Download Biocatalyst Design for Stability and Specificity by Michael E. Himmel, George Georgiou PDF

By Michael E. Himmel, George Georgiou

content material: results of mutations on thermodynamic homes of proteins / Julian M. Sturtevant --
Contribution of hydrogen bonding and the hydrophobic impact to conformational balance of ribonuclease T1 / C. Nick speed, Ketan Gajiwala, and Bret A. Shirley --
Protein constitution and balance evaluate through round dichroism spectroscopy / Mark C. Manning --
Structure-function dating of hyperthermophilic enzymes / Rainer Jaenicke --
Psychrophilic proteinases from Atlantic cod / J.B. Bjarnason, B. Asgeirsson, and J.W. Fox --
Thermal and pH tension in thermal denaturation of Trichoderma reesei Cellobiohydrolase I : helping proof for a two-transition version / John O. Baker and Michael E. Himmel --
Recombinant protein stabilization via engineered metal-chelating websites / Pablo Umaña, James T. Kellis, Jr., and Frances H. Arnold --
Engineering nonaqueous solvent-compatible enzymes / Frances H. Arnold, Keqin Chen, Chara Economou, Wayne Chen, Pascal Martinez, Kyung Pyo Yoon, and Mariana Van Dam --
Mutational results on inclusion physique formation / Ronald Wetzel and Boris A. Chrunyk --
Characterization and refolding of [beta]-lactamase inclusion our bodies in Escherichia coli / Pascal Valax and George Georgiou --
Participation of GroE warmth surprise proteins in polypeptide folding / Anthony A. Gatenby, Gail ok. Donaldson, François Baneyx, George H. Lorimer, Paul V. Viitanen, and Saskia M. van der Vies --
Cosolvent results on refolding and aggregation / Jeffrey L. Cleland and Daniel I.C. Wang --
Facilitation of protein folding and the reversibility of denaturation / P.M. Horowitz --
synthetic bifunctional enzymes : a device to enhance consecutive enzyme reactions and mobilephone metabolism / Leif Bülow --
Proteins designed for adherence to cellulose / Edgar Ong, Jeffrey M. Greenwood, Neil R. Gilkes, Robert C. Miller, Jr., R. Anthony J. Warren, and Douglas G. Kilburn --
amendment of regulatory verbal exchange in aspartate transcarbamoylase / M.E. Wales, C.J. Strang, R. Swanson, and J.R. Wild --
C₁-tetrahydrofolate synthase : dissection of energetic web site and area constitution via protein engineering / Anice E. Thigpen, Charles ok. Barlowe, and Dean R. Appling --
houses of local and site-mutagenized cellobiohydrolase II / C. Barnett, L. Sumner, R. Berka, S. Shoemaker, H. Berg, M. Gritzali, and R. Brown --
Recombinant [beta]-glucosidase of Trichoderma reesei / Tim Fowler --
Structure-function relationships in cellulase genes / David B. Wilson --
Clostridium thermocellum cellulosome : new mechanistic inspiration for cellulose degradation / J.H. David Wu --
Protein chemical cross-linking : implications for protein stabilization / Shan S. Wong, Michael Losiewicz, and Lee-Jun C. Wong --
Glutaraldehyde cross-linking : quickly and gradual modes / Timothy J.A. Johnson --
Chemical amendment : impact on enzyme actions and stabilities / A. Sadana and R.R. Raju --
Cross-linking strategies : purposes to enzyme and protein stabilization and bioconjugate instruction / Munishwar N. Gupta.

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Extra resources for Biocatalyst Design for Stability and Specificity

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5 kcal/mole was used for the correction of the Ser 17 Ala data in Table IV. , the mutants were more stable than wild type RNase T l . 1 kcal/mole for the Asn 81 Ala mutant that potentially removes three hydrogen bonds. 3 kcal/mole. Thus, we think the A(AG) values given in the last two columns in Table IV are due mainly to changes in the hydrogen bonding in the mutants. The results in Table IV cannot be interpreted with any certainty until three-dimensional structures are available for the mutant proteins.

Matthews, H. Nicholson, W. J. Becktel, Proc. Nat. Acad. Sci. A. 84, 6663 (1987). ; ACS Symposium Series; American Chemical Society: Washington, DC, 1993. 32 25. 26. 27. 28. ch002 29. 30. 31. 32. 33. 34. 35. 36. 37. 38. 39. 40. 41. 42. 43. 44. 45. 46. 47. 48. 49. 50. 51. 52. 53. 54. 55. 56. 57. 58. 59. 60. 61. 62. 63. BIOCATALYST DESIGN FOR STABILITY AND SPECIFICITY F. M. Richards, Ann. Rev. Biophys. Bioeng. 6, 151 (1977). E. J. Cohn and J. T. Edsall, Proteins, Amino Acids, and Peptides (Hafner Publishing, New York, 1965) p.

0). 0. At even lower pH values, the overall concentration increased to substantial levels (30 to 90% of initial protein at pH 1 to 4). The effect of pH on specific proteolytic activity of fibrolase was evaluated over the pH range 1 to 10 using azocasein and insulin Β-chain substrates (Figure 3). 0), no significant change in proteolytic activity offibrolasewas observed. 0, the data suggested a slight loss of activity. This decrease was greater for the azocasein substrate relative to the insulin B-chain substrate.

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