LEADER 04528nam 2200613Ia 450 001 9910828832403321 005 20200520144314.0 010 $a1-61942-609-9 035 $a(CKB)2670000000160536 035 $a(EBL)3017834 035 $a(SSID)ssj0000692522 035 $a(PQKBManifestationID)11379621 035 $a(PQKBTitleCode)TC0000692522 035 $a(PQKBWorkID)10637151 035 $a(PQKB)11482809 035 $a(MiAaPQ)EBC3017834 035 $a(Au-PeEL)EBL3017834 035 $a(CaPaEBR)ebr10654805 035 $a(OCoLC)780443428 035 $a(EXLCZ)992670000000160536 100 $a20110224d2011 uy 0 101 0 $aeng 135 $aur|n|---||||| 181 $ctxt 182 $cc 183 $acr 200 00$aProtein structure /$fLauren M. Haggerty, editor 205 $a1st ed. 210 $aNew York $cNova Science Publishers$dc2011 215 $a1 online resource (256 p.) 225 0 $aProtein science and engineering 300 $aDescription based upon print version of record. 311 $a1-61209-656-5 320 $aIncludes bibliographical references and index. 327 $a""PROTEIN STRUCTURE ""; ""PROTEIN STRUCTURE ""; ""Contents ""; ""Preface ""; ""Misfolded Species Involved Regions Which Are Involved in an Early Folding Nucleus""; ""Abstract ""; ""Introduction""; ""Results and Discussion ""; ""Intersection of Experimentally Determined Amyloidogenic Regions with the Predicted Folding Nuclei ""; ""A Description of Globular Proteins with Experimentally Determined Amyloidogenic Regions ""; ""Intersection of Predicted Amyloidogenic Regions and Protected From Hydrogen/Deuterium Exchange with Experimentally Outlined Folding Nuclei "" 327 $a""Modeling of Folding of the Proteins with Swapped Domains """"Materials and Methods ""; ""Creation of the Database of Amyloidogenic Proteins ""; ""The Database of Proteins with Experimentally Outlined Folding Nucleus""; ""Prediction of Amyloidogenic Regions in Proteins""; ""Theoretical Search for Folding Nuclei ""; ""Calculation of I??-Values ""; ""Creation of a Database pf Swapped Proteins""; ""Predicting Protection of Amino Acid Residues From Hydrogen-Deuterium Exchange Using Amino Acid Sequence Only ""; ""Acknowledgments""; ""Funding ""; ""References "" 327 $a""Enzyme Immobilization: A Breakthrough in Enzyme Technology and Boon to Enzyme Based Industries """"Abstract ""; ""Introduction ""; ""Enzyme Immobilization, Proficient Tool of Enzyme Technology""; ""Types of Enzyme Immobilization ""; ""A. Physical ""; ""1) Entrapment within Cross-Linked Polymers ""; ""2) Adsorption""; ""3) Microencapsulation ""; ""B. Chemical ""; ""1) Cross-Linking ""; ""2) Covalent Attachment ""; ""Effect of Enzyme Immobilization on its Kinetic Properties ""; ""Optimum pH ""; ""Optimum Temperature""; ""Kinetic Parameters ""; ""Commercial Implications "" 327 $a""1) Enzymatic Synthesis of Aspartame """"2) Enzymic Production of L-Aspartic acid and L-Malic Acid""; ""3) Production of 6-Amino Penicillanic Acid by Immobilized Penicillin Amidase ""; ""4) Stereochemical Resolution of Racemic Amino Acids by Immobilized Aminoacylase: ""; ""5) Immobilized Glucose Isomerase in the Production of High Fructose Corn Syrup ""; ""6) Enzymic Synthesis of Acrylamide ""; ""7) Immobilized Lactase in the Hydrolysis of Lactose in Milk ""; ""Biosensors ""; ""Immobilization by Cross-Linking of Enzymes among Themselves without Any Support "" 327 $a""Structure-Based Development of Immobilization """"Summary and Conclusion ""; ""Future Perspectives ""; ""References ""; ""Three Approaches for Classifying Protein Tertiary Structures ""; ""Abstract ""; ""1. Introduction ""; ""2. Our Protein Classification Approaches ""; ""2.1. Protein Voxel Based Descriptor ""; ""2.2. Protein Ray Based Descriptor ""; ""2.3. Supervised Growing Neural Gas (SGNG)""; ""2.4. Support Vector Machines (SVM)""; ""2.5. Hidden Markov Model (HMM) ""; ""3. Experimental Results ""; ""Conclusion ""; ""References"" 327 $a""Common Structural Characteristics of Fibrous and Globular Proteins "" 410 0$aProtein Science and Engineering 606 $aProteins$xStructure 606 $aProteins 615 0$aProteins$xStructure. 615 0$aProteins. 676 $a612/.01575 701 $aHaggerty$b Lauren M$01637968 801 0$bMiAaPQ 801 1$bMiAaPQ 801 2$bMiAaPQ 906 $aBOOK 912 $a9910828832403321 996 $aProtein structure$93980087 997 $aUNINA