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Lehninger Principles of Biochemistry Hardcover – 1 February 2008

by Nelson (Author)
4.6 4.6 out of 5 stars 332 ratings
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This edition of the classic introduction to the fundamentals of biochemistry remains faithful to the vision of its predecessors, while embracing the tremendous advances made in biochemical research since the previous edition. It presents the fundamentals through selected topics, emphasising the most important recent developments.
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  1. Print length
    1100 pages
  2. Language
    English
  3. Publisher
    BFW Consign Print
  4. Publication date
    1 February 2008
  5. Dimensions
    22.25 x 4.53 x 27.99 cm
  6. ISBN-10
    9780716771081
  7. ISBN-13
    978-0716771081
  8. See all details
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Product details

  • ASIN ‏ : ‎ 071677108X
  • Publisher ‏ : ‎ BFW Consign Print; 5th edition (1 February 2008)
  • Language ‏ : ‎ English
  • Hardcover ‏ : ‎ 1100 pages
  • ISBN-10 ‏ : ‎ 9780716771081
  • ISBN-13 ‏ : ‎ 978-0716771081
  • Dimensions ‏ : ‎ 22.25 x 4.53 x 27.99 cm
  • Customer Reviews:
    4.6 4.6 out of 5 stars 332 ratings

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  1. Albert L. Lehninger

    Albert L. Lehninger

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    Albert Lester Lehninger (February 17, 1917 – March 4, 1986) was an American biochemist in the field of bioenergetics. He made fundamental contributions to the current understanding of metabolism at a molecular level. In 1948, he discovered, with Eugene P. Kennedy, that mitochondria are the site of oxidative phosphorylation in eukaryotes, which ushered in the modern study of energy transduction. He is the author of a number of classic texts, including: Biochemistry, The Mitochondrion, Bioenergetics and, most notably, his series Principles of Biochemistry. The latter is a widely used text for introductory biochemistry courses at the college and university levels.

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  2. Michael M. Cox

    Michael M. Cox

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  3. David L. Nelson

    David L. Nelson

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Dajana
5.0 out of 5 stars Great service !
Reviewed in Canada on 31 March 2020
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Met all expectations! Fast delivery!
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Carmina
5.0 out of 5 stars Buena elección
Reviewed in Spain on 15 January 2020
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Llegó en unas excelentes condiciones. La librería contesta a los correos con rapidez. Muy recomendable.
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Aniruddho Das
5.0 out of 5 stars Five Stars
Reviewed in India on 24 April 2016
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Best textbook on Biochemistry ever
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Julian S.
5.0 out of 5 stars Absoluter Muss für Biochemiker
Reviewed in Germany on 13 August 2014
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Das Buch wurde schnell und gut verpackt geliefert und sieht einfach super aus mit seinem schnieken Hardcover.
Der Lehninger ist ein absoluter Pflichtkauf für Biochemiker, eventuell auch für Biologen mit tiefergehendem Interesse an der Biochemie oder Mediziner, die es lieber ganz genau wissen wollen. Der Preis ist bei dem Umfang und der Tiefe gerechtfertigt. Das Buch ist zwar nicht allumfassend und vieles ist schon beim Druck wieder obsolet, das Basiswissen wird aber sehr gut aufbereitet und vermittelt.
Würde das Buch wieder kaufen!
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Austin Hudson-Lapore
5.0 out of 5 stars A great textbook, even beyond your biochemistry class
Reviewed in the United States on 1 December 2012
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I was very impressed by this book. It's a great accompaniment to an introductory biochemistry course, but it's helpful as a reference even afterwards. It isn't as jam-packed with information as, say, Alberts' Molecular Biology of the Cell. But because it's less dense, the payoff is that it's excellently written, easy to understand, and adds substantial insight beyond just outlining the pathways. It's also very aesthetically pleasing, with a good layout, a nice font, and beautifully clear diagrams.

My favorite aspect of it is that it reflects, at considerable length, upon some fundamental principles that other texts would not bother to delve into. Some of the gems, paraphrased:

-Weak, noncovalent interactions are essential to binding because several of them, fluctuating randomly in accordance with molecular-level vibrations, will be hard to break simultaneously, simply because the chance of many of these interactions all reaching a low point simultaneously is quite small. Therefore, their contribution to binding is more significant than summing their binding energies would suggest.
-The storage of sugars as starch and glycogen allows the cell to avoid having to deal with a massive amount of osmotic pressure from an equivalent number of sugar monomers.
-Most of what maintains the stability of a protein's conformation is entropic, as clustering of hydrophobic residues reduces the amount of the highly structured solvation layer of water that would have to be present around those residues in the unfolded state. The other main contribution is from internal salt bridges, which have a much higher bond energy in the interior of the protein, which has a low dieletric constant, and prevent excessive structural flexibility caused by the nonspecificity of the hydrophobic interactions. The fairly strict planarity of the peptide bond also helps limit the number of possible conformations that can be adopted. You might think that the formation of hydrogen bonds between hydrophilic residues would also contribute substantially, but because forming these bonds entails breaking an equivalent number of residue-H2O hydrogen bonds, there's basically no net difference.

Anyway, you get the idea. The textbook really strengthened my understanding, not just my knowledge. That's rather unusual, and quite praiseworthy.
9 people found this helpful
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