Bertrand Garcia-Moreno
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Explore the profile of Bertrand Garcia-Moreno including associated specialties, affiliations and a list of published articles.
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19
Citations
697
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Recent Articles
1.
Roche J, Dellarole M, Caro J, Norberto D, Garcia A, Garcia-Moreno B, et al.
J Am Chem Soc
. 2013 Aug;
135(39):14610-8.
PMID: 23987660
The time required to fold proteins usually increases significantly under conditions of high pressure. Taking advantage of this general property of proteins, we combined P-jump experiments with NMR spectroscopy to...
2.
Roche J, Dellarole M, Caro J, Guca E, Norberto D, Yang Y, et al.
Biochemistry
. 2012 Nov;
51(47):9535-46.
PMID: 23116341
The folding of staphylococcal nuclease (SNase) is known to proceed via a major intermediate in which the central OB subdomain is folded and the C-terminal helical subdomain is disordered. To...
3.
Chimenti M, Khangulov V, Robinson A, Heroux A, Majumdar A, Schlessman J, et al.
Structure
. 2012 May;
20(6):1071-85.
PMID: 22632835
Structural consequences of ionization of residues buried in the hydrophobic interior of proteins were examined systematically in 25 proteins with internal Lys residues. Crystal structures showed that the ionizable groups...
4.
Harms M, Schlessman J, Sue G, Garcia-Moreno B
Proc Natl Acad Sci U S A
. 2011 Nov;
108(47):18954-9.
PMID: 22080604
Many functionally essential ionizable groups are buried in the hydrophobic interior of proteins. A systematic study of Lys, Asp, and Glu residues at 25 internal positions in staphylococcal nuclease showed...
5.
Conformational relaxation and water penetration coupled to ionization of internal groups in proteins
Damjanovic A, Brooks B, Garcia-Moreno B
J Phys Chem A
. 2011 Mar;
115(16):4042-53.
PMID: 21428436
Molecular dynamics simulations were used to examine the effects of ionization of internal groups on the structures of eighteen variants of staphylococcal nuclease (SNase) with internal Lys, Asp, or Glu....
6.
Isom D, Castaneda C, Cannon B, Garcia-Moreno B
Proc Natl Acad Sci U S A
. 2011 Mar;
108(13):5260-5.
PMID: 21389271
Internal ionizable groups in proteins are relatively rare but they are essential for catalysis and energy transduction. To examine molecular determinants of their unusual and functionally important properties, we engineered...
7.
Schroer M, Paulus M, Jeworrek C, Krywka C, Schmacke S, Zhai Y, et al.
Biophys J
. 2010 Nov;
99(10):3430-7.
PMID: 21081092
A structural interpretation of the thermodynamic stability of proteins requires an understanding of the structural properties of the unfolded state. High-pressure small-angle x-ray scattering was used to measure the effects...
8.
Karp D, Stahley M, Garcia-Moreno B
Biochemistry
. 2010 Mar;
49(19):4138-46.
PMID: 20329780
The pK(a) values measured previously for the internal Lys-66, Asp-66, and Glu-66 in variants of a highly stable form of staphylococcal nuclease are shifted by as many as 5 pK(a)...
9.
Pey A, Rodriguez-Larrea D, Gavira J, Garcia-Moreno B, Sanchez-Ruiz J
J Am Chem Soc
. 2010 Jan;
132(4):1218-9.
PMID: 20055447
Recent work has shown that proteins can tolerate hydrophobic-to-ionizable-residue mutations. Here, we provide experimental evidence that the essential properties (pK value, protonation state, local dynamics) of buried ionizable groups in...
10.
Garcia-Moreno B
J Biol
. 2009 Dec;
8(11):98.
PMID: 20017887
Bioinformatics-based searches for correlations between subcellular localization and pI or charge distribution of proteins have failed to detect meaningful correlations. Recent work published in BMC Biology finds that a physicochemical...