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Mechanism in Protein Chemistry

Mechanism in Protein Chemistry


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About the Book

Describes proteins' physical and chemical nature and how their molecular structures can be determined experimentally. Intended for upper level undergraduate and graduate students with a background in chemistry or biochemistry.
About the Author:

Jack Kyte, Professor Emeritus in the Chemistry Department at the University of California in San Diego, is well known for his research on the analysis of protein structure. He graduated magna cum laude from Carleton College with a degree in Chemistry. Under the tutelage of Guido Guidotti, he received his graduate degree in the Department of Biochemistry and Molecular Biology at Harvard University in Cambridge Massachusetts. Prof. Kyte joined the Department of Chemistry at the University of California at San Diego in 1974.

Prof. Kyte has had a major impact in the prediction and analysis of protein structure. He ran a laboratory investigating the structure and mechanism of sodium and potassium ATPase, an enzyme from plasma membranes responsible for active transport; acetylcholine receptor, a protein in the plasma membrane that transports cations; the receptor for epidermal growth factor, a protein in the plasma membrane that controls cellular growth; and ribonucleotide reductase, a cytoplasmic enzyme responsible for the conversion of ribonucleotides into deoxyribonucleotides. This research was funded by grants from the National Institutes of Health, the National Science Foundation, and the American Heart Association. Prof. Kyte received a Career Development Award from the National Institutes of Health, and served on the editorial board of Biochemistry for six years.


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Product Details
  • ISBN-13: 9780815317005
  • Publisher: Garland Science
  • Publisher Imprint: Garland Science
  • Height: 288 mm
  • No of Pages: 552
  • Series Title: English
  • Weight: 1626 gr
  • ISBN-10: 081531700X
  • Publisher Date: 01 Aug 1995
  • Binding: Hardback
  • Language: English
  • Returnable: N
  • Spine Width: 31 mm
  • Width: 225 mm


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