking the central four sugar-binding subsites. Residues from two AAI segments target the active-site residues of TMA. A comparison of the TMA-AAI complex with a modeled complex between porcine pancreatic alpha-amylase (PPA) and AAI identified six hydrogen bonds that can be formed only in the TMA-AAI complex. CONCLUSIONS: The binding of AAI to TMA presents a new inhibition mode for alpha-amylases. Due to its unique specificity towards insect alpha-amylases, AAI might represent a valuable tool for protecting crop plants from predatory insects. The close structural homology between AAI and 'knottins' opens new perspectives for the engineering of various novel activities onto the small scaffold of this group of proteins.
Asunto(s)
Inhibidores Enzimáticos/química , Proteínas de Insectos/química , Proteínas de Plantas/química , alfa-Amilasas/antagonistas & inhibidores , alfa-Amilasas/química , Animales , Dominio Catalítico , Cristalografía por Rayos X , Inhibidores Enzimáticos/metabolismo , Inhibidores Enzimáticos/farmacología , Proteínas de Insectos/antagonistas & inhibidores , Proteínas de Insectos/metabolismo , Modelos Moleculares , Proteínas de Plantas/metabolismo , Proteínas de Plantas/farmacología , Conformación Proteica , Tenebrio/enzimología , alfa-Amilasas/metabolismoRESUMEN
A novel single-chain (sc) protein framework containing covalently dimerized DNA-binding domains (DBD) of the phage 434 repressor was used to construct combinatorial mutant libraries in order to isolate mutant DBDs with altered specificities. The library members contain one wild-type DBD and one mutant domain with randomized amino acids in the DNA-contacting region. Based on previous studies, the mutant sc derivatives are expected to recognize a general ACAA-6 bp-NNNN sequence, where ACAA is contacted by the wild-type and NNNN by the mutant domain. In principle, any sequence can stand for NNNN and serve as a selection target. Here an in vivo library screening method was used to isolate mutant sc repressors that interact with an asymmetric operator containing the TTAA target. Several mutants showed high affinity in vitro binding to operators containing the target and strong (up to 80-fold) preference for the TTAA target over the wild-type TTGT. Specificity studies revealed that certain mutants bound with substantially higher affinities (K(d) approximately 10(-11)M) to operators containing the TTAC sequence, a close homolog of the TTAA target. Thus, we have fortuitously isolated mutant sc repressors that show up to a several hundred-fold preference for TTAC over TTGT.
Asunto(s)
ADN/genética , Mutación , Proteínas Represoras/genética , Proteínas Represoras/metabolismo , Secuencia de Aminoácidos , Secuencia de Bases , Sitios de Unión , Huella de ADN , Proteínas de Unión al ADN/metabolismo , Escherichia coli/genética , Cinética , Datos de Secuencia Molecular , Biblioteca de Péptidos , Fenotipo , Unión Proteica , Homología de Secuencia de Ácido Nucleico , Proteínas ViralesRESUMEN
The isolated N-terminal 1-69 domain of the 434-phage repressor, R69, and its covalently linked (head-to-tail and tail-to-tail) dimers have been studied by differential scanning microcalorimetry (DSC) and CD. At neutral solvent conditions the R69 domain maintains its native structure, both in isolated form and within the dimers. The stability of the domain depends highly upon pH within the acidic range, thus at pH 2 and low ionic strength R69 is already partially unfolded at room temperature. The thermodynamic parameters of unfolding calculated from the DSC data are typical for small globular proteins. At neutral pH and moderate ionic strength, the domains of the dimers behave as two independent units with unfolding parameters similar to those of the isolated domain, which means that linking two R69 domains, either by a long peptide linker or by a designed C-terminal disulfide bridge, does not induce any cooperation between them.
Asunto(s)
Proteínas Represoras/química , Rastreo Diferencial de Calorimetría , Dicroismo Circular , Dimerización , Estabilidad de Medicamentos , Concentración de Iones de Hidrógeno , Concentración Osmolar , Conformación Proteica , Pliegue de Proteína , Termodinámica , Proteínas ViralesRESUMEN
alpha-Amylase inhibitor (AAI), a 32-residue miniprotein from the Mexican crop plant amaranth (Amaranthus hypochondriacus), is the smallest known alpha-amylase inhibitor and is specific for insect alpha-amylases (Chagolla-Lopez, A., Blanco-Labra, A., Patthy, A., Sanchez, R., and Pongor, S. (1994) J. Biol. Chem. 269, 23675-23680). Its disulfide topology was confirmed by Edman degradation, and its three-dimensional solution structure was determined by two-dimensional 1H NMR spectroscopy at 500 MHz. Structural constraints (consisting of 348 nuclear Overhauser effect interproton distances, 8 backbone dihedral constraints, and 9 disulfide distance constraints) were used as an input to the X-PLOR program for simulated annealing and energy minimization calculations. The final set of 10 structures had a mean pairwise root mean square deviation of 0.32 A for the backbone atoms and 1.04 A for all heavy atoms. The structure of AAI consists of a short triple-stranded beta-sheet stabilized by three disulfide bonds, forming a typical knottin or inhibitor cystine knot fold found in miniproteins, which binds various macromolecular ligands. When the first intercystine segment of AAI (sequence IPKWNR) was inserted into a homologous position of the spider toxin Huwentoxin I, the resulting chimera showed a significant inhibitory activity, suggesting that this segment takes part in enzyme binding.
Asunto(s)
Inhibidores Enzimáticos/química , Magnoliopsida/química , alfa-Amilasas/antagonistas & inhibidores , Secuencia de Aminoácidos , Sustitución de Aminoácidos , Espectroscopía de Resonancia Magnética , Modelos Moleculares , Datos de Secuencia Molecular , Mapeo Peptídico , Conformación Proteica , Homología de Secuencia de AminoácidoRESUMEN
RESULTS: A WWW server for protein domain homology prediction, based on BLAST search and a simple data-mining algorithm (Hegyi,H. and Pongor,S. (1993) Comput. Appl. Biosci., 9, 371-372), was constructed providing a tabulated list and a graphic plot of similarities. AVAILABILITY: http://www.icgeb.trieste.it/domain. Mirror site is available at http://sbase.abc.hu/domain. A standalone programme will be available on request. SUPPLEMENTARY INFORMATION: A series of help files is available at the above addresses.