Judy Luke
Author's posts
Jul 08 2006
The role of protein dynamics in increasing binding affinity for an engineered protein-protein interaction established by H/D exchange mass spectrometry
Horn JR, Kraybill B, Petro EJ, Coales SJ, Morrow JA, Hamuro Y, Kossiakoff AA
Biochemistry 2006 Jul;45(28):8488-98
PMID: 16834322
Abstract
It is generally accepted that protein and solvation dynamics play fundamental roles in the mechanisms of protein-protein binding; however, assessing their contribution meaningfully has not been straightforward. Here, hydrogen/deuterium exchange mass spectrometry (H/D-Ex) was employed …
May 08 2006
Crystal structure and site 1 binding energetics of human placental lactogen
Walsh ST, Kossiakoff AA
J. Mol. Biol. 2006 May;358(3):773-84
PMID: 16546209
Abstract
In primates, placental lactogen (PL) is a pituitary hormone with fundamental roles during pregnancy involving fetal growth, metabolism, and stimulating lactation in the mother. Human placental lactogen (hPL) is highly conserved with human growth hormone (hGH) and both hormones bind to the hPRLR …
Mar 08 2006
Dissecting the energetics of protein alpha-helix C-cap termination through chemical protein synthesis
Bang D, Gribenko AV, Tereshko V, Kossiakoff AA, Kent SB, Makhatadze GI
Nat. Chem. Biol. 2006 Mar;2(3):139-43
PMID: 16446709
Abstract
The alpha-helix is a fundamental protein structural motif and is frequently terminated by a glycine residue. Explanations for the predominance of glycine at the C-cap terminal portions of alpha-helices have invoked uniquely favorable energetics of …
Mar 08 2006
Structure of bistramide A-actin complex at a 1.35 angstroms resolution
Rizvi SA, Tereshko V, Kossiakoff AA, Kozmin SA
J. Am. Chem. Soc. 2006 Mar;128(12):3882-3
PMID: 16551075
Abstract
Bistramide A is a highly potent antiproliferative marine natural product from Lissoclinum bistratum. We have previously established actin as the primary cellular receptor of bistramide A. We report herein the X-ray structure of bistramide A bound to monomeric …
Jan 08 2006
The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold
Qiu Y, Tereshko V, Kim Y, Zhang R, Collart F, Yousef M, Kossiakoff A, Joachimiak A
Proteins 2006 Jan;62(1):8-16
PMID: 16287087
Abstract
The structure of Aq_328, an uncharacterized protein from hyperthermophilic bacteria Aquifex aeolicus, has been determined to 1.9 A by using multi-wavelength anomalous diffraction (MAD) phasing. Although the amino acid sequence analysis shows that …
Sep 08 2005
Alternative views of functional protein binding epitopes obtained by combinatorial shotgun scanning mutagenesis
Pál G, Fong SY, Kossiakoff AA, Sidhu SS
Protein Sci. 2005 Sep;14(9):2405-13
PMID: 16131663
Abstract
Combinatorial shotgun scanning mutagenesis was used to analyze two large, related protein binding sites to assess the specificity and importance of individual side chain contributions to binding affinity. The strategy allowed for cost-effective generation of a plethora of functional data. …
Jul 08 2005
Shotgun alanine scanning shows that growth hormone can bind productively to its receptor through a drastically minimized interface
Kouadio JL, Horn JR, Pal G, Kossiakoff AA
J. Biol. Chem. 2005 Jul;280(27):25524-32
PMID: 15857837
Abstract
The high affinity binding site (Site1) of the human growth hormone (hGH) binds to its cognate receptor (hGHR) via a concave surface patch containing about 35 residues. Using 167 sequences from a shotgun alanine scanning analysis of Site1, we …
Jun 08 2005
Total chemical synthesis and X-ray crystal structure of a protein diastereomer: [D-Gln 35]ubiquitin
Bang D, Makhatadze GI, Tereshko V, Kossiakoff AA, Kent SB
Angew. Chem. Int. Ed. Engl. 2005 Jun;44(25):3852-6
PMID: 15834850
Abstract
Apr 08 2005
Intramolecular cooperativity in a protein binding site assessed by combinatorial shotgun scanning mutagenesis
Pál G, Ultsch MH, Clark KP, Currell B, Kossiakoff AA, Sidhu SS
J. Mol. Biol. 2005 Apr;347(3):489-94
PMID: 15755445
Abstract
Combinatorial shotgun alanine-scanning was used to assess intramolecular cooperativity in the high affinity site (site 1) of human growth hormone (hGH) for binding to its receptor. A total of 19 side-chains were analyzed and statistically …
Jan 08 2005
The crystal structure of a quercetin 2,3-dioxygenase from Bacillus subtilis suggests modulation of enzyme activity by a change in the metal ion at the active site(s)
Gopal B, Madan LL, Betz SF, Kossiakoff AA
Biochemistry 2005 Jan;44(1):193-201
PMID: 15628860
Abstract
Common structural motifs, such as the cupin domains, are found in enzymes performing different biochemical functions while retaining a similar active site configuration and structural scaffold. The soil bacterium Bacillus subtilis has 20 cupin genes (0.5% of the total genome) with …