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Titlebook: Chemical Aspects of Enzyme Biotechnology; Fundamentals Thomas O. Baldwin,Frank M. Raushel,A. Ian Scott Book 1990 Springer Science+Business

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書目名稱Chemical Aspects of Enzyme Biotechnology
副標(biāo)題Fundamentals
編輯Thomas O. Baldwin,Frank M. Raushel,A. Ian Scott
視頻videohttp://file.papertrans.cn/225/224283/224283.mp4
叢書名稱Industry-University Cooperative Chemistry Program Symposia
圖書封面Titlebook: Chemical Aspects of Enzyme Biotechnology; Fundamentals Thomas O. Baldwin,Frank M. Raushel,A. Ian Scott Book 1990 Springer Science+Business
描述The Industry-University Cooperative Chemistry Program has sponsored seven previous international symposia covering a wide variety of topics of interest to industrial and academic chemists. The eighth IUCCP symposium, held March 19-22, 1990, at Texas A&M University, represents a deviation from the former symposia, in that it is the first of a two-symposium series dedicated to the rapidly moving new field of industrial biochemistry that has beco~e known as biotechnology. Biotechnology is really not a new discipline, but rather is a term coined to describe the new and exciting commercial applications of biochemistry. The development of the field of biotechnology is a direct result of recombinant DNA technology, which began in earnest about 15 years ago. Today, we can routinely do experiments that were inconceivable in the early 1970‘s. Only comparatively simple technology available even in small laboratories is required to synthesize a gene and from it, to produce vast amounts of biological materials of enormous commercial value. These technical developments and others have stimulated increased activities in the field of enzyme biotechnology, using enzymes to catalyze "unnatural" reac
出版日期Book 1990
關(guān)鍵詞Amino acid; Coenzym; DNA; Glutamin; biochemistry; enzymes
版次1
doihttps://doi.org/10.1007/978-1-4757-9637-7
isbn_softcover978-1-4757-9639-1
isbn_ebook978-1-4757-9637-7
copyrightSpringer Science+Business Media New York 1990
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https://doi.org/10.1007/978-1-4302-0564-7hich is required for function. The past three decades have seen tremendous advances in our understanding of the processes of transcription and translation, however, rather little is known about the details of how the amino sequence of a protein directs the rapid and efficient folding to the native conformation.
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Increasing Enzyme Stabilitying curves. Estimates of the conformational stability based on urea unfolding curves are designated ΔG(H.O), and estimates from thermal unfolding curves are designated ΔG(25°C). In the first part of this article, we describe how to measure ΔG(H.O) and ΔG(25°C).
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