About: George D. Rose

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An Entity of Type : wikibase:Item, within Data Space : wikidata.demo.openlinksw.com associated with source document(s)

biophysicist

Attributes	Values
rdf:type	Item
description	biophysicist (en) onderzoeker (nl)
rdfs:label	George D Rose (nl) George D. Rose (en) জর্জ ডি রোজ (bn)
skos:prefLabel	George D Rose (nl) George D. Rose (en) জর্জ ডি রোজ (bn)
name	George D Rose (nl) George D. Rose (en) জর্জ ডি রোজ (bn)
given name	wds:Q90696599-008A9186-0665-44E1-9EFE-80633B65D52C
given name	George
instance of	wds:Q90696599-B1E6F892-4613-4296-906B-D58F37E30C4A
instance of	Homo sapiens
award received	wds:Q90696599-E4A5D3E2-AA58-4427-8E59-02B4739A14C4
award received	Guggenheim Fellowship
Google Scholar author ID	wds:Q90696599-7c85d50f-4c61-35f2-2f1a-cad3bf86e8e3
Guggenheim fellows ID	wds:Q90696599-81e43cd1-4aa5-1b5f-8ffb-ef771ac20874
Google Scholar author ID	mvdw03oAAAAJ
Guggenheim fellows ID	george-d-rose
skos:altLabel	Rose (en) George Rose (en) G D Rose (en) G Rose (en) G. D. Rose (en) G. Rose (en) G.D. Rose (en) George D Rose (en) Rose G. (en) Rose G. D. (en) Rose GD (en)
occupation	wds:Q90696599-CE1C9034-55BB-41D3-B0C8-78B328496595
sex or gender	wds:Q90696599-211CFB9E-B83D-47B1-95F0-814FE0058653
VIAF ID	wds:Q90696599-21f9bce8-8396-4375-add6-a1820dbde9ec
IdRef ID	wds:Q90696599-9A47DA06-ADBD-4FD8-983F-3ABE60190348
family name	wds:Q90696599-CC40E215-48C7-43DB-9B87-7E13BF56DAD1
National Library of Israel J9U ID	wds:Q90696599-14897DF9-92CA-4453-BD00-D92E4F992F5B
VIAF ID	http://viaf.org/viaf/237933510
IdRef ID	http://www.idref.fr/069296472/id
occupation	researcher
sex or gender	male
VIAF ID	237933510
IdRef ID	069296472
family name	Rose
National Library of Israel J9U ID	987007374305005171
ORCID iD	wds:Q90696599-1C997749-7951-42DB-82EB-7AF52FAFF6A2
ORCID iD	https://orcid.org/0000-0002-9185-2123
ORCID iD	0000-0002-9185-2123
is about of	https://www.wikidata.org/wiki/Special:EntityData/Q90696599
is author of	The T-to-R transformation in hemoglobin: a reevaluation Cloning, expression, and initial characterization of a novel cytokine-like gene family Helix capping Are proteins made from a limited parts list? A protein taxonomy based on secondary structure. The role of introns in repeat protein gene formation Identifying two ancient enzymes in Archaea using predicted secondary structure alignment. Helix signals in proteins Hierarchic organization of domains in globular proteins Compact units in proteins Is protein folding hierarchic? II. Folding intermediates and transition states Folding units in globular proteins Reassessing random-coil statistics in unfolded proteins Steric restrictions in protein folding: an alpha-helix cannot be followed by a contiguous beta-strand Methinks it is like a folding curve. Polyproline II structure in a sequence of seven alanine residues. Hydrophobicity of amino acid residues in globular proteins. Hydrogen bonding, hydrophobicity, packing, and protein folding Turns in peptides and proteins Secondary structure determines protein topology Physical-chemical determinants of coil conformations in globular proteins Redrawing the Ramachandran plot after inclusion of hydrogen-bonding constraints A thermodynamic definition of protein domains A physical basis for protein secondary structure A simple model for polyproline II structure in unfolded states of alanine-based peptides Prediction of chain turns in globular proteins on a hydrophobic basis Polyproline II helix is the preferred conformation for unfolded polyalanine in water. The Flory isolated-pair hypothesis is not valid for polypeptide chains: implications for protein folding Sequence determinants of the capping box, a stabilizing motif at the N-termini of alpha-helices Do all backbone polar groups in proteins form hydrogen bonds? Hydrogen bonding in globular proteins Alpha-helix-forming propensities in peptides and proteins Is protein folding hierarchic? I. Local structure and peptide folding Local interactions in protein folding: lessons from the alpha-helix Helix stop signals in proteins and peptides: the capping box Hydrophobicity of amino acid subgroups in proteins Sterics and solvation winnow accessible conformational space for unfolded proteins Hydrogen-bonded turns in proteins: the case for a recount A backbone-based theory of protein folding The Protein Coil Library: a structural database of nonhelix, nonstrand fragments derived from the PDB. LINUS: a hierarchic procedure to predict the fold of a protein. Modeling unfolded states of peptides and proteins Building native protein conformation from NMR backbone chemical shifts using Monte Carlo fragment assembly Loops in globular proteins: a novel category of secondary structure Rules for alpha-helix termination by glycine Structure and energetics of the hydrogen-bonded backbone in protein folding. Antigenic determinants in proteins coincide with surface regions accessible to large probes (antibody domains). Hydrophobic basis of packing in globular proteins A molecular mechanism for osmolyte-induced protein stability

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