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Fairman, Robert, Anthony-Cahill, Spencer J., DeGrado, William F. (1992) The helix-forming propensity of D-alanine in a right-handed .alpha.-helix. Journal Of The American Chemical Society, 114 (13) 5458-5459 doi:10.1021/ja00039a086

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Reference TypeJournal (article/letter/editorial)
TitleThe helix-forming propensity of D-alanine in a right-handed .alpha.-helix
JournalJournal Of The American Chemical Society
AuthorsFairman, RobertAuthor
Anthony-Cahill, Spencer J.Author
DeGrado, William F.Author
Year1992 (June)Volume114
Issue13
PublisherAmerican Chemical Society (ACS)
DOIdoi:10.1021/ja00039a086Search in ResearchGate
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Mindat Ref. ID1458712Long-form Identifiermindat:1:5:1458712:0
GUID0
Full ReferenceFairman, Robert, Anthony-Cahill, Spencer J., DeGrado, William F. (1992) The helix-forming propensity of D-alanine in a right-handed .alpha.-helix. Journal Of The American Chemical Society, 114 (13) 5458-5459 doi:10.1021/ja00039a086
Plain TextFairman, Robert, Anthony-Cahill, Spencer J., DeGrado, William F. (1992) The helix-forming propensity of D-alanine in a right-handed .alpha.-helix. Journal Of The American Chemical Society, 114 (13) 5458-5459 doi:10.1021/ja00039a086
In(1992, June) Journal Of The American Chemical Society Vol. 114 (13) American Chemical Society (ACS)

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Anthony-Cahill, S., Benfield, P., Fairman, R, Wasserman, Z., Brenner, S., Stafford, W., Altenbach, C, Hubbell, W., DeGrado, W. (1992) Molecular characterization of helix-loop-helix peptides. Science, 255 (5047). 979-983 doi:10.1126/science.1312255
Fairman, R., Beran-Steed, R. K., Anthony-Cahill, S. J., Lear, J. D., Stafford, W. F., DeGrado, W. F., Benfield, P. A., Brenner, S. L. (1993) Multiple oligomeric states regulate the DNA binding of helix-loop-helix peptides. Proceedings of the National Academy of Sciences, 90 (22) 10429-10433 doi:10.1073/pnas.90.22.10429
Osterhout, John J., Handel, Tracy, Na, George, Toumadje, Arazdordi, Long, Robert C., Connolly, Peter J., Hoch, Jeffrey C., Johnson, W. Curtis, Live, David, DeGrado, William F. (1992) Characterization of the structural properties of .alpha.1B, a peptide designed to form a four-helix bundle. Journal Of The American Chemical Society, 114 (1) 331-337 doi:10.1021/ja00027a043
Akerfeldt, Karin S., Kim, Ronald M., Camac, Daniel, Groves, John T., Lear, Jim D., DeGrado, William F. (1992) Tetraphilin: a four-helix proton channel built on a tetraphenylporphyrin framework. Journal Of The American Chemical Society, 114 (24) 9656-9657 doi:10.1021/ja00050a054
Huang, Cheng-Yen, Klemke, Jason W., Getahun, Zelleka, DeGrado, William F., Gai, Feng (2001) Temperature-Dependent Helix−Coil Transition of an Alanine Based Peptide. Journal Of The American Chemical Society, 123 (38) 9235-9238 doi:10.1021/ja0158814
Chiu, Hsien-Po, Suzuki, Yuta, Gullickson, Donald, Ahmad, Raheel, Kokona, Bashkim, Fairman, Robert, Cheng, Richard P. (2006) Helix Propensity of Highly Fluorinated Amino Acids. Journal Of The American Chemical Society, 128 (49) 15556-15557 doi:10.1021/ja0640445
Zhang, Li, Hermans, Jan (1994) 310 Helix Versus .alpha.-Helix: A Molecular Dynamics Study of Conformational Preferences of Aib and Alanine. Journal Of The American Chemical Society, 116 (26) 11915-11921 doi:10.1021/ja00105a034
Choma, Christin T., Lear, James D., Nelson, Mark J., Dutton, P. Leslie, Robertson, Dan E., DeGrado, William F. (1994) Design of a heme-binding four-helix bundle. Journal Of The American Chemical Society, 116 (3) 856-865 doi:10.1021/ja00082a005
Huang, Cheng-Yen, He, Shu, DeGrado, William F., McCafferty, Dewey G., Gai, Feng (2002) Light-Induced Helix Formation. Journal Of The American Chemical Society, 124 (43) 12674-12675 doi:10.1021/ja028084u
Ho, Siew Peng, DeGrado, William F. (1987) Design of a 4-helix bundle protein: synthesis of peptides which self-associate into a helical protein. Journal Of The American Chemical Society, 109 (22) 6751-6758 doi:10.1021/ja00256a032
Hudgins, Robert R., Jarrold, Martin F. (1999) Helix Formation in Unsolvated Alanine-Based Peptides:  Helical Monomers and Helical Dimers. Journal Of The American Chemical Society, 121 (14) 3494-3501 doi:10.1021/ja983996a
 
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