Alberty is also known for his textbooks on physical chemistry, which have gone through many editions. The first one, Physical Chemistry, co-authored with Farrington Daniels, was published in 1957. More recent books of the same title have been co-authored with Robert J. Silbey and Moungi G. Bawendi (2004). Other works include Thermodynamics of Biochemical Reactions (2003) and Biochemical Thermodynamics: Applications of Mathematica (Methods of Biochemical Analysis) (2006).
He died in Cambridge, Massachusetts, at the age of 92 on January 18, 2014.[2] Towards the end of his life he wrote a short account of his life and scientific career.[3]
At the beginning of his career Alberty worked principally on aspects of electrophoresisinprotein chemistry.[4] Later he became increasingly concerned with the kinetics and mechanismsofenzyme-catalysed reactions,[5][6] initially studying fumarase in particular.[6] He was among the first to consider the kinetics of reactions with more than one substrate,[7] and in the years that followed there was hardly any aspect of enzyme kinetics he did not touch, his work including, for example, studies of pH,[8] integrated rate equations,[9] reversible reactions,[9] effects of temperature,[10] effects of buffers and inhibitors,[11] and others.
Alberty's early interest in the ionization of adenosine phosphates[12]
and of thermodynamic aspects of biochemical reactions[13] came to be his primary interest, and in his later years he had numerous publications on this topic, such as a compilation of the properties of ATP and related compounds.[14] He worked with IUPAC on recommendations for presenting data for biochemical thermodynamics.[15]
Although he was primarily concerned with single enzyme-catalysed reactions, he also did some work with systems of more than one enzyme, such as the urea cycle.[16]
^Alberty, Robert A. (2010). "Brief Scientific Autobiography of Robert A. Alberty". The Journal of Physical Chemistry B. 114 (49): 16047–16050. doi:10.1021/jp103554e. PMID21141926.
^Alberty, Robert A.; Anderson, Elmer A.; Williams, J. W. (1948). "Homogenicity and the Electrophoretic Behavior of Some Proteins". The Journal of Physical and Colloid Chemistry. 52 (1): 217–230. doi:10.1021/j150457a018. PMID18918870.
^Alberty, Robert A. (1953). "The Relationship between Michaelis Constants, Maximum Velocities and the Equilibrium Constant for an Enzyme-catalyzed Reaction". Journal of the American Chemical Society. 75 (8): 1928–1932. doi:10.1021/ja01104a045.
^ abBock, Robert M.; Alberty, Robert A. (1953). "Studies of the Enzyme Fumarase. I. Kinetics and Equilibrium". Journal of the American Chemical Society. 75 (8): 1921–1925. doi:10.1021/ja01104a043.
^Alberty, Robert A. (1958). "On the Determination of Rate Constants for Coenzyme Mechanisms1". Journal of the American Chemical Society. 80 (8): 1777–1782. doi:10.1021/ja01541a001.
^Alberty, Robert A.; Massey, Vincent (1954). "On the interpretation of the pH variation of the maximum initial velocity of an enzyme-catalyzed reaction". Biochimica et Biophysica Acta. 13 (3): 347–353. doi:10.1016/0006-3002(54)90340-6. PMID13140346.
^ abAlberty, Robert A.; Koerber, Barbara M. (1957). "Studies of the Enzyme Fumarase. VII.1 Series Solutions of Integrated Rate Equations for Irreversible and Reversible Michaelis-Menten Mechanisms2". Journal of the American Chemical Society. 79 (24): 6379–6382. doi:10.1021/ja01581a011.
^Brant, David A.; Barnett, Lewis B.; Alberty, Robert A. (1963). "The Temperature Dependence of the Steady State Kinetic Parameters of the Fumarase Reaction". Journal of the American Chemical Society. 85 (15): 2204–2209. doi:10.1021/ja00898a003.
^Alberty, Robert A.; Goldberg, Robert N. (1992). "Standard thermodynamic formation properties for the adenosine 5'-triphosphate series". Biochemistry. 31 (43): 10610–10615. doi:10.1021/bi00158a025. PMID1420176.
^Alberty, Robert A.; Cornish-Bowden, Athel; Goldberg, Robert N.; Hammes, Gordon G.; Tipton, Keith; Westerhoff, Hans V. (2011). "Recommendations for terminology and databases for biochemical thermodynamics". Biophysical Chemistry. 155 (2–3): 89–103. doi:10.1016/j.bpc.2011.03.007. PMID21501921.
