G H Lorimer
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Explore the profile of G H Lorimer including associated specialties, affiliations and a list of published articles.
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70
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Recent Articles
1.
Thirumalai D, Lorimer G
Annu Rev Biophys Biomol Struct
. 2001 May;
30:245-69.
PMID: 11340060
Molecular chaperones are required to assist folding of a subset of proteins in Escherichia coli. We describe a conceptual framework for understanding how the GroEL-GroES system assists misfolded proteins to...
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Shtilerman M, Lorimer G, Englander S
Science
. 1999 Apr;
284(5415):822-5.
PMID: 10221918
The ability of the GroEL chaperonin to unfold a protein trapped in a misfolded condition was detected and studied by hydrogen exchange. The GroEL-induced unfolding of its substrate protein is...
5.
Horowitz P, Lorimer G, Ybarra J
Proc Natl Acad Sci U S A
. 1999 Mar;
96(6):2682-6.
PMID: 10077571
The interaction of the chaperonin GroEL14 with its cochaperonin GroES7 is dynamic, involving stable, asymmetric 1:1 complexes (GroES7.GroEL7-GroEL7) and transient, metastable symmetric 2:1 complexes [GroES7.GroEL7-GroEL7.GroES7]. The transient formation of a...
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Walter S, Lorimer G, Schmid F
Proc Natl Acad Sci U S A
. 1996 Sep;
93(18):9425-30.
PMID: 8790346
Chaperonins prevent the aggregation of partially folded or misfolded forms of a protein and, thus, keep it competent for productive folding. It was suggested that GroEL, the chaperonin of Escherichia...
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Todd M, Lorimer G, Thirumalai D
Proc Natl Acad Sci U S A
. 1996 Apr;
93(9):4030-5.
PMID: 8633011
We develop a heuristic model for chaperonin-facilitated protein folding, the iterative annealing mechanism, based on theoretical descriptions of "rugged" conformational free energy landscapes for protein folding, and on experimental evidence...
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Lorimer G
FASEB J
. 1996 Jan;
10(1):5-9.
PMID: 8566548
In vitro the chaperonin proteins, GroEL and GroES, facilitate the folding of some other proteins under conditions where that process does not occur spontaneously. Using values drawn from a number...