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Titlebook: NMR Applications in Biopolymers; J. W. Finley,S. J. Schmidt,A. S. Serianni Book 1990 Plenum Press, New York 1990 Nucleotide.Oligosaccharid

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書目名稱NMR Applications in Biopolymers
編輯J. W. Finley,S. J. Schmidt,A. S. Serianni
視頻videohttp://file.papertrans.cn/661/660159/660159.mp4
叢書名稱Basic Life Sciences
圖書封面Titlebook: NMR Applications in Biopolymers;  J. W. Finley,S. J. Schmidt,A. S. Serianni Book 1990 Plenum Press, New York 1990 Nucleotide.Oligosaccharid
描述Elucidating the structures of biopolymers as they exist in nature has long been a goal of biochemists and biologists. Understanding how these substances interact with themselves, other solutes, and solvents can provide useful insights into many areas of biochemistry, agriculture, food science and medicine. Knowledge of the structure of a protein or complex carbohydrate in its native form provides guidelines for the chemical or genetic modifications often desired to optimize these compounds to specific needs and applications. For example, in the pharmaceutical industry, structure-function relationships involving biopolymers are studied rou- tinely as a means to design new drugs and improve their efficacies. The tools to conduct structure investigations of biopolymers at the molecular level are limited in number. Historically X-ray crystallography has been the most attractive method to conduct studies of this type. How- ever, X-ray methods can only be applied to highly ordered, crystalline materials, thus obviating studies of solution dynamics that are often critical to attaining a global understanding of biopolymer behavior. In recent years, nuclear magnetic resonance (NMR) spectros
出版日期Book 1990
關(guān)鍵詞Nucleotide; Oligosaccharid; Oligosaccharide; biochemistry; chemistry; crystallography; food; genetic modifi
版次1
doihttps://doi.org/10.1007/978-1-4684-5868-8
isbn_softcover978-1-4684-5870-1
isbn_ebook978-1-4684-5868-8
copyrightPlenum Press, New York 1990
The information of publication is updating

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,NMR Studies of the Structure and Environment of the Milk Protein α-Lactalbumin,onformations due to multiple states of cation binding. In fact, much of the published data on the physical or structural properties of this protein previous to 1978 are ambiguous since workers were not aware that their α-LA samples contained calcium and/or other strongly bound cations.
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e substances interact with themselves, other solutes, and solvents can provide useful insights into many areas of biochemistry, agriculture, food science and medicine. Knowledge of the structure of a protein or complex carbohydrate in its native form provides guidelines for the chemical or genetic m
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Water Interactions in Bovine Casein: 2H NMR Relaxation and Small-Angle X-Ray Scattering Studies,. The major casein fraction, α., a single-chain polypeptide of 199 amino acid residues, contains 8 phosphoserine residues (Eigel et al., 1984) and a large number of hydrophobic residues; the weight-average number of phosphate groups is 6.6 per monomer.
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Book 1990es interact with themselves, other solutes, and solvents can provide useful insights into many areas of biochemistry, agriculture, food science and medicine. Knowledge of the structure of a protein or complex carbohydrate in its native form provides guidelines for the chemical or genetic modificatio
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The Structure and Behavior of the Starch Granule as Studied by NMR,normous value in elucidating structure and behavior and the results of early NMR studies in many cases echoed the conclusions derived from other techniques. However, increasingly, NMR spectroscopy is making a distinctive contribution to our understanding of the starch granule and its physical chemistry.
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