PMID- 11325741
OWN - NLM
STAT- MEDLINE
DCOM- 20010726
LR  - 20181113
IS  - 0006-3495 (Print)
IS  - 1542-0086 (Electronic)
IS  - 0006-3495 (Linking)
VI  - 80
IP  - 5
DP  - 2001 May
TI  - The conformation of serum albumin in solution: a combined phosphorescence 
      depolarization-hydrodynamic modeling study.
PG  - 2422-30
AB  - There is a striking disparity between the heart-shaped structure of human serum 
      albumin (HSA) observed in single crystals and the elongated ellipsoid model used 
      for decades to interpret the protein solution hydrodynamics at neutral pH. These 
      two contrasting views could be reconciled if the protein were flexible enough to 
      change its conformation in solution from that found in the crystal. To 
      investigate this possibility we recorded the rotational motions in real time of 
      an erythrosin-bovine serum albumin complex (Er-BSA) over an extended time range, 
      using phosphorescence depolarization techniques. These measurements are 
      consistent with the absence of independent motions of large protein segments in 
      solution, in the time range from nanoseconds to fractions of milliseconds, and 
      give a single rotational correlation time phi(BSA, 1 cP, 20 degrees C) = 40 +/- 2 
      ns. In addition, we report a detailed analysis of the protein hydrodynamics based 
      on two bead-modeling methods. In the first, BSA was modeled as a triangular 
      prismatic shell with optimized dimensions of 84 x 84 x 84 x 31.5 A, whereas in 
      the second, the atomic-level structure of HSA obtained from crystallographic data 
      was used to build a much more refined rough-shell model. In both cases, the 
      predicted and experimental rotational diffusion rate and other hydrodynamic 
      parameters were in good agreement. Therefore, the overall conformation in neutral 
      solution of BSA, as of HSA, should be rigid, in the sense indicated above, and 
      very similar to the heart-shaped structure observed in HSA crystals.
FAU - Ferrer, M L
AU  - Ferrer ML
AD  - Instituto Quimica-Fisica "Rocasolano", Consejo Superior de Investigaciones 
      Cientificas, 28006 Madrid, Spain.
FAU - Duchowicz, R
AU  - Duchowicz R
FAU - Carrasco, B
AU  - Carrasco B
FAU - de la Torre, J G
AU  - de la Torre JG
FAU - Acuna, A U
AU  - Acuna AU
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biophys J
JT  - Biophysical journal
JID - 0370626
RN  - 0 (Serum Albumin)
RN  - 059QF0KO0R (Water)
RN  - 27432CM55Q (Serum Albumin, Bovine)
RN  - PDC6A3C0OX (Glycerol)
RN  - PN2ZH5LOQY (Erythrosine)
SB  - IM
MH  - Animals
MH  - Biophysical Phenomena
MH  - Biophysics
MH  - Cattle
MH  - Crystallography
MH  - Erythrosine/chemistry
MH  - Glycerol/chemistry
MH  - Humans
MH  - Hydrogen-Ion Concentration
MH  - Models, Molecular
MH  - Models, Theoretical
MH  - Protein Binding
MH  - Protein Conformation
MH  - Serum Albumin/*chemistry
MH  - Serum Albumin, Bovine/chemistry
MH  - Spectrophotometry
MH  - Thermodynamics
MH  - Time Factors
MH  - Water/chemistry
PMC - PMC1301430
EDAT- 2001/04/28 10:00
MHDA- 2001/07/28 10:01
PMCR- 2002/05/01
CRDT- 2001/04/28 10:00
PHST- 2001/04/28 10:00 [pubmed]
PHST- 2001/07/28 10:01 [medline]
PHST- 2001/04/28 10:00 [entrez]
PHST- 2002/05/01 00:00 [pmc-release]
AID - S0006-3495(01)76211-X [pii]
AID - 10.1016/S0006-3495(01)76211-X [doi]
PST - ppublish
SO  - Biophys J. 2001 May;80(5):2422-30. doi: 10.1016/S0006-3495(01)76211-X.