01780nas a2200193   4500008004100000022001400041245017000055210006900225260006700294300001200361490000700373520095200380100002901332700002601361700002501387700002701412700001901439856012801458       2013                        eng d  a1744-309100aCloning, overexpression, crystallization and preliminary X-ray crystallographic analysis of a slow-processing mutant of penicillin G acylase from Kluyvera citrophila0 aCloning overexpression crystallization and preliminary Xray crys  a111 RIVER ST, HOBOKEN 07030-5774, NJ USAbWILEY-BLACKWELLcAUG  a925-9290 v693 a<p>{Kluyvera citrophila penicillin G acylase (KcPGA) has recently attracted increased attention relative to the well studied and commonly used Escherichia coli PGA (EcPGA) because KcPGA is more resilient to harsh conditions and is easier to immobilize for the industrial hydrolysis of natural penicillins to generate the 6-aminopenicillin (6-APA) nucleus, which is the starting material for semi-synthetic antibiotic production. Like other penicillin acylases, KcPGA is synthesized as a single-chain inactive pro-PGA, which upon autocatalytic processing becomes an active heterodimer of alpha and beta chains. Here, the cloning of the pac gene encoding KcPGA and the preparation of a slow-processing mutant precursor are reported. The purification, crystallization and preliminary X-ray analysis of crystals of this precursor protein are described. The protein crystallized in two different space groups, P1, with unit-cell parameters a = 54.0</p>1 aVarshney, Nishant, Kumar1 aRamasamy, Sureshkumar1 aBrannigan, James, A.1 aWilkinson, Anthony, J.1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/cloning-overexpression-crystallization-and-preliminary-x-ray-crystallographic-analysis-000635nas a2200193   4500008004100000022001400041245007400055210006900129260000800198300000900206490000700215653001300222653002100235653001300256100002500269700002600294700001900320856010200339       2014                        eng d  a2053-273300aChickpea Kunitz Inhibitor: a mechanistic basis for trypsin inhibition0 aChickpea Kunitz Inhibitor a mechanistic basis for trypsin inhibi  cMAR  aC2710 v7010aChickpea10aKunitz Inhibitor10aProtease1 aBendre, Ameya, Dipak1 aRamasamy, Sureshkumar1 aSuresh, C., G.  uhttps://library.ncl.res.in/content/chickpea-kunitz-inhibitor-mechanistic-basis-trypsin-inhibition00626nas a2200181   4500008004100000022001400041245008600055210006900141260000800210300001000218490000700228653002500235653000900260653002200269100001700291700002600308856011000334       2014                        eng d  a2053-273300aCrystal structure of AtGet3 Delta L, a chloroplast Get3 from Arabidopsis thaliana0 aCrystal structure of AtGet3 Delta L a chloroplast Get3 from Arab  cMAY  aC11790 v7010aArabidopsis thaliana10aGet310aprotein targeting1 aManu, M., S.1 aRamasamy, Sureshkumar  uhttps://library.ncl.res.in/content/crystal-structure-atget3-delta-l-chloroplast-get3-arabidopsis-thaliana02696nas a2200301   4500008004100000022001400041245016000055210006900215260010600284300000900390490000700399520155800406653001301964653001801977653002801995653002902023653001502052653002402067100002402091700002002115700001902135700002002154700002202174700002302196700002602219700002002245856012902265       2016                        eng d  a0965-174800aCharacterization of two coleopteran alpha-amylases and molecular insights into their differential inhibition by synthetic alpha-amylase inhibitor, acarbose0 aCharacterization of two coleopteran alphaamylases and molecular   aTHE BOULEVARD, LANGFORD LANE, KIDLINGTON, OXFORD OX5 1GB, ENGLANDbPERGAMON-ELSEVIER SCIENCE LTDcJUL  a1-110 v743 a<p>Post-harvest insect infestation of stored grains makes them unfit for human consumption and leads to severe economic loss. Here, we report functional and structural characterization of two coleopteran alpha-amylases viz. Callosobruchus chinensis alpha-amylase (CcAmy) and Tribolium castaneum alpha-amylase (TcAmy) along with their interactions with proteinaceous and non-proteinaceous alpha-amylase inhibitors. Secondary structural alignment of CcAmy and TcAmy with other coleopteran alpha-amylases revealed conserved motifs, active sites, di-sulfide bonds and two point mutations at spatially conserved substrate or inhibitor binding sites. Homology modeling and molecular docking showed structural differences between these two enzymes. Both the enzymes had similar optimum pH values but differed in their optimum temperature. Overall, pattern of enzyme stabilities were similar under various temperature and pH conditions. Further, CcAmy and TcAmy differed in their substrate affinity and catalytic efficiency towards starch and amylopectin. HPLC analysis detected common amylolytic products like maltose and maltotriose while glucose and malto-tetrose were unique in CcAmy and TcAmy catalyzed reactions respectively. At very low concentrations, wheat alpha-amylase inhibitor was found to be superior over the acarbose as far as complete inhibition of amylolytic activities of CcAmy and TcAmy was concerned. Mechanism underlying differential amylolytic reaction inhibition by acarbose was discussed. (C) 2016 Elsevier Ltd. All rights reserved.</p>10aAcarbose10aalpha-amylase10aalpha-amylase inhibitor10aCallosobruchus chinensis10aColeoptera10aTribolium castaneum1 aChannale, Sonal, M.1 aBhide, Amey, J.1 aYadav, Yashpal1 aKashyap, Garima1 aPawar, Pankaj, K.1 aMaheshwari, V., L.1 aRamasamy, Sureshkumar1 aGiri, Ashok, P.  uhttps://library.ncl.res.in/content/characterization-two-coleopteran-alpha-amylases-and-molecular-insights-their-differential02295nas a2200217   4500008004100000022001400041245007400055210006900129260000800198300001400206490000700220520158900227100002301816700002601839700002101865700002601886700001801912700002301930700002101953856010301974       2019                        eng d  a1744-683X00aCore-composite mediated separation of diverse nanoparticles to purity0 aCorecomposite mediated separation of diverse nanoparticles to pu  cOCT  a7787-77940 v153 a<p>A generalized method for sorting nanoparticles based on their cores does not exist; it is an immediate necessity, and an approach incorporating cost-effectiveness and biocompatibility is in demand. Therefore, an efficient method for the separation of various mixed core-compositions or dissimilar metallic nanoparticles to their pure forms at the nano-bio interface was developed. Various simple core-combinations of monodispersed nanoparticles with dual cores, including silver plus gold, iron oxide plus gold and platinum plus gold, to the complex three-set core-combinations of platinum plus gold plus silver and platinum plus iron plus gold were sorted using step-gradient centrifugation in a sucrose suspension. Viscosity mediated differential terminal velocities of the nanoparticles permitted diversified dragging at different gradients allowing separation. Stability, purity and properties of the nanoparticles during separation were evaluated based on visual confirmation and by employing advanced instrumentations. Moreover, theoretical studies validated our experimental observations, revealing the roles of various parameters, such as the viscosity of sucrose, the density of the particles and the velocity and duration of centrifugation, involved during the separation process. This remarkably rapid, cost-efficient and sustainable strategy can be adapted to separate other cores of nanoparticles for various biomedical research purposes, primarily to understand nanoparticle induced toxicity and particle fate and transformations in natural biotic environments.</p>
1 aBhatt, Chandra, S.1 aNagaraj, Bharathkumar1 aGhosh, Deepanjan1 aRamasamy, Sureshkumar1 aThapa, Ranjit1 aMarpu, Sreekar, B.1 aSuresh, Anil, K.  uhttps://library.ncl.res.in/content/core-composite-mediated-separation-diverse-nanoparticles-purity