Skip to main page content
Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation

Search Page

My NCBI Filters
Text availability
Article attribute
Article type
Publication date

Search Results

184 results
Filters applied: . Clear all Results are displayed in a computed author sort order. Results by year timeline is unavailable
Page 1
Insights from multiple structures of the shell proteins from the beta-carboxysome.
Tanaka S, Sawaya MR, Phillips M, Yeates TO. Tanaka S, et al. Protein Sci. 2009 Jan;18(1):108-20. doi: 10.1002/pro.14. Protein Sci. 2009. PMID: 19177356 Free PMC article.
Crystal and solution studies of the C-terminal deletion mutants demonstrate the tendency of the terminal segments to participate in protein--protein interactions, thereby providing a clue as to which side of the molecular layer of hexameric shell proteins is likely …
Crystal and solution studies of the C-terminal deletion mutants demonstrate the tendency of the terminal segments to participate in p …
The bacterial photosynthetic reaction center as a model for membrane proteins.
Rees DC, Komiya H, Yeates TO, Allen JP, Feher G. Rees DC, et al. Annu Rev Biochem. 1989;58:607-33. doi: 10.1146/annurev.bi.58.070189.003135. Annu Rev Biochem. 1989. PMID: 2673018 Review. No abstract available.
Structure of the reaction center from Rhodobacter sphaeroides R-26 and 2.4.1: symmetry relations and sequence comparisons between different species.
Komiya H, Yeates TO, Rees DC, Allen JP, Feher G. Komiya H, et al. Proc Natl Acad Sci U S A. 1988 Dec;85(23):9012-6. doi: 10.1073/pnas.85.23.9012. Proc Natl Acad Sci U S A. 1988. PMID: 3057498 Free PMC article.
The residues that are conserved in all six species are shown in relation to the structure of Rb. sphaeroides and their possible role in the function of the reaction center is discussed. A method is presented for characterizing the exposure of alpha-helices to the me …
The residues that are conserved in all six species are shown in relation to the structure of Rb. sphaeroides and their possible role …
Algorithms for evaluating the long-range accessibility of protein surfaces.
Yeates TO. Yeates TO. J Mol Biol. 1995 Jun 16;249(4):804-15. doi: 10.1006/jmbi.1995.0339. J Mol Biol. 1995. PMID: 7602592
These two measures of exposure are compared to each other as well as to the more common notion of solvent accessibility. These new procedures provide longer-range descriptions of surface geometry which may be useful in docking studies and other areas where surface c …
These two measures of exposure are compared to each other as well as to the more common notion of solvent accessibility. These …
The structure of chloroplast cytochrome c6 at 1.9 A resolution: evidence for functional oligomerization.
Kerfeld CA, Anwar HP, Interrante R, Merchant S, Yeates TO. Kerfeld CA, et al. J Mol Biol. 1995 Jul 28;250(5):627-47. doi: 10.1006/jmbi.1995.0404. J Mol Biol. 1995. PMID: 7623381
The molecular structure of cytochrome c6 from the green alga Chlamydomonas reinhardtii has been determined from two crystal forms and refined to 1.9 A resolution. ...The overall fold is similar to that of other class I c-type cytochromes, consisting of a series of a …
The molecular structure of cytochrome c6 from the green alga Chlamydomonas reinhardtii has been determined from two crystal forms and refine …
Plastocyanin: structural and functional analysis.
Redinbo MR, Yeates TO, Merchant S. Redinbo MR, et al. J Bioenerg Biomembr. 1994 Feb;26(1):49-66. doi: 10.1007/BF00763219. J Bioenerg Biomembr. 1994. PMID: 8027022 Review.
Since the determination of the structure of poplar plastocyanin in 1978, the structure of algal (Scenedesmus, Enteromorpha, Chlamydomonas) and plant (French bean) plastocyanins has been determined either by crystallographic or NMR methods, and the poplar structure has been refine …
Since the determination of the structure of poplar plastocyanin in 1978, the structure of algal (Scenedesmus, Enteromorpha, Chlamydomonas) a …
Crystallization and preliminary structural studies of neurotrophin-3.
Kelly JA, Singer E, Osslund TD, Yeates TO. Kelly JA, et al. Protein Sci. 1994 Jun;3(6):982-3. doi: 10.1002/pro.5560030614. Protein Sci. 1994. PMID: 8069227 Free PMC article.
Orthorhombic crystals, space group P2(1)2(1)2, diffracted to 2.8 A and have cell dimensions a = 39.1 A, b = 54.0 A, and c = 65.5 A. ...The tetragonal crystals diffract to 2.8 A at room temperature and 2.5 A at -100 degrees C. The unit cell dimensions change signific …
Orthorhombic crystals, space group P2(1)2(1)2, diffracted to 2.8 A and have cell dimensions a = 39.1 A, b = 54.0 A, and c = 65.5 A. . …
Verification of protein structures: patterns of nonbonded atomic interactions.
Colovos C, Yeates TO. Colovos C, et al. Protein Sci. 1993 Sep;2(9):1511-9. doi: 10.1002/pro.5560020916. Protein Sci. 1993. PMID: 8401235 Free PMC article.
Different types of atoms are distributed nonrandomly with respect to each other in proteins. Errors in model building lead to more randomized distributions of the different atom types, which can be distinguished from correct distributions by statistical methods. ... …
Different types of atoms are distributed nonrandomly with respect to each other in proteins. Errors in model building lead to
The asymmetric regions of rotation functions between Patterson functions of arbitrarily high symmetry.
Yeates TO. Yeates TO. Acta Crystallogr A. 1993 Jan 1;49 ( Pt 1):138-41. doi: 10.1107/s0108767392008110. Acta Crystallogr A. 1993. PMID: 8442929
Rotation functions between Patterson functions can be calculated and analyzed more efficiently when it is possible to consider only a unique or asymmetric region of rotation space. ...Here we describe a simple and general solution that applies to rotation functions …
Rotation functions between Patterson functions can be calculated and analyzed more efficiently when it is possible to consider only a …
184 results
Jump to page
Feedback