N
Nils Bergenhem
Researcher at University of Michigan
Publications - 35
Citations - 761
Nils Bergenhem is an academic researcher from University of Michigan. The author has contributed to research in topics: Carbonic anhydrase & Carbonic anhydrase II. The author has an hindex of 14, co-authored 35 publications receiving 748 citations. Previous affiliations of Nils Bergenhem include OSI Pharmaceuticals & Linköping University.
Papers
More filters
Journal ArticleDOI
Isomerase and Chaperone Activity of Prolyl Isomerase in the Folding of Carbonic Anhydrase
TL;DR: Prolyl isomerase, which has been shown to accelerate rate-limiting cis-trans peptidyl-proline isomerization steps in the folding pathway, can also participate in the protein-folding process as a chaperone.
Book ChapterDOI
Carbonic anhydrase (CA)-related proteins (CA-RPs), and transmembrane proteins with CA or CA-RP domains
TL;DR: Members of the a-carbonic anhydrase (α-CA) gene family encode not only proteins that exhibit the characteristic catalytic activity of CA, but also CA-related proteins that are apparently devoid of this activity.
Journal ArticleDOI
The Catalytic Properties of Murine Carbonic Anhydrase VII
J. N. Earnhardt,Minzhang Qian,Chingkuang Tu,Maha M. Lakkis,Nils Bergenhem,P. J. Laipis,Richard E. Tashian,David N. Silverman +7 more
TL;DR: The magnitude of Kcat, its pH profile, 18O-exchange data for both wild-type and a H64A mutant, and inhibition by CuSO4 and acrolein suggest that the histidine at position 64 is functioning as a proton-transfer group and is responsible for one of the observed ionizations, which suggests a role for the amino-terminal end in enhancing proton transfer in catalysis by carbonic anhydrase.
Journal ArticleDOI
The deduced amino acid sequence of human carbonic anhydrase-related protein (CARP) is 98% identical to the mouse homologue.
TL;DR: The polymerase chain reaction (PCR) is used to amplify human CARP sequences from several cDNA libraries and the sequence has an 89.3% sequence identity with mouse CARP at the nucleotide level and 97.9% at the amino acid level.
Journal ArticleDOI
Phosphorescence reveals a continued slow annealing of the protein core following reactivation of Escherichia coli alkaline phosphatase.
TL;DR: The data suggest that the core of theprotein undergoes continued structural rearrangements affecting the rigidity of the protein environment surrounding the emitting tryptophan and the protein lability long after the return of enzyme activity.