M. Akke

Publications123
h-index38
Citations5,611
Highly Influential Citations213
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Backbone dynamics of Escherichia coli ribonuclease HI: correlations with structure and function in an active enzyme.
Ribonuclease H is an endonuclease that hydrolyzes the RNA moiety of RNA-DNA duplex molecules. Escherichia coli ribonuclease H is involved in DNA replication, and retroviral ribonuclease H is… Expand
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Enzyme Dynamics During Catalysis
Internal protein dynamics are intimately connected to enzymatic catalysis. However, enzyme motions linked to substrate turnover remain largely unknown. We have studied dynamics of an enzyme during… Expand
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Global Allocation Rules for Patterns of Biomass Partitioning
A general allometric model has been derived to predict intraspecific and interspecific scaling relationships among seed plant leaf, stem, and root biomass. Analysis of a large compendium of standing… Expand
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From snapshot to movie: phi analysis of protein folding transition states taken one step further.
Kinetic anomalies in protein folding can result from changes of the kinetic ground states (D, I, and N), changes of the protein folding transition state, or both. The 102-residue protein U1A has a… Expand
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Calbindin D28k Exhibits Properties Characteristic of a Ca2+ Sensor*
Calbindin D28k is a member of the calmodulin superfamily of Ca2+-binding proteins and contains six EF-hands. The protein is generally believed to function as a Ca2+ buffer, but the studies presented… Expand
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The ribosomal stalk binds to translation factors IF2, EF-Tu, EF-G and RF3 via a conserved region of the L12 C-terminal domain.
Efficient protein synthesis in bacteria requires initiation factor 2 (IF2), elongation factors Tu (EF-Tu) and G (EF-G), and release factor 3 (RF3), each of which catalyzes a major step of translation… Expand
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Structural dynamics in the C-terminal domain of calmodulin at low calcium levels.
Calmodulin undergoes Ca2+-induced structural rearrangements that are intimately coupled to the regulation of numerous cellular processes. The C-terminal domain of calmodulin has previously been… Expand
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Protein Flexibility and Conformational Entropy in Ligand Design Targeting the Carbohydrate Recognition Domain of Galectin-3
Rational drug design is predicated on knowledge of the three-dimensional structure of the protein−ligand complex and the thermodynamics of ligand binding. Despite the fundamental importance of both… Expand
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Backbone dynamics and energetics of a calmodulin domain mutant exchanging between closed and open conformations.
Previous studies have suggested that the Ca2+-saturated E140Q mutant of the C-terminal domain of calmodulin exhibits equilibrium exchange between "open" and "closed" conformations similar to those of… Expand
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Dynamics of ribonuclease H: temperature dependence of motions on multiple time scales.
The temperature dependence of the backbone motions in Escherichia coli ribonuclease HI was studied on multiple time scales by 15N nuclear magnetic spin relaxation. Laboratory frame relaxation data at… Expand
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