Zobrazeno 1 - 10
of 12
pro vyhledávání: '"Neena L. Summers"'
Autor:
Gunnar J. Hanson, Susan C. Howard, Michelle L. Zacheis, Christine P. Bono, Joseph K. Welply, Jennifer L. Vuletich, Louis J. Bedell, Neena L. Summers, Benjamin D. Schwartz, Susan L. Woulfe
Publikováno v:
Protein & Peptide Letters. 4:63-68
Abstract: We have synthesized a series of retro-inverso D-peptide analogues and a peptoid analog that mimic potent seven residue L-peptide ligands for DR(a. Pl*0401). The L-peptide ligands compete against binding of a 13 residue biotinylated ligand,
Publikováno v:
"Protein Engineering, Design and Selection". 8:1215-1231
A human prolactin (hPRL) model based on a 2.1 A resolution X-ray refinement of porcine growth hormone is reported. Only regions clearly defined in the growth hormone template (the four-helix bundle) or previously assumed to be involved in hPRL-recept
Autor:
Neena L. Summers, Martin Karplus
Publikováno v:
Journal of Molecular Biology. 216:991-1016
A distance-based database search scheme is proposed for modeling Pro----in non-Pro and insertion/deletion regions of homologous globular proteins up to six residues in length. In the first step, geometric descriptors, the number of residues involved
Autor:
Craig Swearingen, Francesco Sinigaglia, Robert W. Karr, Alessandro Sette, Neena L. Summers, Xin-Ting Fu, Benjamin D. Schwartz, Susan L. Woulfe, Chris P. Bono
Publikováno v:
The Journal of Experimental Medicine
To investigate the functional roles of individual HLA-DR residues in T cell recognition, transfectants expressing wild-type or mutant DR(alpha,beta 1*0401) molecules with single amino acid substitutions at 14 polymorphic positions of the DR beta 1*04
Autor:
David J. Neidhart, Louis W. Lim, Gunnar J. Hanson, Anna M. Stevens, Michael Clare, Neena L. Summers, Huey S. Shieh
Publikováno v:
Bioorganicmedicinal chemistry. 2(9)
SC-51106, a ‘minimal-size’ diol-based renin inhibitor lacking a P 4 residue, has been co-crystallized with human renin and the structure of the complex determined by X-ray crystallography. This study defines the mode of binding of this important
Publikováno v:
Biochemistry. 32(8)
The X-ray crystal structure of the copper complex of the rat trypsin mutant Arg96 to His96 (trypsin R96H) has been determined in order to ascertain the nature of the engineered metal-binding site and to understand the structural basis for the metal-i
Autor:
Neena L. Summers, Martin Karplus
Publisher Summary This chapter discusses the modeling of side chains, loops, and insertions in proteins. It describes a hybrid approach to structural modeling that combines the detection, extension, and application of statistical trends in known prot
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::e475e6b02b85da3a1f7197f4a99b7345
https://doi.org/10.1016/0076-6879(91)02011-w
https://doi.org/10.1016/0076-6879(91)02011-w
Autor:
Martin Karplus, Neena L. Summers
Publikováno v:
Journal of Molecular Biology. 210:785-811
A detailed and rule-based side-chain modelling procedure for globular proteins is presented. It uses the conformational information contained in a homologous (template) structure as a starting point and includes recipes for atom placement and for che
Publikováno v:
Journal of Molecular Biology. 196:175-198
The side-chain conformations of topologically equivalent residues in seven pairs of proteins ranging in sequence homology from 16% to 60% are compared. Both identical and mutated residues are included. For proteins with greater than 40% homology, it
Autor:
James Tyrrell, Neena L. Summers
Publikováno v:
Theoretica Chimica Acta. 47:223-231
Ab initio molecular orbital calculations employing a 4-31G basis set have been used to study the minimum energy paths for the formation of HCO+, COH+, and HCOH2+ from CO by protonation. The protonation of N2 to give NNH+ and HNNH2+ and of NO+ to form